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Conserved domains on  [gi|1934296053|ref|WP_195506773|]
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ABC transporter substrate-binding protein [Bifidobacterium pseudocatenulatum]

Protein Classification

ABC transporter substrate-binding protein( domain architecture ID 11447308)

ABC transporter substrate-binding protein functions as the initial receptor in the ABC transport of one or more from a variety of substrates including carbohydrates

Gene Ontology:  GO:0140359|GO:0042626|GO:0055052
PubMed:  26517916|24638992|25750732|26517916
SCOP:  3000083
TCDB:  3.A.1

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
 18-359 1.13e-50

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


:

Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 174.85  E-value: 1.13e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934296053  18 RALTATCAIALTAGLAGCGNST------AGTVTLDFFQFKAEAADWFTAKAKEFEKTHPSIKVNVNN--SSDATTDLRTR 89
Cdd:COG1653     2 RRLALALAAALALALAACGGGGsgaaaaAGKVTLTVWHTGGGEAAALEALIKEFEAEHPGIKVEVESvpYDDYRTKLLTA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934296053  90 LVKNREPDVITINGDiNFGMLAEAGVFHDFtdDDIVDELNPGMVNIAKSLVQTNdESKKRLYGLPYAGNASGYIINADVW 169
Cdd:COG1653    82 LAAGNAPDVVQVDSG-WLAEFAAAGALVPL--DDLLDDDGLDKDDFLPGALDAG-TYDGKLYGVPFNTDTLGLYYNKDLF 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934296053 170 EEAGEDpdnPPQTWSEFIDLLQRFKSK-GIVPIEASTADPWTLQAPLASLNSTLVpeseylsLKDGSKKF-SDLWGTVSD 247
Cdd:COG1653   158 EKAGLD---PPKTWDELLAAAKKLKAKdGVYGFALGGKDGAAWLDLLLSAGGDLY-------DEDGKPAFdSPEAVEALE 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934296053 248 QLVEIYQN-YTQKNPA-VTYQQATQDLAAGKAAILPLGTYAIPQIRLINSDANLRFAQMPATDDASEQQLTAGDDViLTM 325
Cdd:COG1653   228 FLKDLVKDgYVPPGALgTDWDDARAAFASGKAAMMINGSWALGALKDAAPDFDVGVAPLPGGPGGKKPASVLGGSG-LAI 306

                         330       340       350
                  ....*....|....*....|....*....|....
gi 1934296053 326 GAHTKHEKEAREFIGFLMNDENIKDYSKQQSAFT 359
Cdd:COG1653   307 PKGSKNPEAAWKFLKFLTSPEAQAKWDALQAVLL 340
 
Name Accession Description Interval E-value
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
 18-359 1.13e-50

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


Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 174.85  E-value: 1.13e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934296053  18 RALTATCAIALTAGLAGCGNST------AGTVTLDFFQFKAEAADWFTAKAKEFEKTHPSIKVNVNN--SSDATTDLRTR 89
Cdd:COG1653     2 RRLALALAAALALALAACGGGGsgaaaaAGKVTLTVWHTGGGEAAALEALIKEFEAEHPGIKVEVESvpYDDYRTKLLTA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934296053  90 LVKNREPDVITINGDiNFGMLAEAGVFHDFtdDDIVDELNPGMVNIAKSLVQTNdESKKRLYGLPYAGNASGYIINADVW 169
Cdd:COG1653    82 LAAGNAPDVVQVDSG-WLAEFAAAGALVPL--DDLLDDDGLDKDDFLPGALDAG-TYDGKLYGVPFNTDTLGLYYNKDLF 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934296053 170 EEAGEDpdnPPQTWSEFIDLLQRFKSK-GIVPIEASTADPWTLQAPLASLNSTLVpeseylsLKDGSKKF-SDLWGTVSD 247
Cdd:COG1653   158 EKAGLD---PPKTWDELLAAAKKLKAKdGVYGFALGGKDGAAWLDLLLSAGGDLY-------DEDGKPAFdSPEAVEALE 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934296053 248 QLVEIYQN-YTQKNPA-VTYQQATQDLAAGKAAILPLGTYAIPQIRLINSDANLRFAQMPATDDASEQQLTAGDDViLTM 325
Cdd:COG1653   228 FLKDLVKDgYVPPGALgTDWDDARAAFASGKAAMMINGSWALGALKDAAPDFDVGVAPLPGGPGGKKPASVLGGSG-LAI 306

