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Conserved domains on  [gi|1540151759|emb|VEI16337|]
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Maltose-binding periplasmic proteins/domains [Actinomyces viscosus]

Protein Classification

type 2 periplasmic-binding domain-containing protein( domain architecture ID 229383)

type 2 periplasmic-binding protein (PBP2) is typically comprised of two globular subdomains connected by a flexible hinge; it binds its ligand in the cleft between these domains in a manner resembling a Venus flytrap; similar to the ligand-binding domains found in solute binding proteins that serve as initial receptors in the transport, signal transduction and channel gating

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Periplasmic_Binding_Protein_Type_2 super family cl21456
Type 2 periplasmic binding fold superfamily; This evolutionary model and hierarchy represent ...
 50-414 4.13e-40

Type 2 periplasmic binding fold superfamily; This evolutionary model and hierarchy represent the ligand-binding domains found in solute binding proteins that serve as initial receptors in the transport, signal transduction and channel gating. The PBP2 proteins share the same architecture as periplasmic binding proteins type 1 (PBP1), but have a different topology. They are typically 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 origin of PBP module can be traced across the distant phyla, including eukaryotes, archebacteria, and prokaryotes. The majority of PBP2 proteins are involved in the uptake of a variety of soluble substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. 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. Besides transport proteins, the family includes ionotropic glutamate receptors and unorthodox sensor proteins involved in signal transduction. The substrate binding domain of the LysR transcriptional regulators and the oligopeptide-like transport systems also contain the type 2 periplasmic binding fold and thus they are significantly homologous to that of the PBP2; however, these two families are grouped into a separate hierarchy of the PBP2 superfamily due to the large number of protein sequences.


The actual alignment was detected with superfamily member cd13585:

Pssm-ID: 473866 [Multi-domain]  Cd Length: 383  Bit Score: 147.17  E-value: 4.13e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540151759  50 VNDIVARWNAEHPDMKVEATKFDgkASDMNVKLENDVKAGTGPCLAQVGYAEIPKLYSSGLLADVSQQAEK--YKDHFSE 127
Cdd:cd13585    16 LKKLIDAFEKENPGVKVEVVPVP--YDDYWTKLTTAAAAGTAPDVFYVDGPWVPEFASNGALLDLDDYIEKdgLDDDFPP 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540151759 128 GSMSLMTVGKTVVGLPQDSGPLVYFYNKAAFDQLG--LSVPTTSAELADVAQK--AAAQGKYAVAFEPD-EAPNTLAGQS 202
Cdd:cd13585    94 GLLDAGTYDGKLYGLPFDADTLVLFYNKDLFDKAGpgPKPPWTWDELLEAAKKltDKKGGQYGFALRGGsGGQTQWYPFL 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540151759 203 AAAGAQWFSAenDKWKVNVNSPETAKVSTFWQGLLDSKTALVANRWDDAFGKALVDQqliGTIGAAWEGALLADTMKDSP 282
Cdd:cd13585   174 WSNGGDLLDE--DDGKATLNSPEAVEALQFYVDLYKDGVAPSSATTGGDEAVDLFAS---GKVAMMIDGPWALGTLKDSK 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540151759 283 NAGSWAVAQLPAFGDTPMSGPDGGSGVAVLKGCSNPEGAMAFNDWFNTQVDDLATQGLVLTAKAPVKTPESISTFFGGQD 362
Cdd:cd13585   249 VKFKWGVAPLPAGPGGKRASVLGGWGLAISKNSKHPEAAWKFIKFLTSKENQLKLGGAAGPAALAAAAASAAAPDAKPAL 328

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1540151759 363 VYAEFTKANAAVnSKFGFMPTWPSLTDPMTQAAEAA--GKGTGKVDDIFQSAQK 414
Cdd:cd13585   329 ALAAAADALAAA-VPPPVPPPWPEVYPILSEALQEAllGALGKSPEEALKEAAK 381
 
Name Accession Description Interval E-value
PBP2_TMBP_like cd13585
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ...
 50-414 4.13e-40

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: 147.17  E-value: 4.13e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540151759  50 VNDIVARWNAEHPDMKVEATKFDgkASDMNVKLENDVKAGTGPCLAQVGYAEIPKLYSSGLLADVSQQAEK--YKDHFSE 127
Cdd:cd13585    16 LKKLIDAFEKENPGVKVEVVPVP--YDDYWTKLTTAAAAGTAPDVFYVDGPWVPEFASNGALLDLDDYIEKdgLDDDFPP 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540151759 128 GSMSLMTVGKTVVGLPQDSGPLVYFYNKAAFDQLG--LSVPTTSAELADVAQK--AAAQGKYAVAFEPD-EAPNTLAGQS 202
Cdd:cd13585    94 GLLDAGTYDGKLYGLPFDADTLVLFYNKDLFDKAGpgPKPPWTWDELLEAAKKltDKKGGQYGFALRGGsGGQTQWYPFL 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540151759 203 AAAGAQWFSAenDKWKVNVNSPETAKVSTFWQGLLDSKTALVANRWDDAFGKALVDQqliGTIGAAWEGALLADTMKDSP 282
Cdd:cd13585   174 WSNGGDLLDE--DDGKATLNSPEAVEALQFYVDLYKDGVAPSSATTGGDEAVDLFAS---GKVAMMIDGPWALGTLKDSK 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540151759 283 NAGSWAVAQLPAFGDTPMSGPDGGSGVAVLKGCSNPEGAMAFNDWFNTQVDDLATQGLVLTAKAPVKTPESISTFFGGQD 362
Cdd:cd13585   249 VKFKWGVAPLPAGPGGKRASVLGGWGLAISKNSKHPEAAWKFIKFLTSKENQLKLGGAAGPAALAAAAASAAAPDAKPAL 328

