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Conserved domains on  [gi|546343837|gb|AGW86540|]
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sugar ABC transporter, sugar-binding protein, putative [Streptococcus suis YB51]

Protein Classification

ABC transporter substrate-binding protein( domain architecture ID 10194401)

ABC transporter substrate-binding protein functions as the initial receptor in the active transport of one or more from a variety of substrates including sugars and contains type 2 periplasmic binding fold

CATH:  3.40.190.10
Gene Ontology:  GO:0140359|GO:0042626|GO:0055052
PubMed:  26517916|24638992|25750732
TCDB:  3.A.1

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PBP2_TMBP_like cd13585
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ...
 44-414 1.13e-102

The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and similar oligosaccharides; possess type 2 periplasmic binding fold; This family includes the periplasmic trehalose/maltose-binding component of an ABC transport system and related proteins from archaea and bacteria. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


:

Pssm-ID: 270303 [Multi-domain]  Cd Length: 383  Bit Score: 310.11  E-value: 1.13e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837  44 IWDSGQ---EPGLRKIADEFEKKNPDIKINIQVSDWDSYWTMLEAGATGGSLPDTFWMHSNEIYRYGSNEMLLPLDEYLA 120
Cdd:cd13585    4 FWDWGQpaeTAALKKLIDAFEKENPGVKVEVVPVPYDDYWTKLTTAAAAGTAPDVFYVDGPWVPEFASNGALLDLDDYIE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837 121 KSEDAKlaNFPDGLNEIYNINGKQYAIPKDFDTIGLWYNKKLFDEAG-IPYPDDTWDWnkLKEVAKKLTKPDGSQYGFGA 199
Cdd:cd13585   84 KDGLDD--DFPPGLLDAGTYDGKLYGLPFDADTLVLFYNKDLFDKAGpGPKPPWTWDE--LLEAAKKLTDKKGGQYGFAL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837 200 GLS--NQEGYYNFIYQNGGKVITDDL-KSGYADPKTIEALDYYFSFVKEKISP--AITVDKERAEAFQNGQVAMSVFGSW 274
Cdd:cd13585  160 RGGsgGQTQWYPFLWSNGGDLLDEDDgKATLNSPEAVEALQFYVDLYKDGVAPssATTGGDEAVDLFASGKVAMMIDGPW 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837 275 NLSGFTaNDYIRENADVAVLPKGPDGTRATIFNGLGHAIAATTKHPDAAWKWVEYLSSKEAQ-EMQATLGVAISAYKGAA 353
Cdd:cd13585  240 ALGTLK-DSKVKFKWGVAPLPAGPGGKRASVLGGWGLAISKNSKHPEAAWKFIKFLTSKENQlKLGGAAGPAALAAAAAS 318

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 546343837 354 DTWVDSNKNFTIKNYVDMVDYAQIRPYSQTTIKWEDKAYELLKPAYLG--EKATEEAAKETAD 414
Cdd:cd13585  319 AAAPDAKPALALAAAADALAAAVPPPVPPPWPEVYPILSEALQEALLGalGKSPEEALKEAAK 381
 
Name Accession Description Interval E-value
PBP2_TMBP_like cd13585
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ...
 44-414 1.13e-102

The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and similar oligosaccharides; possess type 2 periplasmic binding fold; This family includes the periplasmic trehalose/maltose-binding component of an ABC transport system and related proteins from archaea and bacteria. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270303 [Multi-domain]  Cd Length: 383  Bit Score: 310.11  E-value: 1.13e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837  44 IWDSGQ---EPGLRKIADEFEKKNPDIKINIQVSDWDSYWTMLEAGATGGSLPDTFWMHSNEIYRYGSNEMLLPLDEYLA 120
Cdd:cd13585    4 FWDWGQpaeTAALKKLIDAFEKENPGVKVEVVPVPYDDYWTKLTTAAAAGTAPDVFYVDGPWVPEFASNGALLDLDDYIE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837 121 KSEDAKlaNFPDGLNEIYNINGKQYAIPKDFDTIGLWYNKKLFDEAG-IPYPDDTWDWnkLKEVAKKLTKPDGSQYGFGA 199
Cdd:cd13585   84 KDGLDD--DFPPGLLDAGTYDGKLYGLPFDADTLVLFYNKDLFDKAGpGPKPPWTWDE--LLEAAKKLTDKKGGQYGFAL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837 200 GLS--NQEGYYNFIYQNGGKVITDDL-KSGYADPKTIEALDYYFSFVKEKISP--AITVDKERAEAFQNGQVAMSVFGSW 274
Cdd:cd13585  160 RGGsgGQTQWYPFLWSNGGDLLDEDDgKATLNSPEAVEALQFYVDLYKDGVAPssATTGGDEAVDLFASGKVAMMIDGPW 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837 275 NLSGFTaNDYIRENADVAVLPKGPDGTRATIFNGLGHAIAATTKHPDAAWKWVEYLSSKEAQ-EMQATLGVAISAYKGAA 353
Cdd:cd13585  240 ALGTLK-DSKVKFKWGVAPLPAGPGGKRASVLGGWGLAISKNSKHPEAAWKFIKFLTSKENQlKLGGAAGPAALAAAAAS 318

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 546343837 354 DTWVDSNKNFTIKNYVDMVDYAQIRPYSQTTIKWEDKAYELLKPAYLG--EKATEEAAKETAD 414
Cdd:cd13585  319 AAAPDAKPALALAAAADALAAAVPPPVPPPWPEVYPILSEALQEALLGalGKSPEEALKEAAK 381
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
 32-338 4.20e-82

ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport and metabolism];


Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 256.51  E-value: 4.20e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837  32 GSSSGKTEISYAIWDSGQEPGLRKIADEFEKKNPDIKINIQVSDWDSYWTMLEAGATGGSLPDTFWMHSNEIYRYGSNEM 111
Cdd:COG1653   27 AAAAGKVTLTVWHTGGGEAAALEALIKEFEAEHPGIKVEVESVPYDDYRTKLLTALAAGNAPDVVQVDSGWLAEFAAAGA 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837 112 LLPLDEYLAKsEDAKLANFPDGLNEIYNINGKQYAIPKDFDTIGLWYNKKLFDEAGIPYPddtWDWNKLKEVAKKLTKPD 191
Cdd:COG1653  107 LVPLDDLLDD-DGLDKDDFLPGALDAGTYDGKLYGVPFNTDTLGLYYNKDLFEKAGLDPP---KTWDELLAAAKKLKAKD 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837 192 GsQYGFGAGLSNQEGYYNFIYQNGGKVITDDLKSGYADPKTIEALDYYFSFVKEKISPAITVDKERAEA---FQNGQVAM 268
Cdd:COG1653  183 G-VYGFALGGKDGAAWLDLLLSAGGDLYDEDGKPAFDSPEAVEALEFLKDLVKDGYVPPGALGTDWDDAraaFASGKAAM 261

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 546343837 269 SVFGSWNLSGFTANDYiRENADVAVLPKGPDG-TRATIFNGLGHAIAATTKHPDAAWKWVEYLSSKEAQEM 338
Cdd:COG1653  262 MINGSWALGALKDAAP-DFDVGVAPLPGGPGGkKPASVLGGSGLAIPKGSKNPEAAWKFLKFLTSPEAQAK 331
SBP_bac_1 pfam01547
Bacterial extracellular solute-binding protein; This family also includes the bacterial ...
 45-337 1.43e-32

Bacterial extracellular solute-binding protein; This family also includes the bacterial extracellular solute-binding protein family POTD/POTF.


Pssm-ID: 460248 [Multi-domain]  Cd Length: 294  Bit Score: 124.84  E-value: 1.43e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837   45 WDSGQEPGLRKIADEFEKKNPDIKINIQVSDWDSYWTMLEAGATGGSLP-DTFWMHSNEIYRYGSNEMLLPLDEYLAkse 123
Cdd:pfam01547   2 ASLTEAAALQALVKEFEKEHPGIKVEVESVGSGSLAQKLTTAIAAGDGPaDVFASDNDWIAELAKAGLLLPLDDYVA--- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837  124 daklanfpdglNEIYNINGKQYAIPKDFDTIGLWYNKKLFDEAGIPYPddtWDWNKLKEVAKKLTKPDGSQYGFGAGLSN 203
Cdd:pfam01547  79 -----------NYLVLGVPKLYGVPLAAETLGLIYNKDLFKKAGLDPP---KTWDELLEAAKKLKEKGKSPGGAGGGDAS 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837  204 QEGYYNFIY---QNGGKVITDDLKsGYADPKTIEALDYY-----FSFVKEKISPAITVDK---ERAEAFQNGQVAMSVFG 272
Cdd:pfam01547 145 GTLGYFTLAllaSLGGPLFDKDGG-GLDNPEAVDAITYYvdlyaKVLLLKKLKNPGVAGAdgrEALALFEQGKAAMGIVG 223

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 546343837  273 SWnlSGFTANDYIRENADVAVLPKGPDGTRATIF--------NGLGHAIAATTKHPDAAWKWVEYLSSKEAQE 337
Cdd:pfam01547 224 PW--AALAANKVKLKVAFAAPAPDPKGDVGYAPLpagkggkgGGYGLAIPKGSKNKEAAKKFLDFLTSPEAQA 294
malE PRK09474
maltose/maltodextrin ABC transporter substrate-binding protein MalE;
44-349 3.24e-07

maltose/maltodextrin ABC transporter substrate-binding protein MalE;


Pssm-ID: 236533 [Multi-domain]  Cd Length: 396  Bit Score: 51.94  E-value: 3.24e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837  44 IWDSGQE--PGLRKIADEFEKknpDIKINIQVSDWDSywtmLE-----AGATGGSlPDT-FWMHSneiyRYG---SNEML 112
Cdd:PRK09474  35 IWINGDKgyNGLAEVGKKFEK---DTGIKVTVEHPDK----LEekfpqVAATGDG-PDIiFWAHD----RFGgyaQSGLL 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837 113 LPLDEylAKSEDAKLANFP-DGLNeiynINGKQYAIPKDFDTIGLWYNKKLfdeagIPYPDDTWDW-----NKLKEVAKK 186
Cdd:PRK09474 103 AEVTP--SKAFKDKLVPFTwDAVR----YNGKLIGYPIAVEALSLIYNKDL-----VPTPPKTWEEipaldKELKAKGKS 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837 187 LTKPDGSQYGFGAGLSNQEGYYNFIYQNGGKVITDdlkSGYADPKTIEALDYYFSFVKEKISPAiTVDKERAEA-FQNGQ 265
Cdd:PRK09474 172 AIMWNLQEPYFTWPLIAADGGYAFKFENGGYDVKD---VGVNNAGAKAGLQFLVDLVKNKHMNA-DTDYSIAEAaFNKGE 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837 266 VAMSVFGSW---NL--SGFtandyireNADVAVLPKgPDGTRATIFNG-LGHAIAATTKHPDAAWKWVE-YLSSKEAQEM 338
Cdd:PRK09474 248 TAMTINGPWawsNIdkSGI--------NYGVTVLPT-FNGKPSKPFVGvLSAGINAASPNKELAKEFLEnYLLTDEGLET 318