                         330       340       350
                  ....*....|....*....|....*....|....
gi 1934296053 326 GAHTKHEKEAREFIGFLMNDENIKDYSKQQSAFT 359
Cdd:COG1653   307 PKGSKNPEAAWKFLKFLTSPEAQAKWDALQAVLL 340
PBP2_XBP1_like cd14749
The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; ...
 42-353 5.11e-33

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: 128.27  E-value: 5.11e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934296053  42 TVTLDFFQFKAEAADWFTAKAKEFEKTHPSIKVNVNN--SSDATTDLRTRLVKNREPDVITINGDINFGMLAEAGVFHDF 119
Cdd:cd14749     1 TITYWQYFTGDTKKKYMDELIADFEKENPNIKVKVVVfpYDNYKTKLKTAVAAGEGPDVFNLWPGGWLAEFVKAGLLLPL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934296053 120 TDDDIVDELNPGMVNIAKSLVQTNDEskkrLYGLPYAGNASGYIINADVWEEAGedPDNPPQTWSEFIDLLQRFKSKGIV 199
Cdd:cd14749    81 TDYLDPNGVDKRFLPGLADAVTFNGK----VYGIPFAARALALFYNKDLFEEAG--GVKPPKTWDELIEAAKKDKFKAKG 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934296053 200 PIEASTADPWtlqAPLASLNSTLV------PESEYLSlkdGSKKFSDLWGTVSDQLVEIYQN--YTQKN-PAVTYQQATQ 270
Cdd:cd14749   155 QTGFGLLLGA---QGGHWYFQYLVrqagggPLSDDGS---GKATFNDPAFVQALQKLQDLVKagAFQEGfEGIDYDDAGQ 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934296053 271 DLAAGKAAILPLGTYAIPQIRLINSDANLRFAQMPATDDASEQQLTAGDDVILTMGAHTKHEKEAREFIGFLMNDENIKD 350
Cdd:cd14749   229 AFAQGKAAMNIGGSWDLGAIKAGEPGGKIGVFPFPTVGKGAQTSTIGGSDWAIAISANGKKKEAAVKFLKYLTSPEVMKQ 308


                  ...
gi 1934296053 351 YSK 353
Cdd:cd14749   309 YLE 311
SBP_bac_1 pfam01547
Bacterial extracellular solute-binding protein; This family also includes the bacterial ...
 53-347 3.38e-25

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: 104.42  E-value: 3.38e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934296053  53 EAADWFTAKAKEFEKTHPSIKVNVNN--SSDATTDLRTRLVKNREP-DVITINGDiNFGMLAEAGVFHDFTDDDIVDeln 129
Cdd:pfam01547   5 TEAAALQALVKEFEKEHPGIKVEVESvgSGSLAQKLTTAIAAGDGPaDVFASDND-WIAELAKAGLLLPLDDYVANY--- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934296053 130 pgmvniakslvqtNDESKKRLYGLPYAGNASGYIINADVWEEAGEDpdnPPQTWSEFIDLLQRFKSKGIVPIEASTADPW 209
Cdd:pfam01547  81 -------------LVLGVPKLYGVPLAAETLGLIYNKDLFKKAGLD---PPKTWDELLEAAKKLKEKGKSPGGAGGGDAS 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934296053 210 --TLQAPLASLNSTLVPESEYLSLKDGSKKFSDLWGTVSDQLVEIYQNYTQKNPAV---TYQQATQDLAAGKAAILPLGT 284
Cdd:pfam01547 145 gtLGYFTLALLASLGGPLFDKDGGGLDNPEAVDAITYYVDLYAKVLLLKKLKNPGVagaDGREALALFEQGKAAMGIVGP 224