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1540151759 363 VYAEFTKANAAVnSKFGFMPTWPSLTDPMTQAAEAA--GKGTGKVDDIFQSAQK 414
Cdd:cd13585   329 ALAAAADALAAA-VPPPVPPPWPEVYPILSEALQEAllGALGKSPEEALKEAAK 381
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
 1-328 8.02e-40

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


Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 145.96  E-value: 8.02e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540151759   1 MKKHALAAsMLAFAMIVAGCSATSSSGSSSSDGV-IRYVHrlPDGEGMTKVNDIVARWNAEHPDMKVEATKFDGkaSDMN 79
Cdd:COG1653     1 MRRLALAL-AAALALALAACGGGGSGAAAAAGKVtLTVWH--TGGGEAAALEALIKEFEAEHPGIKVEVESVPY--DDYR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540151759  80 VKLENDVKAGTGPCLAQVGYAEIPKLYSSGLLADVSQQAEKY---KDHFSEGSMSLMTVGKTVVGLPQDSGPLVYFYNKA 156
Cdd:COG1653    76 TKLLTALAAGNAPDVVQVDSGWLAEFAAAGALVPLDDLLDDDgldKDDFLPGALDAGTYDGKLYGVPFNTDTLGLYYNKD 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540151759 157 AFDQLGLSVPTTSAELADVAQK-AAAQGKYAVAFePDEAPNTLAGQSAAAGAQWFsaeNDKWKVNVNSPETAKVSTFWQG 235
Cdd:COG1653   156 LFEKAGLDPPKTWDELLAAAKKlKAKDGVYGFAL-GGKDGAAWLDLLLSAGGDLY---DEDGKPAFDSPEAVEALEFLKD 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540151759 236 LLDSKTAL--VANRWDDAFGKALVDQQLIGTIGAAWEGALLADTMKDSPnagsWAVAQLPAF-GDTPMSGPDGGSGVAVL 312
Cdd:COG1653   232 LVKDGYVPpgALGTDWDDARAAFASGKAAMMINGSWALGALKDAAPDFD----VGVAPLPGGpGGKKPASVLGGSGLAIP 307

                         330
                  ....*....|....*.
gi 1540151759 313 KGCSNPEGAMAFNDWF 328
Cdd:COG1653   308 KGSKNPEAAWKFLKFL 323
SBP_bac_1 pfam01547
Bacterial extracellular solute-binding protein; This family also includes the bacterial ...
 42-330 4.43e-16

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: 78.23  E-value: 4.43e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540151759  42 PDGEGMTKVNDIVARWNAEHPDMKVEATkfDGKASDMNVKLENDVKAGTGPC-LAQVGYAEIPKLYSSGLLADVSQQAEK 120
Cdd:pfam01547   2 ASLTEAAALQALVKEFEKEHPGIKVEVE--SVGSGSLAQKLTTAIAAGDGPAdVFASDNDWIAELAKAGLLLPLDDYVAN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540151759 121 YkdhfsegsmsLMTVGKTVVGLPQDSGPLVYFYNKAAFDQLGLSVPTTSAELADVAQKAAAQGKYAVAFEPDEAPNTLAG 200
Cdd:pfam01547  80 Y----------LVLGVPKLYGVPLAAETLGLIYNKDLFKKAGLDPPKTWDELLEAAKKLKEKGKSPGGAGGGDASGTLGY 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540151759 201 QSAAAGAQWFSAENDKWKVNVNSPETAKVSTFWQGLLDSKTALVANRWDDA-----------FGKALVDQQLIGT---IG 266
Cdd:pfam01547 150 FTLALLASLGGPLFDKDGGGLDNPEAVDAITYYVDLYAKVLLLKKLKNPGVagadgrealalFEQGKAAMGIVGPwaaLA 229

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1540151759 267 AAWEGALLADTMKDSPNAGSWAVAQLPAFGDtpmsGPDGGSGVAVLKGCSNPEGAMAFNDWFNT 330
Cdd:pfam01547 230 ANKVKLKVAFAAPAPDPKGDVGYAPLPAGKG----GKGGGYGLAIPKGSKNKEAAKKFLDFLTS 289
PRK10974 PRK10974
sn-glycerol-3-phosphate ABC transporter substrate-binding protein UgpB;
35-183 1.29e-03

sn-glycerol-3-phosphate ABC transporter substrate-binding protein UgpB;


Pssm-ID: 182876 [Multi-domain]  Cd Length: 438  Bit Score: 40.94  E-value: 1.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540151759  35 IRYVHRLpDGEGMTKVNDIVARWNAEHPDMKVEATkFDGKASDMNVKLENDVKAGTGPCLAQVGYAEIPKLYSSGLLADV 114
Cdd:PRK10974   28 IPFWHSM-EGELGKEVDSLAQRFNASQPDYKIVPV-YKGNYEQSLAAGIAAFRSGNAPAILQVYEVGTATMMASKAIKPV 105

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1540151759 115 SQQAEKYKDHFSEGSM-----SLMTVGKT--VVGLPQDSGPLVYFYNKAAFDQLGL---SVPTTSAELADVAQKAAAQG 183
Cdd:PRK10974  106 YDVFKDAGIPFDESQFvptvaGYYSDAKTghLLSQPFNSSTPVLYYNKDAFKKAGLdpeQPPKTWQDLAAYAAKLRAAG 184
 