                        330
                 ....*....|....*
gi 546343837 339 ---QATLG-VAISAY 349
Cdd:PRK09474 319 vnkDKPLGaVALKSF 333
 
Name Accession Description Interval E-value
PBP2_TMBP_like cd13585
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ...
 44-414 1.13e-102

The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and similar oligosaccharides; possess type 2 periplasmic binding fold; This family includes the periplasmic trehalose/maltose-binding component of an ABC transport system and related proteins from archaea and bacteria. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270303 [Multi-domain]  Cd Length: 383  Bit Score: 310.11  E-value: 1.13e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837  44 IWDSGQ---EPGLRKIADEFEKKNPDIKINIQVSDWDSYWTMLEAGATGGSLPDTFWMHSNEIYRYGSNEMLLPLDEYLA 120
Cdd:cd13585    4 FWDWGQpaeTAALKKLIDAFEKENPGVKVEVVPVPYDDYWTKLTTAAAAGTAPDVFYVDGPWVPEFASNGALLDLDDYIE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837 121 KSEDAKlaNFPDGLNEIYNINGKQYAIPKDFDTIGLWYNKKLFDEAG-IPYPDDTWDWnkLKEVAKKLTKPDGSQYGFGA 199
Cdd:cd13585   84 KDGLDD--DFPPGLLDAGTYDGKLYGLPFDADTLVLFYNKDLFDKAGpGPKPPWTWDE--LLEAAKKLTDKKGGQYGFAL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837 200 GLS--NQEGYYNFIYQNGGKVITDDL-KSGYADPKTIEALDYYFSFVKEKISP--AITVDKERAEAFQNGQVAMSVFGSW 274
Cdd:cd13585  160 RGGsgGQTQWYPFLWSNGGDLLDEDDgKATLNSPEAVEALQFYVDLYKDGVAPssATTGGDEAVDLFASGKVAMMIDGPW 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837 275 NLSGFTaNDYIRENADVAVLPKGPDGTRATIFNGLGHAIAATTKHPDAAWKWVEYLSSKEAQ-EMQATLGVAISAYKGAA 353
Cdd:cd13585  240 ALGTLK-DSKVKFKWGVAPLPAGPGGKRASVLGGWGLAISKNSKHPEAAWKFIKFLTSKENQlKLGGAAGPAALAAAAAS 318

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 546343837 354 DTWVDSNKNFTIKNYVDMVDYAQIRPYSQTTIKWEDKAYELLKPAYLG--EKATEEAAKETAD 414
Cdd:cd13585  319 AAAPDAKPALALAAAADALAAAVPPPVPPPWPEVYPILSEALQEALLGalGKSPEEALKEAAK 381
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
 32-338 4.20e-82

ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport and metabolism];


Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 256.51  E-value: 4.20e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837  32 GSSSGKTEISYAIWDSGQEPGLRKIADEFEKKNPDIKINIQVSDWDSYWTMLEAGATGGSLPDTFWMHSNEIYRYGSNEM 111
Cdd:COG1653   27 AAAAGKVTLTVWHTGGGEAAALEALIKEFEAEHPGIKVEVESVPYDDYRTKLLTALAAGNAPDVVQVDSGWLAEFAAAGA 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837 112 LLPLDEYLAKsEDAKLANFPDGLNEIYNINGKQYAIPKDFDTIGLWYNKKLFDEAGIPYPddtWDWNKLKEVAKKLTKPD 191
Cdd:COG1653  107 LVPLDDLLDD-DGLDKDDFLPGALDAGTYDGKLYGVPFNTDTLGLYYNKDLFEKAGLDPP---KTWDELLAAAKKLKAKD 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837 192 GsQYGFGAGLSNQEGYYNFIYQNGGKVITDDLKSGYADPKTIEALDYYFSFVKEKISPAITVDKERAEA---FQNGQVAM 268
Cdd:COG1653  183 G-VYGFALGGKDGAAWLDLLLSAGGDLYDEDGKPAFDSPEAVEALEFLKDLVKDGYVPPGALGTDWDDAraaFASGKAAM 261

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 546343837 269 SVFGSWNLSGFTANDYiRENADVAVLPKGPDG-TRATIFNGLGHAIAATTKHPDAAWKWVEYLSSKEAQEM 338
Cdd:COG1653  262 MINGSWALGALKDAAP-DFDVGVAPLPGGPGGkKPASVLGGSGLAIPKGSKNPEAAWKFLKFLTSPEAQAK 331
PBP2_UgpB cd14748
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ...
 45-414 7.71e-71

The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; possesses type 2 periplasmic binding fold; This group includes the periplasmic component of an ABC transport system specific for sn-glycerol-3-phosphate (G3P) and closely related proteins from archaea and bacteria. Under phophate starvation conditions, Escherichia coli can utilize G3P as phosphate source when exclusively imported by an ATP-binding cassette (ABC) transporter composed of the periplasmic binding protein, UgpB, the transmembrane subunits, UgpA and UgpE, and a homodimer of the nucleotide binding subunit, UgpC. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 proteins are comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270451 [Multi-domain]  Cd Length: 385  Bit Score: 227.95  E-value: 7.71e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837  45 WDSGQEPGLRKIADEFEKKNPDIKINIQVSDWDSYW-TMLEAGATGGSLPDTFWMHSNEIYRYGSNEMLLPLDEYLAKSE 123
Cdd:cd14748    8 MSGPDGKALEELVDEFNKSHPDIKVKAVYQGSYDDTlTKLLAALAAGTAPDVAQVDASWVAQLADSGALEPLDDYIDKDG 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837 124 DaKLANFPDGLNEIYNINGKQYAIPKDFDTIGLWYNKKLFDEAGIPYPDDTWDWNKLKEVAKKLTKPDG--SQYGFGAGL 201
Cdd:cd14748   88 V-DDDDFYPAALDAGTYDGKLYGLPFDTSTPVLYYNKDLFEEAGLDPEKPPKTWDELEEAAKKLKDKGGktGRYGFALPP 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837 202 SNQEG-YYNFIYQNGGKVITDDL-KSGYADPKTIEALDYYFSFV-KEKISPAITVDKERAeAFQNGQVAMSVFGSWNLSG 278
Cdd:cd14748  167 GDGGWtFQALLWQNGGDLLDEDGgKVTFNSPEGVEALEFLVDLVgKDGVSPLNDWGDAQD-AFISGKVAMTINGTWSLAG 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837 279 FTANDYiRENADVAVLPKGPDGTRATIFNGLGHAI-AATTKHPDAAWKWVEYLSSKEAQEMQATLGVAISAYKGAADT-- 355
Cdd:cd14748  246 IRDKGA-GFEYGVAPLPAGKGKKGATPAGGASLVIpKGSSKKKEAAWEFIKFLTSPENQAKWAKATGYLPVRKSAAEDpe 324

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 546343837 356 -WVDSNKNFTIknYVDMVDYAQ-IRPYSQTTIKWEDKAYELLKPAYLGEKATEEAAKETAD 414
Cdd:cd14748  325 eFLAENPNYKV--AVDQLDYAKpWGPPVPNGAEIRDELNEALEAALLGKKTPEEALKEAQE 383
PBP2_MalE cd14747
Maltose-binding protein MalE; possesses type 2 periplasmic binding fold; This group includes ...
 44-421 3.13e-60

Maltose-binding protein MalE; possesses type 2 periplasmic binding fold; This group includes the periplasmic maltose-binding component of an ABC transport system from the phytopathogen Xanthomonas citri and its related bacterial proteins. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 proteins are comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270450 [Multi-domain]  Cd Length: 386  Bit Score: 200.62  E-value: 3.13e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837  44 IW--DSGQEPGLRK-IADEFEKKNPDIKINIQVSDWDSYWTMLEAGATGGSLPDTFWMHSNEIYRYGSNEMLLPLDEYLA 120
Cdd:cd14747    4 VWamGNSAEAELLKeLADEFEKENPGIEVKVQVLPWGDAHTKITTAAASGDGPDVVQLGNTWVAEFAAMGALEDLTPYLE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837 121 KSEDAKlaNFPDGLNEIYNINGKQYAIPKDFDTIGLWYNKKLFDEAGIPYPDDTWDwnKLKEVAKKLTKPDGSQYGFG-- 198
Cdd:cd14747   84 DLGGDK--DLFPGLVDTGTVDGKYYGVPWYADTRALFYRTDLLKKAGGDEAPKTWD--ELEAAAKKIKADGPDVSGFAip 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837 199 AGLSNQEGYYNFIYQNGGKVITDDL-KSGYADPKTIEALDYYFSFVKEKISPAITVDKERA--EAFQNGQVAMSVFGSWN 275
Cdd:cd14747  160 GKNDVWHNALPFVWGAGGDLATKDKwKATLDSPEAVAGLEFYTSLYQKGLSPKSTLENSADveQAFANGKVAMIISGPWE 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837 276 LSGFT-ANDYIRENADVAVLPKGPDGTRATIFNGLGHAIAATTKHPDAAWKWVEYLSSKEAQEMQATLGVAISAYKGAAD 354
Cdd:cd14747  240 IGAIReAGPDLAGKWGVAPLPGGPGGGSPSFAGGSNLAVFKGSKNKDLAWKFIEFLSSPENQAAYAKATGMLPANTSAWD 319

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 546343837 355 TWVDSNKNFTiKNYVDMVDYAQIRPysqTTIKWE----DKAYELLKPAYLGEKATEEAAKETADMMNAELA 421
Cdd:cd14747  320 DPSLANDPLL-AVFAEQLKTGKATP---ATPEWGeieaELVLVLEEVWIGVGADVEDALDKAAAEINEILN 386
MalE COG2182
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];
44-421 7.18e-59

Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];


Pssm-ID: 441785 [Multi-domain]  Cd Length: 410  Bit Score: 197.48  E-value: 7.18e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837  44 IWDSGQE-PGLRKIADEFEKKnPDIKINIQVSDWDSYWTMLEAGATGGSLPDTFWMHSNEIYRYGSNEMLLPLDEYLAKS 122
Cdd:COG2182   43 VWVDDDEaEALEEAAAAFEEE-PGIKVKVVEVPWDDLREKLTTAAPAGKGPDVFVGAHDWLGELAEAGLLAPLDDDLADK 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837 123 EDaklanFPDGLNEIYNINGKQYAIPKDFDTIGLWYNKKLFDEagipYPDDTWDwnKLKEVAKKLTKPDgsQYGFGAGLS 202
Cdd:COG2182  122 DD-----FLPAALDAVTYDGKLYGVPYAVETLALYYNKDLVKA----EPPKTWD--ELIAAAKKLTAAG--KYGLAYDAG 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837 203 NqeGYYN--FIYQNGGKVITDDL----KSGYADPKTIEALDYYFSFVKEKISPAITVDKERAEAFQNGQVAMSVFGSWNL 276
Cdd:COG2182  189 D--AYYFypFLAAFGGYLFGKDGddpkDVGLNSPGAVAALEYLKDLIKDGVLPADADYDAADALFAEGKAAMIINGPWAA 266