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1934296053 285 YAIPQIRLINSDANLRFAQMPATDD---ASEQQLTAGDDVILTMG--AHTKHEKEAREFIGFLMNDEN 347
Cdd:pfam01547 225 WAALAANKVKLKVAFAAPAPDPKGDvgyAPLPAGKGGKGGGYGLAipKGSKNKEAAKKFLDFLTSPEA 292
 
Name Accession Description Interval E-value
UgpB COG1653
ABC-type glycerol-3-phosphate transport system, periplasmic component [Carbohydrate transport ...
 18-359 1.13e-50

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


Pssm-ID: 441259 [Multi-domain]  Cd Length: 363  Bit Score: 174.85  E-value: 1.13e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934296053  18 RALTATCAIALTAGLAGCGNST------AGTVTLDFFQFKAEAADWFTAKAKEFEKTHPSIKVNVNN--SSDATTDLRTR 89
Cdd:COG1653     2 RRLALALAAALALALAACGGGGsgaaaaAGKVTLTVWHTGGGEAAALEALIKEFEAEHPGIKVEVESvpYDDYRTKLLTA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934296053  90 LVKNREPDVITINGDiNFGMLAEAGVFHDFtdDDIVDELNPGMVNIAKSLVQTNdESKKRLYGLPYAGNASGYIINADVW 169
Cdd:COG1653    82 LAAGNAPDVVQVDSG-WLAEFAAAGALVPL--DDLLDDDGLDKDDFLPGALDAG-TYDGKLYGVPFNTDTLGLYYNKDLF 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934296053 170 EEAGEDpdnPPQTWSEFIDLLQRFKSK-GIVPIEASTADPWTLQAPLASLNSTLVpeseylsLKDGSKKF-SDLWGTVSD 247
Cdd:COG1653   158 EKAGLD---PPKTWDELLAAAKKLKAKdGVYGFALGGKDGAAWLDLLLSAGGDLY-------DEDGKPAFdSPEAVEALE 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934296053 248 QLVEIYQN-YTQKNPA-VTYQQATQDLAAGKAAILPLGTYAIPQIRLINSDANLRFAQMPATDDASEQQLTAGDDViLTM 325
Cdd:COG1653   228 FLKDLVKDgYVPPGALgTDWDDARAAFASGKAAMMINGSWALGALKDAAPDFDVGVAPLPGGPGGKKPASVLGGSG-LAI 306

                         330       340       350
                  ....*....|....*....|....*....|....
gi 1934296053 326 GAHTKHEKEAREFIGFLMNDENIKDYSKQQSAFT 359
Cdd:COG1653   307 PKGSKNPEAAWKFLKFLTSPEAQAKWDALQAVLL 340
PBP2_XBP1_like cd14749
The periplasmic-binding component of ABC transport systems specific for xylo-oligosaccharides; ...
 42-353 5.11e-33

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: 128.27  E-value: 5.11e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934296053  42 TVTLDFFQFKAEAADWFTAKAKEFEKTHPSIKVNVNN--SSDATTDLRTRLVKNREPDVITINGDINFGMLAEAGVFHDF 119
Cdd:cd14749     1 TITYWQYFTGDTKKKYMDELIADFEKENPNIKVKVVVfpYDNYKTKLKTAVAAGEGPDVFNLWPGGWLAEFVKAGLLLPL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934296053 120 TDDDIVDELNPGMVNIAKSLVQTNDEskkrLYGLPYAGNASGYIINADVWEEAGedPDNPPQTWSEFIDLLQRFKSKGIV 199
Cdd:cd14749    81 TDYLDPNGVDKRFLPGLADAVTFNGK----VYGIPFAARALALFYNKDLFEEAG--GVKPPKTWDELIEAAKKDKFKAKG 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934296053 200 PIEASTADPWtlqAPLASLNSTLV------PESEYLSlkdGSKKFSDLWGTVSDQLVEIYQN--YTQKN-PAVTYQQATQ 270
Cdd:cd14749   155 QTGFGLLLGA---QGGHWYFQYLVrqagggPLSDDGS---GKATFNDPAFVQALQKLQDLVKagAFQEGfEGIDYDDAGQ 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934296053 271 DLAAGKAAILPLGTYAIPQIRLINSDANLRFAQMPATDDASEQQLTAGDDVILTMGAHTKHEKEAREFIGFLMNDENIKD 350
Cdd:cd14749   229 AFAQGKAAMNIGGSWDLGAIKAGEPGGKIGVFPFPTVGKGAQTSTIGGSDWAIAISANGKKKEAAVKFLKYLTSPEVMKQ 308