Name Accession Description Interval E-value
PBP2_TMBP_like cd13585
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ...
 50-414 4.13e-40

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: 147.17  E-value: 4.13e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540151759  50 VNDIVARWNAEHPDMKVEATKFDgkASDMNVKLENDVKAGTGPCLAQVGYAEIPKLYSSGLLADVSQQAEK--YKDHFSE 127
Cdd:cd13585    16 LKKLIDAFEKENPGVKVEVVPVP--YDDYWTKLTTAAAAGTAPDVFYVDGPWVPEFASNGALLDLDDYIEKdgLDDDFPP 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540151759 128 GSMSLMTVGKTVVGLPQDSGPLVYFYNKAAFDQLG--LSVPTTSAELADVAQK--AAAQGKYAVAFEPD-EAPNTLAGQS 202
Cdd:cd13585    94 GLLDAGTYDGKLYGLPFDADTLVLFYNKDLFDKAGpgPKPPWTWDELLEAAKKltDKKGGQYGFALRGGsGGQTQWYPFL 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540151759 203 AAAGAQWFSAenDKWKVNVNSPETAKVSTFWQGLLDSKTALVANRWDDAFGKALVDQqliGTIGAAWEGALLADTMKDSP 282
Cdd:cd13585   174 WSNGGDLLDE--DDGKATLNSPEAVEALQFYVDLYKDGVAPSSATTGGDEAVDLFAS---GKVAMMIDGPWALGTLKDSK 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540151759 283 NAGSWAVAQLPAFGDTPMSGPDGGSGVAVLKGCSNPEGAMAFNDWFNTQVDDLATQGLVLTAKAPVKTPESISTFFGGQD 362
Cdd:cd13585   249 VKFKWGVAPLPAGPGGKRASVLGGWGLAISKNSKHPEAAWKFIKFLTSKENQLKLGGAAGPAALAAAAASAAAPDAKPAL 328

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1540151759 363 VYAEFTKANAAVnSKFGFMPTWPSLTDPMTQAAEAA--GKGTGKVDDIFQSAQK 414
Cdd:cd13585   329 ALAAAADALAAA-VPPPVPPPWPEVYPILSEALQEAllGALGKSPEEALKEAAK 381
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
 1-328 8.02e-40

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


Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 145.96  E-value: 8.02e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540151759   1 MKKHALAAsMLAFAMIVAGCSATSSSGSSSSDGV-IRYVHrlPDGEGMTKVNDIVARWNAEHPDMKVEATKFDGkaSDMN 79
Cdd:COG1653     1 MRRLALAL-AAALALALAACGGGGSGAAAAAGKVtLTVWH--TGGGEAAALEALIKEFEAEHPGIKVEVESVPY--DDYR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540151759  80 VKLENDVKAGTGPCLAQVGYAEIPKLYSSGLLADVSQQAEKY---KDHFSEGSMSLMTVGKTVVGLPQDSGPLVYFYNKA 156
Cdd:COG1653    76 TKLLTALAAGNAPDVVQVDSGWLAEFAAAGALVPLDDLLDDDgldKDDFLPGALDAGTYDGKLYGVPFNTDTLGLYYNKD 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540151759 157 AFDQLGLSVPTTSAELADVAQK-AAAQGKYAVAFePDEAPNTLAGQSAAAGAQWFsaeNDKWKVNVNSPETAKVSTFWQG 235
Cdd:COG1653   156 LFEKAGLDPPKTWDELLAAAKKlKAKDGVYGFAL-GGKDGAAWLDLLLSAGGDLY---DEDGKPAFDSPEAVEALEFLKD 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540151759 236 LLDSKTAL--VANRWDDAFGKALVDQQLIGTIGAAWEGALLADTMKDSPnagsWAVAQLPAF-GDTPMSGPDGGSGVAVL 312
Cdd:COG1653   232 LVKDGYVPpgALGTDWDDARAAFASGKAAMMINGSWALGALKDAAPDFD----VGVAPLPGGpGGKKPASVLGGSGLAIP 307

                         330
                  ....*....|....*.
gi 1540151759 313 KGCSNPEGAMAFNDWF 328
Cdd:COG1653   308 KGSKNPEAAWKFLKFL 323
PBP2_UgpB cd14748
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ...
 35-416 2.91e-35

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: 134.34  E-value: 2.91e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540151759  35 IRYVHRLPDGEGMTkVNDIVARWNAEHPDMKVEATkFDGKASDMNVKLENDVKAGTGPCLAQVGYAEIPKLYSSGLLADV 114
Cdd:cd14748     2 ITFWHGMSGPDGKA-LEELVDEFNKSHPDIKVKAV-YQGSYDDTLTKLLAALAAGTAPDVAQVDASWVAQLADSGALEPL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540151759 115 SQQAEKYK---DHFSEGSMSLMTVGKTVVGLPQDSGPLVYFYNKAAFDQLGL---SVPTTSAELADVAQKAAAQGK---- 184
Cdd:cd14748    80 DDYIDKDGvddDDFYPAALDAGTYDGKLYGLPFDTSTPVLYYNKDLFEEAGLdpeKPPKTWDELEEAAKKLKDKGGktgr 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540151759 185 YAVAFEPDEAPNTLAGQSAAAGAQWFSaeNDKWKVNVNSPETAKVSTFWQGLLDsKTALVANRWDDAFGKALVDQQLIGT 264
Cdd:cd14748   160 YGFALPPGDGGWTFQALLWQNGGDLLD--EDGGKVTFNSPEGVEALEFLVDLVG-KDGVSPLNDWGDAQDAFISGKVAMT 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540151759 265 IGAAWEGALLADTMKDSPnagsWAVAQLPAFGDTPMSGPDGGSGVAVLKGCS-NPEGAMAFNDWFNTqvDDLATQGLVLT 343
Cdd:cd14748   237 INGTWSLAGIRDKGAGFE----YGVAPLPAGKGKKGATPAGGASLVIPKGSSkKKEAAWEFIKFLTS--PENQAKWAKAT 310