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837 277 SGFTANDYIreNADVAVLPKGPDGTRATIFNG-LGHAIAATTKHPDAAWKWVEYLSSKEAQEMQATLGVAISAYKGAADT 355
Cdd:COG2182  267 ADLKKALGI--DYGVAPLPTLAGGKPAKPFVGvKGFGVSAYSKNKEAAQEFAEYLTSPEAQKALFEATGRIPANKAAAED 344

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 546343837 356 WvDSNKNFTIKNYVDMVDYAQIRPYSQTTIKWEDKAYELLKPAYLGEKATEEAAKETADMMNAELA 421
Cdd:COG2182  345 A-EVKADPLIAAFAEQAEYAVPMPNIPEMGAVWTPLGTALQAIASGKADPAEALDAAQKQIEAAIA 409
PBP2_XBP1_like cd14749
The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; ...
 44-418 7.77e-54

The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; possesses type 2 periplasmic binding fold; This group represents the periplasmic component of an ABC transport system XBP1 that shows preference for xylo-oligosaccharides in the order of xylotriose > xylobiose > xylotetraose. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 proteins are comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270452 [Multi-domain]  Cd Length: 388  Bit Score: 183.74  E-value: 7.77e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837  44 IWDSGQEPGLRKIADE----FEKKNPDIKINIQVSDWDSYWTMLEAGATGGSLPDTFWMHS-NEIYRYGSNEMLLPLDEY 118
Cdd:cd14749    4 YWQYFTGDTKKKYMDEliadFEKENPNIKVKVVVFPYDNYKTKLKTAVAAGEGPDVFNLWPgGWLAEFVKAGLLLPLTDY 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837 119 LakSEDAKLANFPDGLNEIYNINGKQYAIPKDFDTIGLWYNKKLFDEAGIPYPDDTWDwnKLKEVAKKLTKPDGSQYGFG 198
Cdd:cd14749   84 L--DPNGVDKRFLPGLADAVTFNGKVYGIPFAARALALFYNKDLFEEAGGVKPPKTWD--ELIEAAKKDKFKAKGQTGFG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837 199 AGLSNQEG---YYNFIYQNGGKVITDDLKSG--YADPKTIEALDYYFSFVKEKISPAITVDKERAE---AFQNGQVAMSV 270
Cdd:cd14749  160 LLLGAQGGhwyFQYLVRQAGGGPLSDDGSGKatFNDPAFVQALQKLQDLVKAGAFQEGFEGIDYDDagqAFAQGKAAMNI 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837 271 FGSWNLSGFTaNDYIRENADVAVLPKGPDG--TRATIFNGLGHAIAATTKHPDAAWKWVEYLSSKEAQeMQATLGVAISA 348
Cdd:cd14749  240 GGSWDLGAIK-AGEPGGKIGVFPFPTVGKGaqTSTIGGSDWAIAISANGKKKEAAVKFLKYLTSPEVM-KQYLEDVGLLP 317

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 546343837 349 YKGAADTWVDSNKNFTIKNYVDMVDYAQIRPYSQTTikWEDKAYELLKP---AYLGEKATEEAAKETADMMNA 418
Cdd:cd14749  318 AKEVVAKDEDPDPVAILGPFADVLNAAGSTPFLDEY--WPAAAQVHKDAvqkLLTGKIDPEQVVKQAQSAAAK 388
PBP2_GacH cd14751
The periplasmic-binding component of the putative oligosacchride ABC transporter GacHFG; ...
 55-417 3.20e-52

The periplasmic-binding component of the putative oligosacchride ABC transporter GacHFG; possesses type 2 periplasmic binding fold; This group represents the periplasmic component GacH of an ABC import system. GacH is identified as a maltose/maltodextrin-binding protein with a low affinity for acarbose. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 proteins are comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270454 [Multi-domain]  Cd Length: 376  Bit Score: 179.11  E-value: 3.20e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837  55 KIADEFEKKNPDIKINIQVSDWDSYWTMLEAGATGGSLPDTFWMHSNEIYRYGSNEMLLPLDEYLAkSEDAKlANFPDGL 134
Cdd:cd14751   18 KLIPAFEKEYPKIKVKAVRVPFDGLHNQIKTAAAGGQAPDVMRADIAWVPEFAKLGYLQPLDGTPA-FDDIV-DYLPGPM 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837 135 NEIYnINGKQYAIPKDFDTIGLWYNKKLFDEAGIPYPdDTWDwnKLKEVAKKLTKPDGsQYGFgaGLSNQEGYY--NFIY 212
Cdd:cd14751   96 ETNR-YNGHYYGVPQVTNTLALFYNKRLLEEAGTEVP-KTMD--ELVAAAKAIKKKKG-RYGL--YISGDGPYWllPFLW 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837 213 QNGGKVITDDLKSGY-ADPKTIEALDYYFSFVKEK-ISPAITVDKERA-EAFQNGQVAMSVFGSWNLS--GFTANDYIRE 287
Cdd:cd14751  169 SFGGDLTDEKKATGYlNSPESVRALETIVDLYDEGaITPCASGGYPNMqDGFKSGRYAMIVNGPWAYAdiLGGKEFKDPD 248

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837 288 NADVAVLPKGPDGTRATIfNGLGHAIAATTKHPDAAWKWVEYLSSKEAQEMQA----TLGVAISAYKGAADTwvdsnKNF 363
Cdd:cd14751  249 NLGIAPVPAGPGGSGSPV-GGEDLVIFKGSKNKDAAWKFVKFMSSAEAQALTAaklgLLPTRTSAYESPEVA-----NNP 322

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 546343837 364 TIKNYVDMVDYAQIRPysqTTIKWEdKAYELLKPAY----LGEKATEEAAKETADMMN 417
Cdd:cd14751  323 MVAAFKPALETAVPRP---PIPEWG-ELFEPLTLAFakvlRGEKSPREALDEAAKQWD 376
PBP2_TMBP cd14750
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose; ...
 39-414 2.64e-45

The periplasmic-binding component of ABC transport systems specific for trehalose/maltose; possesses type 2 periplasmic binding fold; This group represents the periplasmic trehalose/maltose-binding component of an ABC transport system and related proteins from archaea and bacteria. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 proteins are comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270453 [Multi-domain]  Cd Length: 385  Bit Score: 161.31  E-value: 2.64e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837  39 EISYAIWDSGQEPG-LRKIADEFEKKNPDIKINIQ--VSDWDS----YWTMLEAGATGGSL--PDTFWmhSNEIYRYGsn 109
Cdd:cd14750    1 TITFAAGSDGQEGElLKKAIAAFEKKHPDIKVEIEelPASSDDqrqqLVTALAAGSSAPDVlgLDVIW--IPEFAEAG-- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837 110 eMLLPLDEYLAKSEDAKlanFPDGLNEIYNINGKQYAIPKDFDTIGLWYNKKLFDEAGIPYPDdTWDwnKLKEVAKKLTK 189
Cdd:cd14750   77 -WLLPLTEYLKEEEDDD---FLPATVEANTYDGKLYALPWFTDAGLLYYRKDLLEKYGPEPPK-TWD--ELLEAAKKRKA 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837 190 PDGSQYGFGAGLSNQEG----YYNFIYQNGGKVITDDL-KSGYADPKTIEALDYYFSFVKEKISPA-ITVDKERA--EAF 261
Cdd:cd14750  150 GEPGIWGYVFQGKQYEGlvcnFLELLWSNGGDIFDDDSgKVTVDSPEALEALQFLRDLIGEGISPKgVLTYGEEEarAAF 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837 262 QNGQVAMSvfGSWNLSGFTANDYIRENAD---VAVLPKGPDGTRATIFNGLGHAIAATTKHPDAAWKWVEYLSSKEAQEM 338
Cdd:cd14750  230 QAGKAAFM--RNWPYAYALLQGPESAVAGkvgVAPLPAGPGGGSASTLGGWNLAISANSKHKEAAWEFVKFLTSPEVQKR 307

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837 339 QATLGVAISAYKGAADTWVDSNKNFTIKNYVDMVDYAQIRP----YSQTtikwEDKAYELLKPAYLGEKATEEAAKETAD 414
Cdd:cd14750  308 RAINGGLPPTRRALYDDPEVLEAYPFLPALLEALENAVPRPvtpkYPEV----STAIQIALSAALSGQATPEEALKQAQE 383
PBP2_Maltose_binding_like cd13586
The periplasmic-binding component of ABC transport systems specific for maltose and related ...
 39-379 1.41e-32

The periplasmic-binding component of ABC transport systems specific for maltose and related polysaccharides; possess type 2 periplasmic binding fold; This subfamily represents the periplasmic binding component of ABC transport systems involved in uptake of polysaccharides including maltose, maltodextrin, and cyclodextrin. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270304 [Multi-domain]  Cd Length: 367  Bit Score: 126.26  E-value: 1.41e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837  39 EISYAIWDSGQEPGLRKIADEFEKKNpDIKINIQVSDWDSYWTMLEAGATGGSLPDTFWMHSNEIYRYGSNEMLLPLDEY 118
Cdd:cd13586    1 TITVWTDEDGELEYLKELAEEFEKKY-GIKVEVVYVDSGDTREKFITAGPAGKGPDVFFGPHDWLGELAAAGLLAPIPEY 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837 119 LAKSEDAkLANFPDGLNeiynINGKQYAIPKDFDTIGLWYNKKLfdeagIPYPDDTWDwnKLKEVAKKLTKPDGSQYGFG 198
Cdd:cd13586   80 LAVKIKN-LPVALAAVT----YNGKLYGVPVSVETIALFYNKDL-----VPEPPKTWE--ELIALAKKFNDKAGGKYGFA 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837 199 AGLsnQEGYYNFIYQ--NGGKVITDDLK----SGYADPKTIEALDYYFSFV-KEKISPAITVDKERAEAFQNGQVAMSVF 271
Cdd:cd13586  148 YDQ--TNPYFSYPFLaaFGGYVFGENGGdptdIGLNNEGAVKGLKFIKDLKkKYKVLPPDLDYDIADALFKEGKAAMIIN 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837 272 GSWNLSGFTANDYireNADVAVLPKGPDGTRATIFNG-LGHAIAATTKHPDAAWKWVEYLSSKEAQEMQATLGVAISAYK 350
Cdd:cd13586  226 GPWDLADYKDAGI---NFGVAPLPTLPGGKQAAPFVGvQGAFVSAYSKNKEAAVEFAEYLTSDEAQLLLFEKTGRIPALK 302

                        330       340
                 ....*....|....*....|....*....
gi 546343837 351 GAADTWVDSNkNFTIKNYVDMVDYAQIRP 379
Cdd:cd13586  303 DALNDAAVKN-DPLVKAFAEQAQYGVPMP 330
SBP_bac_1 pfam01547
Bacterial extracellular solute-binding protein; This family also includes the bacterial ...
 45-337 1.43e-32

Bacterial extracellular solute-binding protein; This family also includes the bacterial extracellular solute-binding protein family POTD/POTF.