                  ...
gi 1934296053 351 YSK 353
Cdd:cd14749   309 YLE 311
PBP2_UgpB cd14748
The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; ...
 62-365 5.91e-32

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: 125.10  E-value: 5.91e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934296053  62 AKEFEKTHPSIKVN-VNNSSDATTD--LRTRLVKNREPDVITInGDINFGMLAEAGVFHDFtdDDIVDELNPGMVNIAKS 138
Cdd:cd14748    20 VDEFNKSHPDIKVKaVYQGSYDDTLtkLLAALAAGTAPDVAQV-DASWVAQLADSGALEPL--DDYIDKDGVDDDDFYPA 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934296053 139 LVQTNDESKKrLYGLPYAGNASGYIINADVWEEAGEDPDNPPQTWSEFIDLLQRFKSK-------GIVPieASTADPWTL 211
Cdd:cd14748    97 ALDAGTYDGK-LYGLPFDTSTPVLYYNKDLFEEAGLDPEKPPKTWDELEEAAKKLKDKggktgryGFAL--PPGDGGWTF 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934296053 212 QAPLASLNSTLvpeseylslkdgskkFSDLWGTV---SDQLVEI---YQNYTQKN---PAVTYQQATQDLAAGKAAILPL 282
Cdd:cd14748   174 QALLWQNGGDL---------------LDEDGGKVtfnSPEGVEAlefLVDLVGKDgvsPLNDWGDAQDAFISGKVAMTIN 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934296053 283 GTYAIPQIRLINSDANLRFAQMPATDDasEQQLTAGDDVILTMGAH-TKHEKEAREFIGFLMNDENIKDYSKQQSAFTPY 361
Cdd:cd14748   239 GTWSLAGIRDKGAGFEYGVAPLPAGKG--KKGATPAGGASLVIPKGsSKKKEAAWEFIKFLTSPENQAKWAKATGYLPVR 316


                  ....
gi 1934296053 362 KDTY 365
Cdd:cd14748   317 KSAA 320
PBP2_TMBP_like cd13585
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and ...
 52-420 1.41e-31

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: 124.05  E-value: 1.41e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934296053  52 AEAADWFTAKAKEFEKTHPSIKVNV--NNSSDATTDLRTRLVKNREPDVITINGdINFGMLAEAGVFHDFTD----DDIV 125
Cdd:cd13585    10 PAETAALKKLIDAFEKENPGVKVEVvpVPYDDYWTKLTTAAAAGTAPDVFYVDG-PWVPEFASNGALLDLDDyiekDGLD 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934296053 126 DELNPGMVNIAKSlvqtndesKKRLYGLPYAGNASGYIINADVWEEAGEDPDnPPQTWSEFIDLLQRFKSKGI----VPI 201
Cdd:cd13585    89 DDFPPGLLDAGTY--------DGKLYGLPFDADTLVLFYNKDLFDKAGPGPK-PPWTWDELLEAAKKLTDKKGgqygFAL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934296053 202 EASTADPWTLQAPLASLNSTLvpeseylslkdgskkFSDLWGTV---SDQLVE--------IYQNYTQKNPAVTYQQATQ 270
Cdd:cd13585   160 RGGSGGQTQWYPFLWSNGGDL---------------LDEDDGKAtlnSPEAVEalqfyvdlYKDGVAPSSATTGGDEAVD 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934296053 271 DLAAGKAAILPLGTYAIPQIRLINSDANLRFAQMPATDDASEQQLTAGDDviLTMGAHTKHEKEAREFIGFLMNDENIKD 350
Cdd:cd13585   225 LFASGKVAMMIDGPWALGTLKDSKVKFKWGVAPLPAGPGGKRASVLGGWG--LAISKNSKHPEAAWKFIKFLTSKENQLK 302