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1540151759 344 AKAPVKT--PESISTFFGGQDVYAEFTKANAAVNSKFGFMPTWPSLTDPMTQAAEAAGKGTGKVDDIFQSAQKTA 416
Cdd:cd14748   311 GYLPVRKsaAEDPEEFLAENPNYKVAVDQLDYAKPWGPPVPNGAEIRDELNEALEAALLGKKTPEEALKEAQEKI 385
MalE COG2182
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];
1-422 8.26e-29

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


Pssm-ID: 441785 [Multi-domain]  Cd Length: 410  Bit Score: 116.59  E-value: 8.26e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540151759   1 MKKH--ALAASMLAFAMIVAGC----SATSSSGSSSSDGVIRYVHRLPDGEGMtkvNDIVARWNAEhPDMKVEATKFDgk 74
Cdd:COG2182     1 MKRRllAALALALALALALAACgsgsSSSGSSSAAGAGGTLTVWVDDDEAEAL---EEAAAAFEEE-PGIKVKVVEVP-- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540151759  75 ASDMNVKLENDVKAGTGPCLAQVGYAEIPKLYSSGLLADVSQQAEKYKDhFSEGSMSLMTVGKTVVGLPQDSGPLVYFYN 154
Cdd:COG2182    75 WDDLREKLTTAAPAGKGPDVFVGAHDWLGELAEAGLLAPLDDDLADKDD-FLPAALDAVTYDGKLYGVPYAVETLALYYN 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540151759 155 KAAFDQlglSVPTTSAELADVAQKAAAQGKYAVAFEPDEAPNTLagqsaaagaQWFSA---------ENDKWKVNVNSPE 225
Cdd:COG2182   154 KDLVKA---EPPKTWDELIAAAKKLTAAGKYGLAYDAGDAYYFY---------PFLAAfggylfgkdGDDPKDVGLNSPG 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540151759 226 TAKVSTFWQGLLDSKTALVANRWDDAFGkALVDQQLIGTIGAAWEGALLADTMKDspnagSWAVAQLPAF-GDTPMSGPD 304
Cdd:COG2182   222 AVAALEYLKDLIKDGVLPADADYDAADA-LFAEGKAAMIINGPWAAADLKKALGI-----DYGVAPLPTLaGGKPAKPFV 295

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540151759 305 GGSGVAVLKGCSNPEGAMAFNDWFNT---QVDDLATQGLVLTAKAPVKTPESIStffgGQDVYAEFTKANAAVnskfgFM 381
Cdd:COG2182   296 GVKGFGVSAYSKNKEAAQEFAEYLTSpeaQKALFEATGRIPANKAAAEDAEVKA----DPLIAAFAEQAEYAV-----PM 366

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 1540151759 382 PTWPSLT---DPMTQAAEAAGKGTGKVDDIFQSAQKTAVSSLKD 422
Cdd:COG2182   367 PNIPEMGavwTPLGTALQAIASGKADPAEALDAAQKQIEAAIAQ 410
PBP2_XBP1_like cd14749
The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; ...
 35-416 4.04e-23

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: 100.15  E-value: 4.04e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540151759  35 IRYVHRLPDGEGMTKVNDIVARWNAEHPDMKVEATKFDGkaSDMNVKLENDVKAGTGPCLAQV-GYAEIPKLYSSGLLAD 113
Cdd:cd14749     2 ITYWQYFTGDTKKKYMDELIADFEKENPNIKVKVVVFPY--DNYKTKLKTAVAAGEGPDVFNLwPGGWLAEFVKAGLLLP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540151759 114 VSQQA--EKYKDHFSEGSMSLMTVGKTVVGLPQDSGPLVYFYNKAAFDQLG-LSVPTTSAELADVAQKAAAQGKYAVAFe 190
Cdd:cd14749    80 LTDYLdpNGVDKRFLPGLADAVTFNGKVYGIPFAARALALFYNKDLFEEAGgVKPPKTWDELIEAAKKDKFKAKGQTGF- 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540151759 191 pdeapntlagqSAAAGAQWFSAENDKWkvnvnspetakvstFWQGLLDSKTALVANRW---DDAFGKA---LVDQQLIGT 264
Cdd:cd14749   159 -----------GLLLGAQGGHWYFQYL--------------VRQAGGGPLSDDGSGKAtfnDPAFVQAlqkLQDLVKAGA 213

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540151759 265 IGAAWEGALLADTMKD-------SPNAGSWA----VAQLPAF------------GDTPMSGPDGGSGVAVLKGCSNPEGA 321
Cdd:cd14749   214 FQEGFEGIDYDDAGQAfaqgkaaMNIGGSWDlgaiKAGEPGGkigvfpfptvgkGAQTSTIGGSDWAIAISANGKKKEAA 293