Pssm-ID: 460248 [Multi-domain]  Cd Length: 294  Bit Score: 124.84  E-value: 1.43e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837   45 WDSGQEPGLRKIADEFEKKNPDIKINIQVSDWDSYWTMLEAGATGGSLP-DTFWMHSNEIYRYGSNEMLLPLDEYLAkse 123
Cdd:pfam01547   2 ASLTEAAALQALVKEFEKEHPGIKVEVESVGSGSLAQKLTTAIAAGDGPaDVFASDNDWIAELAKAGLLLPLDDYVA--- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837  124 daklanfpdglNEIYNINGKQYAIPKDFDTIGLWYNKKLFDEAGIPYPddtWDWNKLKEVAKKLTKPDGSQYGFGAGLSN 203
Cdd:pfam01547  79 -----------NYLVLGVPKLYGVPLAAETLGLIYNKDLFKKAGLDPP---KTWDELLEAAKKLKEKGKSPGGAGGGDAS 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837  204 QEGYYNFIY---QNGGKVITDDLKsGYADPKTIEALDYY-----FSFVKEKISPAITVDK---ERAEAFQNGQVAMSVFG 272
Cdd:pfam01547 145 GTLGYFTLAllaSLGGPLFDKDGG-GLDNPEAVDAITYYvdlyaKVLLLKKLKNPGVAGAdgrEALALFEQGKAAMGIVG 223

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 546343837  273 SWnlSGFTANDYIRENADVAVLPKGPDGTRATIF--------NGLGHAIAATTKHPDAAWKWVEYLSSKEAQE 337
Cdd:pfam01547 224 PW--AALAANKVKLKVAFAAPAPDPKGDVGYAPLpagkggkgGGYGLAIPKGSKNKEAAKKFLDFLTSPEAQA 294
PBP2_CMBP cd13658
The periplasmic binding component of ABC transport systems specific for cyclo/maltodextrin; ...
 44-336 1.18e-30

The periplasmic binding component of ABC transport systems specific for cyclo/maltodextrin; possess the type 2 periplasmic binding fold; This group includes the periplasmic cyclo/maltodextrin-binding protein of Thermoactinomyces vulgaris ATP-binding cassette transporter and related proteins. Cyclodextrins are a family of compounds composed of glucose units connected by 1, 4 glycosidic linkages to form a series of oligosaccharide rings, and their cavity is hydrophibic which allows cyclodextrins to accomodate hydrophobic molecules/moieties in the cavity. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270376 [Multi-domain]  Cd Length: 372  Bit Score: 121.05  E-value: 1.18e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837  44 IWDSG--QEPGLRKIADEFEKKNpDIKINIQVSDWDSYWTMLEAGATGGSLPDTFWMHSNEIYRYGSNEMLLPLdeylaK 121
Cdd:cd13658    4 VWVDEdkKMAFIKKIAKQYTKKT-GVKVKLVEVDQLDQLEKLSLDGPAGKGPDVMVAPHDRIGSAVLQGLLSPI-----K 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837 122 SEDAKLANFPDGLNEIYNINGKQYAIPKDFDTIGLWYNKKLFDEAgipyPDDTWDWNKLkevAKKLTKPDGSQYGFGAGL 201
Cdd:cd13658   78 LSKDKKKGFTDQALKALTYDGKLYGLPAAVETLALYYNKDLVKNA----PKTFDELEAL---AKDLTKEKGKQYGFLADA 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837 202 SNQEGYYNFIYQNGGKVITDDLKS------GYADPKTIEALDYYFSFVKEKISPAITVDKERAEAFQNGQVAMSVFGSWN 275
Cdd:cd13658  151 TNFYYSYGLLAGNGGYIFKKNGSDldindiGLNSPGAVKAVKFLKKWYTEGYLPKGMTGDVIQGLFKEGKAAAVIDGPWA 230

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 546343837 276 LSGFTAndyIRENADVAVLPKGPDGTRATIFNGL-GHAIAATTKHPDAAWKWVEYLSSKEAQ 336
Cdd:cd13658  231 IQEYQE---AGVNYGVAPLPTLPNGKPMAPFLGVkGWYLSAYSKHKEWAQKFMEFLTSKENL 289
PBP2_ABC_oligosaccharides cd13522
The periplasmic-binding component of ABC transport systems specific for maltose and related ...
 40-413 4.64e-30

The periplasmic-binding component of ABC transport systems specific for maltose and related oligosaccharides; possess type 2 periplasmic binding fold; This family represents the periplasmic binding component of ABC transport systems involved in uptake of oligosaccharides including maltose, trehalose, maltodextrin, and cyclodextrin. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270240 [Multi-domain]  Cd Length: 368  Bit Score: 119.44  E-value: 4.64e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837  40 ISYAIW-DSGQEPGLRKIADEFEKKNPDIKINIQVSDWDSYWTMLEAGATGGSLPDTFWMHSNEIYRYGSNEMLLPLDEY 118
Cdd:cd13522    2 ITVWHQyDTGENQAVNELIAKFEKAYPGITVEVTYQDTEARRQFFSTAAAGGKGPDVVFGPSDSLGPFAAAGLLAPLDEY 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837 119 LAKSEDaklaNFPDGLNEIyNINGKQYAIPKDFDTIGLWYNKKLFdeagIPYPDDTWDwnKLKEVAKKLTKPDGSQYGFG 198
Cdd:cd13522   82 VSKSGK----YAPNTIAAM-KLNGKLYGVPVSVGAHLMYYNKKLV----PKNPPKTWQ--ELIALAQGLKAKNVWGLVYN 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837 199 AGlsnqEGYYN--FIYQNGGKVITDDL---KSGYADPKTIEALDYYFSFV-KEKISPAITVDKERAEAFQNGQVAMSVFG 272
Cdd:cd13522  151 QN----EPYFFaaWIGGFGGQVFKANNgknNPTLDTPGAVEALQFLVDLKsKYKIMPPETDYSIADALFKAGKAAMIING 226

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837 273 SWNLSGFTANDYIreNADVAVLPKGPDGTRATIF-NGLGHAIAATTKHPDAAWKWVEYLSSKEAQEMQA-TLGVA---IS 347
Cdd:cd13522  227 PWDLGDYRQALKI--NLGVAPLPTFSGTKHAAPFvGGKGFGINKESQNKAAAVEFVKYLTSYQAQLVLFdDAGDIpanLQ 304

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 546343837 348 AYKGAAdtwvdSNKNFTIKNYVDMVDYAQIRP-YSQTTIKWEdkAYELLKPAYLGEKATEEAAKETA 413
Cdd:cd13522  305 AYESPA-----VQNKPAQKASAEQAAYGVPMPnIPEMRAVWD--AFRIAVNSVLAGKVTPEAAAKDA 364
PBP2_Maltodextrin cd13657
The periplasmic binding component of ABC transport system specific for maltodextrin; This ...
 45-354 5.82e-26

The periplasmic binding component of ABC transport system specific for maltodextrin; This group includes the periplasmic maltodextrin-binding protein of a binding protein-dependent ATP-binding cassette transporter. Maltodextrin is a polysaccharide that is used as a food addtive and can be enzymatically produced from any starch . Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270375 [Multi-domain]  Cd Length: 368  Bit Score: 107.85  E-value: 5.82e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837  45 WDSGQEPGLRKIADEFEKKNPDIKINIQVSDWDSYWTMLEAGATGGSLPDTFWMHSNEIYRYGSNEMLLPLDEYLAkseD 124
Cdd:cd13657    8 LTGAEEDALQQIIDEFEAKYPVPNVKVPFEKKPDLQNKLLTAIPAGEGPDLFIWAHDWIGQFAEAGLLVPISDYLS---E 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837 125 AKLANFPDGLNEIYNINGKQYAIPKDFDTIGLWYNKKLFDEagipyPDDTWDwnKLKEVAKKLTKPDGSQYGFGAGLSNQ 204
Cdd:cd13657   85 DDFENYLPTAVEAVTYKGKVYGLPEAYETVALIYNKALVDQ-----PPETTD--ELLAIMKDHTDPAAGSYGLAYQVSDA 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837 205 EGYYNFIYQNGGKVITDD-LKSGYADPKTIEALDYYFSFVKEKISPAITVDKERAeAFQNGQVAMSVFGSWNLSGFTAN- 282
Cdd:cd13657  158 YFVSAWIFGFGGYYFDDEtDKPGLDTPETIKGIQFLKDFSWPYMPSDPSYNTQTS-LFNEGKAAMIINGPWFIGGIKAAg 236

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 546343837 283 -DYirenaDVAVLPKGPDGTRATIFNG---LGHAIAATTKHPDAAWKWVEYLSSKEAQEMQATLGVAISAYKGAAD 354
Cdd:cd13657  237 iDL-----GVAPLPTVDGTNPPRPYSGvegIYVTKYAERKNKEAALDFAKFFTTAEASKILADENGYVPAATNAYD 307
SBP_bac_8 pfam13416
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 55-355 2.91e-22

Bacterial extracellular solute-binding protein; This family includes bacterial extracellular solute-binding proteins.


Pssm-ID: 433189 [Multi-domain]  Cd Length: 281  Bit Score: 95.94  E-value: 2.91e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837   55 KIADEFEKKNpDIKINIQVSDWDSYWTMLEAGATGGSLPD--TFWMHSNEIYRYGSNEMLLPLDEYLAksedakLANFPD 132
Cdd:pfam13416   1 ALAKAFEKKT-GVTVEVEPQASNDLQAKLLAAAAAGNAPDldVVWIAADQLATLAEAGLLADLSDVDN------LDDLPD 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837  133 GLNEiYNINGKQYAIPKDFDT-IGLWYNKKLFDEAGipypDDTWDWNKLKEVAKKLTKpdgsQYGFGAglsNQEGYYNFI 211
Cdd:pfam13416  74 ALDA-AGYDGKLYGVPYAASTpTVLYYNKDLLKKAG----EDPKTWDELLAAAAKLKG----KTGLTD---PATGWLLWA 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837  212 YQNGGKVITDDLKsgyADPKTIEALDYYFSFVKEKISPAITVDKerAEAFQNGQVAMSVFGSWNLSGFTANDYirenaDV 291
Cdd:pfam13416 142 LLADGVDLTDDGK---GVEALDEALAYLKKLKDNGKVYNTGADA--VQLFANGEVAMTVNGTWAAAAAKKAGK-----KL 211

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 546343837  292 AVLPKGPdgtrATIFNGLGHAIAATTKHPD-AAWKWVEYLSSKEAQEMQATLGVAISAYKGAADT 355
Cdd:pfam13416 212 GAVVPKD----GSFLGGKGLVVPAGAKDPRlAALDFIKFLTSPENQAALAEDTGYIPANKSAALS 272
PotD COG0687
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism];
56-354 2.19e-17

Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism];