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934296053 351 YSKQQSAFTPYKDTYV-------GDEALNGVLDFYQAGKLADFCDHYVPASINIAGFLQTLVQS---GNTEKFLNSMQSE 420
Cdd:cd13585   303 LGGAAGPAALAAAAASaaapdakPALALAAAADALAAAVPPPVPPPWPEVYPILSEALQEALLGalgKSPEEALKEAAKE 382
MalE COG2182
Maltose-binding periplasmic protein MalE [Carbohydrate transport and metabolism];
13-353 5.74e-28

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


Pssm-ID: 441785 [Multi-domain]  Cd Length: 410  Bit Score: 114.28  E-value: 5.74e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934296053  13 RRIVYRALTATCAIALTagLAGCGNST---------AGTVTLDFfQFKAEAADWFTAKAKEFEKThPSIKVNVNN--SSD 81
Cdd:COG2182     2 KRRLLAALALALALALA--LAACGSGSsssgsssaaGAGGTLTV-WVDDDEAEALEEAAAAFEEE-PGIKVKVVEvpWDD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934296053  82 ATTDLRTRLVKNREPDVITINGDiNFGMLAEAGVFHDFTDD-DIVDELNPGMVNIakslVQTNDEskkrLYGLPYAGNAS 160
Cdd:COG2182    78 LREKLTTAAPAGKGPDVFVGAHD-WLGELAEAGLLAPLDDDlADKDDFLPAALDA----VTYDGK----LYGVPYAVETL 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934296053 161 GYIINADVWeeagedPDNPPQTWSEFIDLLQRFKSKGIVPIEASTADPWTLQAPLASLNSTLVPESEYLSLK-----DGS 235
Cdd:COG2182   149 ALYYNKDLV------KAEPPKTWDELIAAAKKLTAAGKYGLAYDAGDAYYFYPFLAAFGGYLFGKDGDDPKDvglnsPGA 222

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934296053 236 KKFSDLWGTVSDQLVeiyqnytqKNPAVTYQQATQDLAAGKAAILPLGTYAIPQIRlINSDANLRFAQMPATDDASEQQL 315
Cdd:COG2182   223 VAALEYLKDLIKDGV--------LPADADYDAADALFAEGKAAMIINGPWAAADLK-KALGIDYGVAPLPTLAGGKPAKP 293

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1934296053 316 TAGddVI-LTMGAHTKHEKEAREFIGFLMNDENIKDYSK 353
Cdd:COG2182   294 FVG--VKgFGVSAYSKNKEAAQEFAEYLTSPEAQKALFE 330
SBP_bac_1 pfam01547
Bacterial extracellular solute-binding protein; This family also includes the bacterial ...
 53-347 3.38e-25

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: 104.42  E-value: 3.38e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934296053  53 EAADWFTAKAKEFEKTHPSIKVNVNN--SSDATTDLRTRLVKNREP-DVITINGDiNFGMLAEAGVFHDFTDDDIVDeln 129
Cdd:pfam01547   5 TEAAALQALVKEFEKEHPGIKVEVESvgSGSLAQKLTTAIAAGDGPaDVFASDND-WIAELAKAGLLLPLDDYVANY--- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934296053 130 pgmvniakslvqtNDESKKRLYGLPYAGNASGYIINADVWEEAGEDpdnPPQTWSEFIDLLQRFKSKGIVPIEASTADPW 209
Cdd:pfam01547  81 -------------LVLGVPKLYGVPLAAETLGLIYNKDLFKKAGLD---PPKTWDELLEAAKKLKEKGKSPGGAGGGDAS 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934296053 210 --TLQAPLASLNSTLVPESEYLSLKDGSKKFSDLWGTVSDQLVEIYQNYTQKNPAV---TYQQATQDLAAGKAAILPLGT 284
Cdd:pfam01547 145 gtLGYFTLALLASLGGPLFDKDGGGLDNPEAVDAITYYVDLYAKVLLLKKLKNPGVagaDGREALALFEQGKAAMGIVGP 224