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540151759 322 MAFNDWFNTQvdDLATQGLVLTAKAPVKTPESISTFFGGQDVYAEFTKANAAVNSKFGFMPTWPSLTDPMTQAAEAAGKG 401
Cdd:cd14749   294 VKFLKYLTSP--EVMKQYLEDVGLLPAKEVVAKDEDPDPVAILGPFADVLNAAGSTPFLDEYWPAAAQVHKDAVQKLLTG 371

                         410
                  ....*....|....*
gi 1540151759 402 TGKVDDIFQSAQKTA 416
Cdd:cd14749   372 KIDPEQVVKQAQSAA 386
PBP2_MalE cd14747
Maltose-binding protein MalE; possesses type 2 periplasmic binding fold; This group includes ...
 49-416 2.76e-19

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: 88.91  E-value: 2.76e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540151759  49 KVNDIVARWNAEHPDMKVEATKFDgkASDMNVKLENDVKAGTGPCLAQVGYAEIPKLYSSGLLADVSQQAEKYK--DHFS 126
Cdd:cd14747    15 LLKELADEFEKENPGIEVKVQVLP--WGDAHTKITTAAASGDGPDVVQLGNTWVAEFAAMGALEDLTPYLEDLGgdKDLF 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540151759 127 EGSMSLMTVGKTVVGLPQDSGPLVYFYNKAAFDQLGLS-VPTTSAELADVAQKAAAQG--KYAVAFEPDEApntlagqsa 203
Cdd:cd14747    93 PGLVDTGTVDGKYYGVPWYADTRALFYRTDLLKKAGGDeAPKTWDELEAAAKKIKADGpdVSGFAIPGKND--------- 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540151759 204 aagaQWFS------------AENDKWKVNVNSPETAKVSTFWQGLLDSKTALVANRWDDA-FGKALVDQQLIGTIGAAWE 270
Cdd:cd14747   164 ----VWHNalpfvwgaggdlATKDKWKATLDSPEAVAGLEFYTSLYQKGLSPKSTLENSAdVEQAFANGKVAMIISGPWE 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540151759 271 GALLADTMKDSpnAGSWAVAQLPAFGDTPMSGPDGGSGVAVLKGCSNPEGAMAFNDWF--NTQVDDLATQGLVLTAKAPV 348
Cdd:cd14747   240 IGAIREAGPDL--AGKWGVAPLPGGPGGGSPSFAGGSNLAVFKGSKNKDLAWKFIEFLssPENQAAYAKATGMLPANTSA 317

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540151759 349 KTPESISTffggQDVYAEFtkANAAVNSKFG-FMPTWPSLTDPMTQAAEAAGKGTGK-VDDIFQSAQKTA 416
Cdd:cd14747   318 WDDPSLAN----DPLLAVF--AEQLKTGKATpATPEWGEIEAELVLVLEEVWIGVGAdVEDALDKAAAEI 381
PBP2_GacH cd14751
The periplasmic-binding component of the putative oligosacchride ABC transporter GacHFG; ...
 35-407 3.58e-19

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: 88.59  E-value: 3.58e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540151759  35 IRYVHRLPDGEGMTKvNDIVARWNAEHPDMKVEATK--FDGKasdMNVKLENdVKAGTGPCLAQVGYAEIPKLYSSGLLA 112
Cdd:cd14751     2 ITFWHTSSDEEKVLY-EKLIPAFEKEYPKIKVKAVRvpFDGL---HNQIKTA-AAGGQAPDVMRADIAWVPEFAKLGYLQ 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540151759 113 DVSQQA--EKYKDHFsEGSMSLMTVGKTVVGLPQDSGPLVYFYNKAAFDQLGLSVPTTSAELADVAQKAA-AQGKYAVAF 189
Cdd:cd14751    77 PLDGTPafDDIVDYL-PGPMETNRYNGHYYGVPQVTNTLALFYNKRLLEEAGTEVPKTMDELVAAAKAIKkKKGRYGLYI 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540151759 190 EPDEApntlagqsaaagaqWFSA-----------ENDKWKVNVNSPETAKVSTFWQGLLDSKTALVANR-WDDAFGKALV 257
Cdd:cd14751   156 SGDGP--------------YWLLpflwsfggdltDEKKATGYLNSPESVRALETIVDLYDEGAITPCASgGYPNMQDGFK 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540151759 258 DQQLIGTIGAAWEGALLADTMKDSPnAGSWAVAQLPAfGDTPMSGPDGGSGVAVLKGCSNPEGAMAFNDWFN---TQVDD 334
Cdd:cd14751   222 SGRYAMIVNGPWAYADILGGKEFKD-PDNLGIAPVPA-GPGGSGSPVGGEDLVIFKGSKNKDAAWKFVKFMSsaeAQALT 299

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1540151759 335 LATQGLVLTAKAPVKTPESIstffgGQDVYAEFTKA-NAAVNSKfgFMPTWPSLTDPMTQAAEAAGKGTGKVDD 407
Cdd:cd14751   300 AAKLGLLPTRTSAYESPEVA-----NNPMVAAFKPAlETAVPRP--PIPEWGELFEPLTLAFAKVLRGEKSPRE 366
PBP2_TMBP cd14750
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose; ...
 34-415 6.11e-17