Pssm-ID: 440451 [Multi-domain]  Cd Length: 348  Bit Score: 82.65  E-value: 2.19e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837  56 IADEFEKKNpDIKINIQVSD-WDSYWTMLEAGATGgslPDTFWMHSNEIYRYGSNEMLLPLDeylaKSEDAKLANFPDGL 134
Cdd:COG0687   44 VLEPFEKET-GIKVVYDTYDsNEEMLAKLRAGGSG---YDVVVPSDYFVARLIKAGLLQPLD----KSKLPNLANLDPRF 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837 135 NEIYNINGKQYAIPKDFDTIGLWYNKKLFDEagipyPDDTWD--WNklKEVAKKLTKPDGSQYGFGAGLsnqegyynfiY 212
Cdd:COG0687  116 KDPPFDPGNVYGVPYTWGTTGIAYNTDKVKE-----PPTSWAdlWD--PEYKGKVALLDDPREVLGAAL----------L 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837 213 QNGGKVITddlksgyADPKTIEALdyyFSFVKEkISPAITV----DKERAEAFQNGQVAMSVfgSWNLSGFTANDyirEN 288
Cdd:COG0687  179 YLGYDPNS-------TDPADLDAA---FELLIE-LKPNVRAfwsdGAEYIQLLASGEVDLAV--GWSGDALALRA---EG 242

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 546343837 289 ADVA-VLPKgpDGTRATIFNglgHAIAATTKHPDAAWKWVEYLSSKEAQEMQATLGVAISAYKGAAD 354
Cdd:COG0687  243 PPIAyVIPK--EGALLWFDN---MAIPKGAPNPDLAYAFINFMLSPEVAAALAEYVGYAPPNKAARE 304
PBP2_AlgQ_like_1 cd13580
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 51-419 5.85e-17

Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 periplasmic binding fold; This subgroup includes uncharacterized periplasmic-binding proteins that are closely related to high molecular weight (HMW) alginate bining proteins (AlgQ1 and AlgQ2) found in gram-negative soil bacteria. The HMW alginate uptake system is composed of a novel pit formed on the cell surface and a pit-dependent ATP-binding cassette (ABC) transporter in the inner membrane. The transportation of HMW alginate from the pit to the ABC transporter is mediated by periplasmic HMW alginate-binding proteins (AlgQ1 and AlgQ2). Alginate is an anionic polysaccharide that is made up of alpha-L-mannuronate and its 5'-epimer, alpha-L-guluronate. Alginate is present in the cell walls of brown seaweeds, where it forms a viscous gum by binding water. Alginate is also produced by two bacteria genera Pseudomonas and Azotobacter. AlgQ1 and AlgQ2 belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. However, unlike other bacterial periplasmic-binding proteins that deliver small solutes to ABC transporters, AlgQ1/2 can bind a macromolecule and may have specificity for either sugar or a certain type of polysaccharide.


Pssm-ID: 270298 [Multi-domain]  Cd Length: 471  Bit Score: 82.38  E-value: 5.85e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837  51 PGLRKIADEFEkknpdIKINIQVSDWDSYWTMLEAGATGGSLPDTFWMHS-NEIYRYGSNEMLLPLDEYLAKSEDAKLAN 129
Cdd:cd13580   23 PYTKYLEEKTN-----IDVKVKWVPDSSYDEKLNLALASGDLPDIVVVNDpQLSITLVKQGALWDLTDYLDKYYPNLKKI 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837 130 FPDGLNEIYNINGKQYAIPK---DFDTIGLWYNKKLFDEAGIPYPdDTWDwnKLKEVAKKLTK--PDG-----------S 193
Cdd:cd13580   98 IEQEGWDSASVDGKIYGIPRkrpLIGRNGLWIRKDWLDKLGLEVP-KTLD--ELYEVAKAFTEkdPDGngkkdtygltdT 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837 194 QYGFGAGLSNQEGYY-----NFIYQNGGKVITDDLksgyaDPKTIEALDYYFSFVKEK-ISPA-ITVDKERA-EAFQNGQ 265
Cdd:cd13580  175 KDLIGSGFTGLFGAFgappnNWWKDEDGKLVPGSI-----QPEMKEALKFLKKLYKEGlIDPEfAVNDGTKAnEKFISGK 249

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837 266 VAMSV----FGSWNLSGFTANDyirENADVAVL--PKGPDGTR---ATIFNGLGHAIAATTKHPDAAWKWVEYLSSKEAQ 336
Cdd:cd13580  250 AGIFVgnwwDPAWPQASLKKND---PDAEWVAVpiPSGPDGKYgvwAESGVNGFFVIPKKSKKPEAILKLLDFLSDPEVQ 326

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837 337 EMqATLGVAISAYkgaadtWVDSNKNFTIKNYVDMVDYAQIRPYSQTTIKWED-KAYELLKPAYLGEKATEEAAKETADM 415
Cdd:cd13580  327 KL-LDYGIEGVHY------TVKDGGPVNIIPPDKQEVGDATLDYFQGSLALEKyKLTNNGERKSDAKKEALDERVVNAND 399


                 ....
gi 546343837 416 MNAE 419
Cdd:cd13580  400 EENE 403
PBP2_polyamine_RpCGA009 cd13589
The periplasmic-binding component of an uncharacterized ABC transport system from ...
 45-343 1.17e-13

The periplasmic-binding component of an uncharacterized ABC transport system from Rhodopseudomonas palustris CGA009 and related proteins; contains the type 2 periplasmic-binding fold; This group represents the periplasmic binding domain that serves as the primary high-affinity receptor of an uncharacterized ABC-type polyamine transporter from Rhodopseudomonas palustris Cga009 and related proteins from other bacteria. Polyamine transport plays an essential role in the regulation of intracellular polyamine levels which are known to be elevated in rapidly proliferating cells and tumors. Natural polyamines are putrescine, spermindine, and spermine. They are polycations that play multiple roles in cell growth, survival and proliferation, and plant stress and disease resistance. They can interact with negatively charged molecules, such as nucleic acids, to modulate their functions. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270307 [Multi-domain]  Cd Length: 268  Bit Score: 70.72  E-value: 1.17e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837  45 WDSGQEPGLRK-IADEFEKKNPdIKINIQVSDWDSYWTMLEAGAtGGSLPDTFWMHSNEIYRYGSNEMLLPLDEylakse 123
Cdd:cd13589    7 WGGSYEDAQRKaVIEPFEKETG-IKVVYDTGTSADRLAKLQAQA-GNPQWDVVDLDDGDAARAIAEGLLEPLDY------ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837 124 dAKLANFPDglNEIYNINGKQYAIPKDFDTIGLWYNKKLFDEAgipyPDDTWDWNKlkEVAKKLTKPDGSQYGFGAGLsn 203
Cdd:cd13589   79 -SKIPNAAK--DKAPAALKTGYGVGYTLYSTGIAYNTDKFKEP----PTSWWLADF--WDVGKFPGPRILNTSGLALL-- 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837 204 qegyYNFIYQNGGKVITDDLKSGYAdpktieALDyyfsfvkeKISPAITVDKER----AEAFQNGQVAMSVFGSwnlsgF 279
Cdd:cd13589  148 ----EAALLADGVDPYPLDVDRAFA------KLK--------ELKPNVVTWWTSgaqlAQLLQSGEVDMAPAWN-----G 204

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 546343837 280 TANDYIRENADVA-VLPKGpdGTRATIfNGLghAIAATTKHPDAAWKWVEYLSSKEAQEMQATLG 343
Cdd:cd13589  205 RAQALIDAGAPVAfVWPKE--GAILGP-DTL--AIVKGAPNKELAMKFINFALSPEVQAALAEAL 264
PBP2_AlgQ_like cd13521
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 56-373 3.90e-13

Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 periplasmic binding fold; This family represents the periplasmic-binding component of high molecular weight (HMW) alginate uptake system found in gram-negative soil bacteria and related proteins. The HMW alginate uptake system is composed of a novel pit formed on the cell surface and a pit-dependent ATP-binding cassette (ABC) transporter in the inner membrane. In Sphingomonas sp. A1, the transportation of HMW alginate from the pit to the ABC transporter is mediated by periplasmic HMW alginate-binding proteins AlgQ1 and AlgQ2. Alginate is an anionic polysaccharide that is made up of alpha-L-mannuronate and its 5'-epimer, alpha-L-guluronate. Alginate is present in the cell walls of brown seaweeds, where it forms a viscous gum by binding water. Alginate is also produced by two bacteria genera Pseudomonas and Azotobacter. AlgQ1 and AlgQ2 belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. However, unlike other bacterial periplasmic-binding proteins that deliver small solutes to ABC transporters, AlgQ1/2 can bind a macromolecule and may have specificity for either sugar or a certain type of polysaccharide.


Pssm-ID: 270239 [Multi-domain]  Cd Length: 483  Bit Score: 70.95  E-value: 3.90e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837  56 IADEFEKKNpDIKINIQVSDWDSYWTMLEAGATGGSLPD----TFWmhSNEIYRYGSNEMLLPLDEYLAKSED--AKLAN 129
Cdd:cd13521   22 VAKEIEKLT-NVKLEIVAVTAATSQQKLNLMLASGDLPDivgaDYL--KDKFIAYGMEGAFLPLSKYIDQYPNlkAFFKQ 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837 130 FPDGLNEIYNINGKQYAIP----KDFDTIGLWYNKKLFDEAGIPYPDdTWDwnKLKEVAKKLTKPDGSQYG----FGAGL 201
Cdd:cd13521   99 HPDVLRASTASDGKIYLIPyeppKDVPNQGYFIRKDWLDKLNLKTPK-TLD--ELYNVLKAFKEKDPNGNGkadeIPFID 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837 202 SNQE-GYYNFI----------------YQNGGKVITDDLKSGYADpktieALDYYFSFVKEKISPA---ITVDKERAEAF 261
Cdd:cd13521  176 RDPLyGAFRLInswgarsaggstdsdwYEDNGKFKHPFASEEYKD-----GMKYMNKLYTEGLIDKesfTQKDDQAEQKF 250

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837 262 QNGQVAMSVFGSW---NLSGFTANDYIRENADVAVLPKGPDGTRA-------TIFNGLghAIAATTKHPDAAWKWVEYLS 331
Cdd:cd13521  251 SNGKLGGFTHNWFasdNLFTAQLGKEKPMYILLPIAPAGNVKGRReedspgyTGPDGV--AISKKAKNPVAALKFFDWLA 328

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 546343837 332 SKEAQEmQATLGVAISAYKgaadtwVDSNKNFTIKNYVDMVD 373
Cdd:cd13521  329 SEEGRE-LANFGIEGVHYN------KDNGKKRTKDPVKKSDQ 363
PBP2_oligosaccharide_1 cd13655
The periplasmic binding component of ABC tansport system specific for an unknown ...
 53-338 4.33e-12