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: 81.96  E-value: 6.11e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540151759  34 VIRYVHRLPDGEGMTKVndiVARWNAEHPDMKVEATKFDGKASDMNVKLENDVKAGTGPC-LAQVGYAEIPKLYSSGLLA 112
Cdd:cd14750     3 TFAAGSDGQEGELLKKA---IAAFEKKHPDIKVEIEELPASSDDQRQQLVTALAAGSSAPdVLGLDVIWIPEFAEAGWLL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540151759 113 DVSQQAEKYKDH-FSEGSMSLMTVGKTVVGLPQ--DSGplVYFYNKAAFDQLGLSVPTTSAELADVAQKAAAQGK----Y 185
Cdd:cd14750    80 PLTEYLKEEEDDdFLPATVEANTYDGKLYALPWftDAG--LLYYRKDLLEKYGPEPPKTWDELLEAAKKRKAGEPgiwgY 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540151759 186 AVAFEPDEAPNTlagqsaaAGAQWFSA------ENDKWKVNVNSPETAKVSTFWQGLLDSKtalVANRWDDAFGKALVDQ 259
Cdd:cd14750   158 VFQGKQYEGLVC-------NFLELLWSnggdifDDDSGKVTVDSPEALEALQFLRDLIGEG---ISPKGVLTYGEEEARA 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540151759 260 QLI-GTIGAA--WEGALLADTMKDSPNAGSWAVAQLPAFGDTPMSGPDGGSGVAVLKGCSNPEGAMAFNDWFNT---QVD 333
Cdd:cd14750   228 AFQaGKAAFMrnWPYAYALLQGPESAVAGKVGVAPLPAGPGGGSASTLGGWNLAISANSKHKEAAWEFVKFLTSpevQKR 307

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540151759 334 DLATQGLVLTAKAPVKTPESISTFFGGQDVYAEFTKANAAVNSkfgfmPTWPSLTDPMTQAAEAAGKGTGKVDDIFQSAQ 413
Cdd:cd14750   308 RAINGGLPPTRRALYDDPEVLEAYPFLPALLEALENAVPRPVT-----PKYPEVSTAIQIALSAALSGQATPEEALKQAQ 382


                  ..
gi 1540151759 414 KT 415
Cdd:cd14750   383 EK 384
SBP_bac_1 pfam01547
Bacterial extracellular solute-binding protein; This family also includes the bacterial ...
 42-330 4.43e-16

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: 78.23  E-value: 4.43e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540151759  42 PDGEGMTKVNDIVARWNAEHPDMKVEATkfDGKASDMNVKLENDVKAGTGPC-LAQVGYAEIPKLYSSGLLADVSQQAEK 120
Cdd:pfam01547   2 ASLTEAAALQALVKEFEKEHPGIKVEVE--SVGSGSLAQKLTTAIAAGDGPAdVFASDNDWIAELAKAGLLLPLDDYVAN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540151759 121 YkdhfsegsmsLMTVGKTVVGLPQDSGPLVYFYNKAAFDQLGLSVPTTSAELADVAQKAAAQGKYAVAFEPDEAPNTLAG 200
Cdd:pfam01547  80 Y----------LVLGVPKLYGVPLAAETLGLIYNKDLFKKAGLDPPKTWDELLEAAKKLKEKGKSPGGAGGGDASGTLGY 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540151759 201 QSAAAGAQWFSAENDKWKVNVNSPETAKVSTFWQGLLDSKTALVANRWDDA-----------FGKALVDQQLIGT---IG 266
Cdd:pfam01547 150 FTLALLASLGGPLFDKDGGGLDNPEAVDAITYYVDLYAKVLLLKKLKNPGVagadgrealalFEQGKAAMGIVGPwaaLA 229

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1540151759 267 AAWEGALLADTMKDSPNAGSWAVAQLPAFGDtpmsGPDGGSGVAVLKGCSNPEGAMAFNDWFNT 330
Cdd:pfam01547 230 ANKVKLKVAFAAPAPDPKGDVGYAPLPAGKG----GKGGGYGLAIPKGSKNKEAAKKFLDFLTS 289
PBP2_Maltose_binding_like cd13586
The periplasmic-binding component of ABC transport systems specific for maltose and related ...
 50-416 3.71e-11

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: 64.24  E-value: 3.71e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540151759  50 VNDIVARWNAEHpDMKVEATKfdGKASDMNVKLENDVKAGTGPCLAQVGYAEIPKLYSSGLLADVSQQAEKyKDHFSEGS 129
Cdd:cd13586    15 LKELAEEFEKKY-GIKVEVVY--VDSGDTREKFITAGPAGKGPDVFFGPHDWLGELAAAGLLAPIPEYLAV-KIKNLPVA 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540151759 130 MSLMTVGKTVVGLPQDSGPLVYFYNKaafdQLGLSVPTTSAELADVAQK--AAAQGKYAVAFEPDEAPNTlagqsaaagA 207
Cdd:cd13586    91 LAAVTYNGKLYGVPVSVETIALFYNK----DLVPEPPKTWEELIALAKKfnDKAGGKYGFAYDQTNPYFS---------Y 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540151759 208 QWFSA---------ENDKWKVNVNSPETAKVSTFWQGLLDSKTALVANRWDDAFGKALVDQQLIGTIGAAWEgalLADTM 278
Cdd:cd13586   158 PFLAAfggyvfgenGGDPTDIGLNNEGAVKGLKFIKDLKKKYKVLPPDLDYDIADALFKEGKAAMIINGPWD---LADYK 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540151759 279 KDSPNagsWAVAQLPAF-GDTPMSGPDGGSGVAVLKGCSNPEGAMAFNDWFNTqvdDLATQGLVLTA-KAPVKTPESIST 356
Cdd:cd13586   235 DAGIN---FGVAPLPTLpGGKQAAPFVGVQGAFVSAYSKNKEAAVEFAEYLTS---DEAQLLLFEKTgRIPALKDALNDA 308

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1540151759 357 FFGGQDVYAEFTKAnaavnSKFGF-MPTWP---SLTDPMTQAAEAAGKGTGKVDDIFQSAQKTA 416
Cdd:cd13586   309 AVKNDPLVKAFAEQ-----AQYGVpMPNIPemaAVWDAMGNALNLVASGKATPEEAAKDAVAAI 367
PBP2_AlgQ_like_1 cd13580
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 98-340 5.83e-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: 270298 [Multi-domain]  Cd Length: 471  Bit Score: 63.89  E-value: 5.83e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540151759  98 GYAEIPKLYSSGLLADVSQQAEKY-----KDHFSEGSMSLMTVGKtVVGLPQ---DSGPLVYFYNKAAFDQLGLSVPTTS 169
Cdd:cd13580    67 DPQLSITLVKQGALWDLTDYLDKYypnlkKIIEQEGWDSASVDGK-IYGIPRkrpLIGRNGLWIRKDWLDKLGLEVPKTL 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540151759 170 AELADVAQKAAAQ-----GK---YAVAfepdeAPNTLAGQSAAAGAQWFSAENDKWKVNVN--------SPETAKVSTFW 233
Cdd:cd13580   146 DELYEVAKAFTEKdpdgnGKkdtYGLT-----DTKDLIGSGFTGLFGAFGAPPNNWWKDEDgklvpgsiQPEMKEALKFL 220

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540151759 234 Q-----GLLDSKTALvaNRWDDAfgKALVDQQLIG-TIGAAWEGALLADTMKDS-PNAgswAVAQLPAF----GDTPMSG 302
Cdd:cd13580   221 KklykeGLIDPEFAV--NDGTKA--NEKFISGKAGiFVGNWWDPAWPQASLKKNdPDA---EWVAVPIPsgpdGKYGVWA 293

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1540151759 303 PDGGSG-VAVLKGCSNPEGAMAFNDWFNTQ-VDDLATQGL 340
Cdd:cd13580   294 ESGVNGfFVIPKKSKKPEAILKLLDFLSDPeVQKLLDYGI 333
PBP2_ABC_oligosaccharides cd13522
The periplasmic-binding component of ABC transport systems specific for maltose and related ...
 50-333 9.30e-10

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: 60.12  E-value: 9.30e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540151759  50 VNDIVARWNAEHPDMKVEATKfdgKASDMNVKLENDVKAG-TGPCLAQVGYAEIPKLYSSGLLADVSQ-QAEKYKDHFSe 127
Cdd:cd13522    16 VNELIAKFEKAYPGITVEVTY---QDTEARRQFFSTAAAGgKGPDVVFGPSDSLGPFAAAGLLAPLDEyVSKSGKYAPN- 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540151759 128 gSMSLMTVGKTVVGLPQDSGPLVYFYNKaafDQLGLSVPTTSAELADVAQKAAAQGKYAVAFEPDEaPNTLAGQSAAAGA 207
Cdd:cd13522    92 -TIAAMKLNGKLYGVPVSVGAHLMYYNK---KLVPKNPPKTWQELIALAQGLKAKNVWGLVYNQNE-PYFFAAWIGGFGG 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540151759 208 QWFSAENDKWKVNVNSPETAKVSTFWQGLLDSKTALVANRWDDAFGKALVDQQLIGTIGAAWEGALLADTMKDspNAGsw 287
Cdd:cd13522   167 QVFKANNGKNNPTLDTPGAVEALQFLVDLKSKYKIMPPETDYSIADALFKAGKAAMIINGPWDLGDYRQALKI--NLG-- 242

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1540151759 288 aVAQLPAFGDTPMSGP-DGGSGVAVLKGCSNPEGAMAFNDWF-NTQVD 333
Cdd:cd13522   243 -VAPLPTFSGTKHAAPfVGGKGFGINKESQNKAAAVEFVKYLtSYQAQ 289
PBP2_Maltodextrin cd13657
The periplasmic binding component of ABC transport system specific for maltodextrin; This ...
 52-414 6.02e-09

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: 57.39  E-value: 6.02e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540151759  52 DIVARWNAEHPDMKVEATkFDGKASDMNvKLENDVKAGTGPCLaqVGYAE--IPKLYSSGLLADVSQQ-AEKYKDHFSEG 128
Cdd:cd13657    18 QIIDEFEAKYPVPNVKVP-FEKKPDLQN-KLLTAIPAGEGPDL--FIWAHdwIGQFAEAGLLVPISDYlSEDDFENYLPT 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540151759 129 SMSLMTVGKTVVGLPQDSGPLVYFYNKAAFDQLglsvPTTSAELADVAQK--AAAQGKYAVAFePDEAPNTLAGQSAAAG 206
Cdd:cd13657    94 AVEAVTYKGKVYGLPEAYETVALIYNKALVDQP----PETTDELLAIMKDhtDPAAGSYGLAY-QVSDAYFVSAWIFGFG 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540151759 207 AQWFSAENDKwkVNVNSPETAKVSTFwqgLLDSKTALVANRWDDAFGKAL-VDQQLIGTIGAAWEGALLADTMKDspnag 285
Cdd:cd13657   169 GYYFDDETDK--PGLDTPETIKGIQF---LKDFSWPYMPSDPSYNTQTSLfNEGKAAMIINGPWFIGGIKAAGID----- 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540151759 286 sWAVAQLPAFGDTPMSGPDGG---SGVAVLKGCSNPEGAMAFNDWFnTQVDDLATQGLVLTAkAPVKTPESISTFFGGQD 362
Cdd:cd13657   239 -LGVAPLPTVDGTNPPRPYSGvegIYVTKYAERKNKEAALDFAKFF-TTAEASKILADENGY-VPAATNAYDDAEVAADP 315