The periplasmic binding component of ABC tansport system specific for an unknown oligosaccharide; possess the type 2 periplasmic binidng fold; This group represents an uncharacterized periplasmic-binding protein of an ATP-binding cassette transporter predicted to be involved in uptake of an unknown oligosaccharide molecule. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270373 [Multi-domain]  Cd Length: 363  Bit Score: 66.99  E-value: 4.33e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837  53 LRKIADEFEKKNPDIKINIQVSDWDSYWTMLEAGATGGSLPDTFWMHSNEIyrygsNEM-----LLPLdeylAKSEDAKL 127
Cdd:cd13655   14 LKEMVDAFKEKHPEWKITITIGVVGEADAKDEVLKDPSAAADVFAFANDQL-----GELvdagaIYPL----TGSAVDKI 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837 128 ANF-PDGLNEIYNINGKQYAIPKDFDTIGLWYNKKLFDEagipypDDTWDWNKLkevakkLTKPDGSQYGFGAGLSNqeG 206
Cdd:cd13655   85 KNTnSEATVDAVTYNGKLYGYPFTANTWFMYYDKSKLTE------DDVKSLDTM------LAKAPDAKGKVSFDLSN--S 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837 207 YYN--FIYQNGGKVI----TDDLKSGYADPKTIEALDYyfsFVKEKISPAITVDKERA--EAFQNGQVAMSVFGSWNlsg 278
Cdd:cd13655  151 WYLyaFFFGAGCKLFgnngGDTAGCDFNNEKGVAVTNY---LVDLVANPKFVNDADGDaiSGLKDGTLGAGVSGPWD--- 224

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 546343837 279 ftANDYIR---ENADVAVLPK-GPDGTRATIFNGLGH---AIAATTKHPDAAWKWVEYLSSKEAQEM 338
Cdd:cd13655  225 --AANLKKalgDNYAVAKLPTyTLGGKDVQMKSFAGYkaiGVNSNTKNPEAAMALADYLTNEESQLT 289
PBP2_AlgQ_like_2 cd13581
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 54-344 3.51e-11

Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 periplasmic binding fold; This subgroup includes uncharacterized periplasmic-binding proteins that are closely related to high molecular weight (HMW) alginate bining proteins (AlgQ1 and AlgQ2) found in gram-negative soil bacteria. The HMW alginate uptake system is composed of a novel pit formed on the cell surface and a pit-dependent ATP-binding cassette (ABC) transporter in the inner membrane. The transportation of HMW alginate from the pit to the ABC transporter is mediated by periplasmic HMW alginate-binding proteins (AlgQ1 and AlgQ2). Alginate is an anionic polysaccharide that is made up of alpha-L-mannuronate and its 5'-epimer, alpha-L-guluronate. Alginate is present in the cell walls of brown seaweeds, where it forms a viscous gum by binding water. Alginate is also produced by two bacteria genera Pseudomonas and Azotobacter. AlgQ1 and AlgQ2 belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. However, unlike other bacterial periplasmic-binding proteins that deliver small solutes to ABC transporters, AlgQ1/2 can bind a macromolecule and may have specificity for either sugar or a certain type of polysaccharide.


Pssm-ID: 270299 [Multi-domain]  Cd Length: 490  Bit Score: 64.65  E-value: 3.51e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837  54 RKIADEFEKKNpDIKINIQVSDWDSYWTMLEAGATGGSLPDTFwMHSN----EIYRYGSNEMLLPLDEYLAKSE---DAK 126
Cdd:cd13581   20 NLFFKRLEEKT-GIKIEWETVPEDAWAEKKNLMLASGDLPDAF-LGAGasdaDLMTYGKQGLFLPLEDLIDKYApnlKAL 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837 127 LANFPDGLNEIYNINGKQYAIPKDFDTIG------LWYNKKLFDEAGIPYPdDTWDwnKLKEVAKKL------------- 187
Cdd:cd13581   98 FDENPDIKAAITAPDGHIYALPSVNECYHcsygqrMWINKKWLDKLGLEMP-TTTD--ELYEVLKAFkeqdpngngkade 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837 188 ----TKPDGSQYGFGAGLSNQEGY------YNFIYQNGGKVITddlksGYADPKTIEALDYYFSFVKEK-ISP-AITVDK 255
Cdd:cd13581  175 iplsFSGLNGGTDDPAFLLNSFGIndggygGYGFVVKDGKVIY-----TATDPEYKEALAYLNKLYKEGlIDPeAFTQDY 249

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837 256 ERAEAFQNGQVAM-SVFGSWNLSGFTANDYIRENADVAVLpKGPDGTRA------TIFNGLGHAIAATTKHPDAAWKWVE 328
Cdd:cd13581  250 DQLAAKGKASTAKvGVFFGWDPGLFFGEERYEQYVPLPPL-KGPNGDQLawvgnsSGYGRGGFVITSKNKNPEAAIRWAD 328

                        330
                 ....*....|....*.
gi 546343837 329 YLSSKEaQEMQATLGV 344
Cdd:cd13581  329 FLYSPE-GSLQANFGP 343
PBP2_MBP cd13656
The periplasmic binding component of ABC tansport system specific for maltose; possess the ...
 44-337 4.28e-10

The periplasmic binding component of ABC tansport system specific for maltose; possess the type 2 periplasmic binidng fold; This group includes the periplasmic maltose-binding protein of an ATP-binding cassette transporter. Maltose is a disaccharide formed from two units of glucose. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270374 [Multi-domain]  Cd Length: 364  Bit Score: 61.07  E-value: 4.28e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837  44 IWDSGQE--PGLRKIADEFEKknpDIKINIQVSDWDSYWTMLEAGATGGSLPDTFWMHSNEIYRYGSNEMLLPLDeyLAK 121
Cdd:cd13656    5 IWINGDKgyNGLAEVGKKFEK---DTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEIT--PDK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837 122 SEDAKLANFPdglNEIYNINGKQYAIPKDFDTIGLWYNKKLfdeagIPYPDDTWDW-----NKLKEVAKKLTKPDGSQYG 196
Cdd:cd13656   80 AFQDKLYPFT---WDAVRYNGKLIAYPIAVEALSLIYNKDL-----LPNPPKTWEEipaldKELKAKGKSALMFNLQEPY 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837 197 FGAGLSNQEGYYNFIYQNGGKVITDdlkSGYADPKTIEALDYYFSFVKEKISPAITvDKERAEA-FQNGQVAMSVFGSWN 275
Cdd:cd13656  152 FTWPLIAADGGYAFKYENGKYDIKD---VGVDNAGAKAGLTFLVDLIKNKHMNADT-DYSIAEAaFNKGETAMTINGPWA 227

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 546343837 276 LSGFTANdyiRENADVAVLPkGPDGTRATIFNG-LGHAIAATTKHPDAAWKWVE-YLSSKEAQE 337
Cdd:cd13656  228 WSNIDTS---KVNYGVTVLP-TFKGQPSKPFVGvLSAGINAASPNKELAKEFLEnYLLTDEGLE 287
AfuA COG1840
ABC-type Fe3+ transport system, periplasmic component [Inorganic ion transport and metabolism]; ...
 56-353 4.46e-09

ABC-type Fe3+ transport system, periplasmic component [Inorganic ion transport and metabolism];


Pssm-ID: 441445 [Multi-domain]  Cd Length: 286  Bit Score: 57.25  E-value: 4.46e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837  56 IADEFEKKNpDIKINIQVSDWDSYWTMLEAGAtGGSLPDTFWmhsneiyryGSNEMLLPL---DEYLAKSEDAKLANFPD 132
Cdd:COG1840    1 LLEAFEKKT-GIKVNVVRGGSGELLARLKAEG-GNPPADVVW---------SGDADALEQlanEGLLQPYKSPELDAIPA 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837 133 GLneiYNINGKQYAIpkDFDTIGLWYNKKLFDEAGIPypdDTWD------WnklkevAKKLTKPDGSQYGFGAGLsnqeg 206
Cdd:COG1840   70 EF---RDPDGYWFGF--SVRARVIVYNTDLLKELGVP---KSWEdlldpeY------KGKIAMADPSSSGTGYLL----- 130

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837 207 YYNFIYQNGGKvitddlksgyadpktiEALDYYfsfvkEKISPAITV----DKERAEAFQNGQVAMSVFGSWNlsgftAN 282
Cdd:COG1840  131 VAALLQAFGEE----------------KGWEWL-----KGLAANGARvtgsSSAVAKAVASGEVAIGIVNSYY-----AL 184

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 546343837 283 DYIRENADVA-VLPKgpDGTratIFNGLGHAIAATTKHPDAAWKWVEYLSSKEAQEMQATLGVAISAYKGAA 353
Cdd:COG1840  185 RAKAKGAPVEvVFPE--DGT---LVNPSGAAILKGAPNPEAAKLFIDFLLSDEGQELLAEEGYEYPVRPDVE 251
PBP2_PotD_PotF_like cd13590
The periplasmic-binding component of ABC transporters involved in uptake of polyamines; ...
 58-336 1.04e-08

The periplasmic-binding component of ABC transporters involved in uptake of polyamines; possess the type 2 periplasmic binding fold; This family represents the periplasmic substrate-binding domain that functions as the primary high-affinity receptors of ABC-type polyamine transport systems. Polyamine transport plays an essential role in the regulation of intracellular polyamine levels which are known to be elevated in rapidly proliferating cells and tumors. Natural polyamines are putrescine, spermindine, and spermine. They are polycations that play multiple roles in cell growth, survival and proliferation, and plant stress and disease resistance. They can interact with negatively charged molecules, such as nucleic acids, to modulate their functions. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270308 [Multi-domain]  Cd Length: 315  Bit Score: 56.47  E-value: 1.04e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837  58 DEFEKKNpDIKINIQV-SDWDSYWTMLEAGATGG---SLPDTFWMHsneiyRYGSNEMLLPLDEylaksedAKLANFPDG 133
Cdd:cd13590   17 KAFEKET-GVKVNYDTyDSNEEMLAKLRAGGGSGydlVVPSDYMVE-----RLIKQGLLEPLDH-------SKLPNLKNL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837 134 LNEIYNIN---GKQYAIPKDFDTIGLWYNKKLFDEAGIPYPDDTWDwnklKEVAKKLTKPDGSQYGFGAGLsnqegyynf 210
Cdd:cd13590   84 DPQFLNPPydpGNRYSVPYQWGTTGIAYNKDKVKEPPTSWDLDLWD----PALKGRIAMLDDAREVLGAAL--------- 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837 211 iyqnggkvitddLKSGY----ADPKTIEAldyyfsfVKEKIS---PAITV--DKERAEAFQNGQVAMSVfgSWNLSGFTA 281
Cdd:cd13590  151 ------------LALGYspntTDPAELAA-------AAELLIkqkPNVRAfdSDSYVQDLASGEIWLAQ--AWSGDALQA 209

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 546343837 282 NdyiRENADVA-VLPKgpDGtraTIFNGLGHAIAATTKHPDAAWKWVEYLSSKEAQ 336
Cdd:cd13590  210 N---RENPNLKfVIPK--EG---GLLWVDNMAIPKGAPNPELAHAFINFLLDPEVA 257
PBP2_AlgQ_like_4 cd13583
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 56-370 2.59e-08

Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 periplasmic binding fold; This subgroup includes uncharacterized periplasmic-binding proteins that are closely related to high molecular weight (HMW) alginate bining proteins (AlgQ1 and AlgQ2) found in gram-negative soil bacteria. The HMW alginate uptake system is composed of a novel pit formed on the cell surface and a pit-dependent ATP-binding cassette (ABC) transporter in the inner membrane. The transportation of HMW alginate from the pit to the ABC transporter is mediated by periplasmic HMW alginate-binding proteins (AlgQ1 and AlgQ2). Alginate is an anionic polysaccharide that is made up of alpha-L-mannuronate and its 5'-epimer, alpha-L-guluronate. Alginate is present in the cell walls of brown seaweeds, where it forms a viscous gum by binding water. Alginate is also produced by two bacteria genera Pseudomonas and Azotobacter. AlgQ1 and AlgQ2 belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. However, unlike other bacterial periplasmic-binding proteins that deliver small solutes to ABC transporters, AlgQ1/2 can bind a macromolecule and may have specificity for either sugar or a certain type of polysaccharide.


Pssm-ID: 270301 [Multi-domain]  Cd Length: 478  Bit Score: 55.83  E-value: 2.59e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837  56 IADEFEKKNpDIKINIQV---SDWDSYWTMLEAGatgGSLPDtfWMHS---NEIYRYGSNEMLLPLDEYL-------AKS 122
Cdd:cd13583   22 IWKEIEEKT-NVKFKRTPipsSDYETKRSLLIAS---GDAPD--IIPVlypGEENEFVASGALLPISDYLdympnykKYV 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837 123 EDAKLAnfpDGLNEIYNINGKQYAIP-----KDFDTIGLwYNKKLFDEAGIPYPddtWDWNKLKEVAKKL------TKPD 191
Cdd:cd13583   96 EKWGLG---KELATGRQSDGKYYSLPglhedPGVQYSFL-YRKDIFEKAGIKIP---TTWDEFYAALKKLkekypdSYPY 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837 192 GSQYGFGAGLSNQEGYYN----------FIYQNGGKVITDDLKSGYADpktieALDYYFSFVKEK-ISPAITVDKERA-- 258
Cdd:cd13583  169 SDRWNSNALLLIAAPAFGttagwgfsnyTYDPDTDKFVYGATTDEYKD-----MLQYFNKLYAEGlLDPESFTQTDDQak 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837 259 EAFQNGQVAMSVFGSWNLSGFTANDYIRENADVAVLPKGPDG-------TRATIFNGLGHAIAAT-TKHPDAAWKWVEYL 330
Cdd:cd13583  244 AKFLNGKSFVITTNPQTVDELQRNLRAADGGNYEVVSITPPAgpagkaiNGSRLENGFMISSKAKdSKNFEALLQFLDWL 323

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 546343837 331 SSKEAQEMqATLGVAISAYKGAADTWVDSNKNFTIKNYVD 370
Cdd:cd13583  324 YSDEGQEL-ATWGVEGETYTKEGDGKVYLADSNTPALNPS 362
PBP2_Fbp_like_2 cd13547
Substrate binding domain of an uncharacterized ferric iron transporter, a member of the type 2 ...
 47-343 2.76e-08

Substrate binding domain of an uncharacterized ferric iron transporter, a member of the type 2 periplasmic binding fold superfamily; The periplasmic iron binding protein plays an essential role in the iron uptake pathway of Gram-negative pathogenic bacteria from the Pasteurellaceae and Neisseriaceae families and is critical for survival of these pathogens within the host. This periplasmic domain (Fbp) has high affinity for ferric iron and serves as the primary receptor for transport. After binding iron with high affinity, Fbp interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The ferric iron-binding proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270265 [Multi-domain]  Cd Length: 259  Bit Score: 54.54  E-value: 2.76e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837  47 SGQEPGLRKIADEFEKKNPDIKINIQVSDWDSYWTMLEAGATGGSL-PDTFWMHS-NEIYRYGSNEMLLPldeYLAKSED 124
Cdd:cd13547    7 SMPEDLANALVEAFEKKYPGVKVEVFRAGTGKLMAKLAAEAEAGNPqADVLWVADpPTAEALKKEGLLLP---YKSPEAD 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837 125 AKLANFPDGlneiyniNGkqYAIPKDFDTIGLWYNKKLFDEAGipyPDDTWDWNKlKEVAKKLTKPD----GSQYGFGAG 200
Cdd:cd13547   84 AIPAPFYDK-------DG--YYYGTRLSAMGIAYNTDKVPEEA---PKSWADLTK-PKYKGQIVMPDplysGAALDLVAA 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837 201 LSNQEG----YYNFIYQNGGKV------ITDDLKSGyadpktiealdyyfsfvkeKISPAITVDkeraeafqngqvamsv 270
Cdd:cd13547  151 LADKYGlgweYFEKLKENGVKVeggngqVLDAVASG-------------------ERPAGVGVD---------------- 195

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 546343837 271 fgswnlsgFTANDYIRENADVAVL-PKgpDGTRAT---IfnglghAIAATTKHPDAAWKWVEYLSSKEAQEMQATLG 343
Cdd:cd13547  196 --------YNALRAKEKGSPLEVIyPE--EGTVVIpspI------AILKGSKNPEAAKAFVDFLLSPEGQELVADAG 256
PBP2_AlgQ1_2 cd13584
Periplasmic-binding component of alginate-specific ABC uptake system; contains the type 2 ...
 87-415 3.24e-07

Periplasmic-binding component of alginate-specific ABC uptake system; contains the type 2 periplasmic binding fold; This group represents the periplasmic-binding component of high molecular weight (HMW) alginate uptake system found in gram-negative soil bacteria such as Sphingomonas sp. A1. The HMW alginate uptake system is composed of a novel pit formed on the cell surface and a pit-dependent ATP-binding cassette (ABC) transporter in the inner membrane. The transportation of HMW alginate from the pit to the ABC transporter is mediated by periplasmic HMW alginate-binding proteins (AlgQ1 and AlgQ2). Alginate is an anionic polysaccharide that includes alpha-L-mannuronate and its 5'-epimer, alpha-L-guluronate. Alginate is present in the cell walls of brown seaweeds, where it forms a viscous gum by binding water. Alginate is also produced by two bacteria genera Pseudomonas and Azotobacter. AlgQ1 and AlgQ2 belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. However, unlike other bacterial periplasmic-binding proteins that deliver small solutes to ABC transporters, AlgQ1/2 can bind a macromolecule and may have specificity for either sugar or a certain type of polysaccharide.


Pssm-ID: 270302 [Multi-domain]  Cd Length: 481  Bit Score: 52.44  E-value: 3.24e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837  87 ATGGSLPDTF---WM-HSNEIYRYGSNEMLLPLDEYL---AKSEDAKLANFPDGLNEIYNINGKQYAIP--KDFDTIGLW 157
Cdd:cd13584   53 MASGQLPDIIggdWLkDKGGFEKYGEDGAFLPLNDLIdqyAPNLKKFLDEHPDVKKAITTDDGNIYGFPylPDGDVAKEA 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837 158 Y----NKKLFDEAGIPYPDDTWDWNKLKeVAKKLTKPDGSQYGFGAGLSNQEGYYNFI-------------YQNGGKVit 220
Cdd:cd13584  133 RgyfiRKDWLDKLGLKTPSTIDEWYTVL-KAFKERDPNGNGKADEVPLILTKPGYDETgrlinawgaymdfYQENGKV-- 209

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837 221 ddlKSGYADPKTIEALDYYFSFVKEK-ISPAITVDKERAEA--FQNGQVAmSVFGSWNLSGFTANDYIRENAD----VAV 293
Cdd:cd13584  210 ---KYGPLEPGFKDFLKTMNQWYKEGlIDPDFFTRKAKAREqnIMNGNIG-GFTHDWFASTGTFNLALLKNVPdfklVAV 285

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837 294 LP----KG--PDGTRAT-IFNGLGHAIAATTKHPDAAWKWVEYLSSKEAQeMQATLGVAISAYkgaadTWVDSNKNFT-- 364
Cdd:cd13584  286 PPpvlnKGqtPYEEDSRqIAKGDGAAITASNKNPVLAIKWLDYAYSEEGR-LLSNFGVEGESY-----TIKNGKPVFTdd 359

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 546343837 365 -IKNYVDMVDYAQIRPYSQTTIK-WEDKAYEllkpaylgEKATEEAAKETADM 415
Cdd:cd13584  360 vLKDPQPLVNALSLYYGAQIPGGfWQDYEYE--------EQWTTPEALESKDI 404
malE PRK09474
maltose/maltodextrin ABC transporter substrate-binding protein MalE;
44-349 3.24e-07

maltose/maltodextrin ABC transporter substrate-binding protein MalE;


Pssm-ID: 236533 [Multi-domain]  Cd Length: 396  Bit Score: 51.94  E-value: 3.24e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837  44 IWDSGQE--PGLRKIADEFEKknpDIKINIQVSDWDSywtmLE-----AGATGGSlPDT-FWMHSneiyRYG---SNEML 112
Cdd:PRK09474  35 IWINGDKgyNGLAEVGKKFEK---DTGIKVTVEHPDK----LEekfpqVAATGDG-PDIiFWAHD----RFGgyaQSGLL 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837 113 LPLDEylAKSEDAKLANFP-DGLNeiynINGKQYAIPKDFDTIGLWYNKKLfdeagIPYPDDTWDW-----NKLKEVAKK 186
Cdd:PRK09474 103 AEVTP--SKAFKDKLVPFTwDAVR----YNGKLIGYPIAVEALSLIYNKDL-----VPTPPKTWEEipaldKELKAKGKS 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837 187 LTKPDGSQYGFGAGLSNQEGYYNFIYQNGGKVITDdlkSGYADPKTIEALDYYFSFVKEKISPAiTVDKERAEA-FQNGQ 265
Cdd:PRK09474 172 AIMWNLQEPYFTWPLIAADGGYAFKFENGGYDVKD---VGVNNAGAKAGLQFLVDLVKNKHMNA-DTDYSIAEAaFNKGE 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837 266 VAMSVFGSW---NL--SGFtandyireNADVAVLPKgPDGTRATIFNG-LGHAIAATTKHPDAAWKWVE-YLSSKEAQEM 338
Cdd:PRK09474 248 TAMTINGPWawsNIdkSGI--------NYGVTVLPT-FNGKPSKPFVGvLSAGINAASPNKELAKEFLEnYLLTDEGLET 318

                        330
                 ....*....|....*
gi 546343837 339 ---QATLG-VAISAY 349
Cdd:PRK09474 319 vnkDKPLGaVALKSF 333
PBP2_PotD_PotF_like_2 cd13663
The periplasmic substrate-binding component of an uncharacterized active transport system ...
 58-335 2.11e-05