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1540151759 363 VYAEFTK-ANAAVNskfgfMPTWPSLT---DPMTQAAEAAGKGTGKVDDIFQSAQK 414
Cdd:cd13657   316 VIAAFKAqAEHGVP-----MPNSPEMAsvwGPVTLALAAVYQGGQDPQEALAAAQQ 366
SBP_bac_8 pfam13416
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 52-330 5.45e-07

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


Pssm-ID: 433189 [Multi-domain]  Cd Length: 281  Bit Score: 50.87  E-value: 5.45e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540151759  52 DIVARWNAEHpDMKVEATKFDGkaSDMNVKLENDVKAGTGP--CLAQVGYAEIPKLYSSGLLADVSQqaEKYKDHFSEGS 129
Cdd:pfam13416   1 ALAKAFEKKT-GVTVEVEPQAS--NDLQAKLLAAAAAGNAPdlDVVWIAADQLATLAEAGLLADLSD--VDNLDDLPDAL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540151759 130 MSLMTVGKTVVGLPQDSGPLVYFYNKAAFDQLGlSVPTTSAELADVAQKaaAQGKYAVAFEPDeapntlagqSAAAGAQW 209
Cdd:pfam13416  76 DAAGYDGKLYGVPYAASTPTVLYYNKDLLKKAG-EDPKTWDELLAAAAK--LKGKTGLTDPAT---------GWLLWALL 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540151759 210 FSAENDKwKVNVNSPETAKVSTFWQGLLDSKTalVANRWDDAfGKALVDQQLIGTIGAAWEgalLADTMKDSPNagsWAV 289
Cdd:pfam13416 144 ADGVDLT-DDGKGVEALDEALAYLKKLKDNGK--VYNTGADA-VQLFANGEVAMTVNGTWA---AAAAKKAGKK---LGA 213

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1540151759 290 AQLpafgdtPMSGPDGGSGVAVLKGCSNPE-GAMAFNDWFNT 330
Cdd:pfam13416 214 VVP------KDGSFLGGKGLVVPAGAKDPRlAALDFIKFLTS 249
PBP2_CMBP cd13658
The periplasmic binding component of ABC transport systems specific for cyclo/maltodextrin; ...
 77-330 7.84e-07

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: 50.94  E-value: 7.84e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540151759  77 DMNVKLEN---DVKAGTGPCLAQVGYAEIPKLYSSGLLADVSQQAEKyKDHFSEGSMSLMTVGKTVVGLPQDSGPLVYFY 153
Cdd:cd13658    36 DQLDQLEKlslDGPAGKGPDVMVAPHDRIGSAVLQGLLSPIKLSKDK-KKGFTDQALKALTYDGKLYGLPAAVETLALYY 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540151759 154 NKAAFDQlglsVPTTSAELADVAQKAA--AQGKYAVAFEPDEAPNTLAGQSAAAGAQWfsAENDK----WKVNVNSPETA 227
Cdd:cd13658   115 NKDLVKN----APKTFDELEALAKDLTkeKGKQYGFLADATNFYYSYGLLAGNGGYIF--KKNGSdldiNDIGLNSPGAV 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540151759 228 KVSTFWQGLLDSKtalvanRWDDAFGKALVDQQLI-GTIGAAWEGALLADTMKDspnAG-SWAVAQLPAFGDT-PMSGPD 304
Cdd:cd13658   189 KAVKFLKKWYTEG------YLPKGMTGDVIQGLFKeGKAAAVIDGPWAIQEYQE---AGvNYGVAPLPTLPNGkPMAPFL 259

                         250       260
                  ....*....|....*....|....*.
gi 1540151759 305 GGSGVAVLKGCSNPEGAMAFNDWFNT 330
Cdd:cd13658   260 GVKGWYLSAYSKHKEWAQKFMEFLTS 285
PRK10974 PRK10974
sn-glycerol-3-phosphate ABC transporter substrate-binding protein UgpB;
35-183 1.29e-03

sn-glycerol-3-phosphate ABC transporter substrate-binding protein UgpB;


Pssm-ID: 182876 [Multi-domain]  Cd Length: 438  Bit Score: 40.94  E-value: 1.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540151759  35 IRYVHRLpDGEGMTKVNDIVARWNAEHPDMKVEATkFDGKASDMNVKLENDVKAGTGPCLAQVGYAEIPKLYSSGLLADV 114
Cdd:PRK10974   28 IPFWHSM-EGELGKEVDSLAQRFNASQPDYKIVPV-YKGNYEQSLAAGIAAFRSGNAPAILQVYEVGTATMMASKAIKPV 105

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1540151759 115 SQQAEKYKDHFSEGSM-----SLMTVGKT--VVGLPQDSGPLVYFYNKAAFDQLGL---SVPTTSAELADVAQKAAAQG 183
Cdd:PRK10974  106 YDVFKDAGIPFDESQFvptvaGYYSDAKTghLLSQPFNSSTPVLYYNKDAFKKAGLdpeQPPKTWQDLAAYAAKLRAAG 184
 
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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