The periplasmic substrate-binding component of an uncharacterized active transport system closely related to spermidine and putrescine transporters; contains the type 2 periplasmic binding fold; This group represents the periplasmic substrate-binding domain that serves as a primary polyamine receptor of an uncharacterized ABC-type transport system from gram-negative bacteria. Polyamine transport plays an essential role in the regulation of intracellular polyamine levels which are known to be elevated in rapidly proliferating cells and tumors. Natural polyamines are putrescine, spermindine, and spermine. They are polycations that play multiple roles in cell growth, survival and proliferation, as well as plant stress and disease resistance. They can interact with negatively charged molecules, such as nucleic acids, to modulate their functions. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270381 [Multi-domain]  Cd Length: 323  Bit Score: 46.13  E-value: 2.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837  58 DEFEKKNpDIKINIQVsdWDSYWTMLEAGATGGSLPDTFWMHSNEIYRYGSNEMLLPLDEYLAKSEDAKLANFPDGLNEI 137
Cdd:cd13663   17 DDFEKET-GIKVNYET--FDSNEEMYTKIKTGGTSYDVIVPSDYMIEKLIKEDLLQPLDYSKLPNVDKNINIQPDLLNLA 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837 138 YNiNGKQYAIPKDFDTIGLWYNKKLFDEagipYPDDTWDWNKLKEVAKKLTKPDGSQYGFGAGLsnqegyynfiYQNGGK 217
Cdd:cd13663   94 FD-PINEYSVPYFWGTLGIVYNKTKVSL----EELSWWNILWNKKYKGKILMYDSPRDAFMVAL----------KALGYS 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837 218 VITddlksgyADPKTIEALDYYFSFVKEKISPAITVDKERAEAfqNGQVAMSVfgSWnlSGfTANDYIRENADVA-VLPK 296
Cdd:cd13663  159 LNT-------TNPDEIEEAKDWLIKQKPNVKAFVVDEIKDLMI--NGNADIAV--TY--SG-DAAYAMEENENLDyVIPK 224

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 546343837 297 gpDGTRAtIFNGLghAIAATTKHPDAAWKWVEYLSSKEA 335
Cdd:cd13663  225 --EGSNL-WFDNW--VIPKNAKNVDLAYKFINFLLRPDN 258
PBP2_polyamine_1 cd13588
The periplasmic-binding component of an uncharacterized ABC transporter involved in uptake of ...
 59-336 8.11e-05

The periplasmic-binding component of an uncharacterized ABC transporter involved in uptake of polyamines; contains the type 2 periplasmic binding fold; This group represents the periplasmic binding domain that functions as the primary high-affinity receptor of an uncharactertized ABC-type polyamine transport system. Polyamine transport plays an essential role in the regulation of intracellular polyamine levels which are known to be elevated in rapidly proliferating cells and tumors. Natural polyamines are putrescine, spermindine, and spermine. They are polycations that play multiple roles in cell growth, survival and proliferation, and plant stress and disease resistance. They can interact with negatively charged molecules, such as nucleic acids, to modulate their functions. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270306 [Multi-domain]  Cd Length: 279  Bit Score: 44.21  E-value: 8.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837  59 EFEKKNPDIKINIQVSDWDSYWTMLEagaTGGSLPDTFWMHSNEIYRYGSNEMLLPLDEYL---AKSEDAKLANFPDgln 135
Cdd:cd13588   18 AFEEATGCKVVVKFFGSEDEMVAKLR---SGGGDYDVVTPSGDALLRLIAAGLVQPIDTSKipnYANIDPRLRNLPW--- 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837 136 eiYNINGKQYAIPKDFDTIGLWYNKKLFDEAgipypdDTWDWNKL--KEVAKKLTKPDGS--QYGFGAglsnqegyynfi 211
Cdd:cd13588   92 --LTVDGKVYGVPYDWGANGLAYNTKKVKTP------PTSWLALLwdPKYKGRVAARDDPidAIADAA------------ 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837 212 yqnggkvitddLKSGYADPK--TIEALDYYFSFVKEKISPAITVDKERAEA---FQNGQVAMSvfGSWNlsgFTANDYIR 286
Cdd:cd13588  152 -----------LYLGQDPPFnlTDEQLDAVKAKLREQRPLVRKYWSDGAELvqlFANGEVVAA--TAWS---GQVNALQK 215

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 546343837 287 ENADVA-VLPKGpdGTRATIFNglgHAIAATTKHPDAAWKWVEYLSSKEAQ 336
Cdd:cd13588  216 AGKPVAyVIPKE--GATGWVDT---WMILKDAKNPDCAYKWLNYMLSPKVQ 261
PBP2_polyamines cd13523
The periplasmic-binding component of ABC transporters involved in uptake of polyamines; ...
 58-340 7.65e-04

The periplasmic-binding component of ABC transporters involved in uptake of polyamines; possess the type 2 periplasmic binding fold; This family represents the periplasmic substrate-binding proteins that function as the primary high-affinity receptors of ABC-type polyamine transport systems. Polyamine transport plays an essential role in the regulation of intracellular polyamine levels which are known to be elevated in rapidly proliferating cells and tumors. Natural polyamines are putrescine, spermindine, and spermine. They are polycations that play multiple roles in cell growth, survival and proliferation, as well as plant stress and disease resistance. They can interact with negatively charged molecules, such as nucleic acids, to modulate their functions. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270241 [Multi-domain]  Cd Length: 268  Bit Score: 40.88  E-value: 7.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837  58 DEFEKKNpDIKINIQVSDWDSYWTMLEAGATGGSLpDTFWMHSNEIYRYGSNEMLLPLDEYLAKSeDAKLANFPDGLNEI 137
Cdd:cd13523   17 DPFEKET-GIKVVVDTAANSERMIKKLSAGGSGGF-DLVTPSDSYTSRQLGVGLMQPIDKSLLPS-WATLDPHLTLAAVL 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837 138 YNiNGKQYAIPKDFDTIGLWYNKKLFDEAGIPYPDDTWDwnklKEVAKKLTKPDGSQYGF-GAGLSNQEGYYNFIYQNGG 216
Cdd:cd13523   94 TV-PGKKYGVPYQWGATGLVYNTDKVKAPPKSYAADLDD----PKYKGRVSFSDIPRETFaMALANLGADGNEELYPDFT 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837 217 KVITDDLKSGYADPKTiealdYYfsfvkekispaiTVDKERAEAFQNGQVAMSVfgSWNLSGFTANdyiRENADVA-VLP 295
Cdd:cd13523  169 DAAAALLKELKPNVKK-----YW------------SNASQPANLLLNGEVVLAM--AWLGSGFKLK---QAGAPIEfVVP 226

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 546343837 296 KGpdGTRATIFNglgHAIAATTKHPDAAWKWVEYLSSKEAQEMQA 340
Cdd:cd13523  227 KE--GAVGWLDT---FAVPANAPNKDGAYKLLNALLRPKVAAAVA 266
PBP2_AlgQ_like_3 cd13582
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 87-336 1.96e-03

Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 periplasmic binding fold; This subgroup includes uncharacterized periplasmic-binding proteins that are closely related to high molecular weight (HMW) alginate bining proteins (AlgQ1 and AlgQ2) found in gram-negative soil bacteria. The HMW alginate uptake system is composed of a novel pit formed on the cell surface and a pit-dependent ATP-binding cassette (ABC) transporter in the inner membrane. The transportation of HMW alginate from the pit to the ABC transporter is mediated by periplasmic HMW alginate-binding proteins (AlgQ1 and AlgQ2). Alginate is an anionic polysaccharide that is made up of alpha-L-mannuronate and its 5'-epimer, alpha-L-guluronate. Alginate is present in the cell walls of brown seaweeds, where it forms a viscous gum by binding water. Alginate is also produced by two bacteria genera Pseudomonas and Azotobacter. AlgQ1 and AlgQ2 belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. However, unlike other bacterial periplasmic-binding proteins that deliver small solutes to ABC transporters, AlgQ1/2 can bind a macromolecule and may have specificity for either sugar or a certain type of polysaccharide.


Pssm-ID: 270300 [Multi-domain]  Cd Length: 504  Bit Score: 40.38  E-value: 1.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837  87 ATGGSLPDTFWMHsNEIYRYGSNEMLLPLDEYLAK----------SEDAKLANFPDGLNEIYNINGKQYAIPKDFDtiGL 156
Cdd:cd13582   51 IASGDLPDLIYAK-GDTDKLIEAGALVPLDDLIEKygpnikkwygDYLLKKLRSEDGHIYYLPNYRVEDAPWYPNG--GF 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837 157 WYNKKLFDEAGIPYPDdTWD--WNKLKEVAKKLTKPDG--------SQYGFGAGLSNQEGYYNFIYQNGGKVITDD--LK 224
Cdd:cd13582  128 WLQHDVLKELGYPKIK-TLDdyENLIKDYKKKYPTINGqptigftaLTDDWRFLISVTNPAFLAGYPNDGEVYVDPktLK 206

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837 225 SGYaDPKTIEALDYYF---SFVKEKIspaitVDKEraeAF-QN----------GQVAMSVFGSWNLSGftANDYIRENAD 290
Cdd:cd13582  207 AKF-HYTRPYYKEYYKwlnELWNEGL-----LDKE---SFtQKydqylakiasGRVLGFYDAGWDIGN--AITALKAKGK 275

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 546343837 291 -----------VAVLPKGPDGTRATIFNGLGHAIAATTKHPDAAWKWVEYLSSKEAQ 336
Cdd:cd13582  276 derlyayypvaVGVDDKDYNYGDPGYLGGDGIAITKSCKDPERAFKFLDWLASEEAQ 332
PBP2_PotD cd13660
The periplasmic substrate-binding component of an active spermidine-preferential transport ...
 111-330 5.34e-03

The periplasmic substrate-binding component of an active spermidine-preferential transport system; contains the type 2 periplasmic binding fold; This group represents the periplasmic binding domain that serves as the primary polyamine receptor of ABC-type spermindine-preferential transport system from gram-negative bacteria. Polyamine transport plays an essential role in the regulation of intracellular polyamine levels which are known to be elevated in rapidly proliferating cells and tumors. Natural polyamines are putrescine, spermindine, and spermine. They are polycations that play multiple roles in cell growth, survival and proliferation, and plant stress and disease resistance. They can interact with negatively charged molecules, such as nucleic acids, to modulate their functions. Members of this family belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270378 [Multi-domain]  Cd Length: 315  Bit Score: 38.72  E-value: 5.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837 111 MLLPLDEylaksedAKLANF----PDGLNEIYNINgKQYAIPKDFDTIGLWYNKKLFDEAGIPYPDDTWDwnklKEVAKK 186
Cdd:cd13660   68 LIQKIDK-------SKITNFsnidPDFLNQPFDPN-NDYSIPYIWGATALAVNGDAVDGKSVTSWADLWK----PEYKGK 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546343837 187 LTKPDGSQYGFGAGLsnqegyynfiyqnggkvitddLKSGYA----DPKTIEALdyyFSFVKEKISPAITVD-KERAEAF 261
Cdd:cd13660  136 LLLTDDAREVFQMAL---------------------RKLGYSgntkDPEEIEAA---FEELKKLMPNVAAFDsDNPANPY 191

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 546343837 262 QNGQVAMSVFgsWNLSGFTANDYiRENADVAVLPKGpdgtraTIFNGLGHAIAATTKHPDAAWKWVEYL 330
Cdd:cd13660  192 MEGEVALGMI--WNGSAFVARQA-NKPIHVVWPKEG------GIFWMDSFAIPANAKNKEGALKFINFL 251
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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