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1934296053 285 YAIPQIRLINSDANLRFAQMPATDD---ASEQQLTAGDDVILTMG--AHTKHEKEAREFIGFLMNDEN 347
Cdd:pfam01547 225 WAALAANKVKLKVAFAAPAPDPKGDvgyAPLPAGKGGKGGGYGLAipKGSKNKEAAKKFLDFLTSPEA 292
PBP2_MalE cd14747
Maltose-binding protein MalE; possesses type 2 periplasmic binding fold; This group includes ...
 52-354 1.63e-24

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: 104.32  E-value: 1.63e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934296053  52 AEAADWFTAKAKEFEKTHPSIKVNVNNS--SDATTDLRTRLVKNREPDVITINGDINFGmLAEAGVFHDFTDDDIVDEln 129
Cdd:cd14747    10 SAEAELLKELADEFEKENPGIEVKVQVLpwGDAHTKITTAAASGDGPDVVQLGNTWVAE-FAAMGALEDLTPYLEDLG-- 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934296053 130 pGMVNIAKSLVQTNdESKKRLYGLPYAGNASGYIINADVWEEAGedPDNPPQTWSEFIDLLQRFKSKGI------VPI-- 201
Cdd:cd14747    87 -GDKDLFPGLVDTG-TVDGKYYGVPWYADTRALFYRTDLLKKAG--GDEAPKTWDELEAAAKKIKADGPdvsgfaIPGkn 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934296053 202 -EASTADPWTLQAplaslnstlvpESEYLSLKDGSKKFSDLwGTVS--DQLVEIYQN-YTQKNPAVTYQQATQDLAAGKA 277
Cdd:cd14747   163 dVWHNALPFVWGA-----------GGDLATKDKWKATLDSP-EAVAglEFYTSLYQKgLSPKSTLENSADVEQAFANGKV 230

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1934296053 278 AILPLGTYAIPQIRLINSDANLRF--AQMPATDDASEQQLTAGDDviLTMGAHTKHEKEAREFIGFLMNDENIKDYSKQ 354
Cdd:cd14747   231 AMIISGPWEIGAIREAGPDLAGKWgvAPLPGGPGGGSPSFAGGSN--LAVFKGSKNKDLAWKFIEFLSSPENQAAYAKA 307
SBP_bac_8 pfam13416
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
 62-369 4.25e-17

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


Pssm-ID: 433189 [Multi-domain]  Cd Length: 281  Bit Score: 80.91  E-value: 4.25e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934296053  62 AKEFEKTHPsIKVNV--NNSSDATTDLRTRLVKNREPDVITINGDIN-FGMLAEAGVFHDFTDDDIVDELNPgmvniAKS 138
Cdd:pfam13416   3 AKAFEKKTG-VTVEVepQASNDLQAKLLAAAAAGNAPDLDVVWIAADqLATLAEAGLLADLSDVDNLDDLPD-----ALD 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934296053 139 LVQTNDEskkrLYGLPYAGNASGYII-NADVWEEAGEDPdnppQTWSEFIDLLQRFKSKGIVPIEASTADPWTLQAplas 217
Cdd:pfam13416  77 AAGYDGK----LYGVPYAASTPTVLYyNKDLLKKAGEDP----KTWDELLAAAAKLKGKTGLTDPATGWLLWALLA---- 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934296053 218 lnstlvpeseylslkDGSKKFSDLWGTV-SDQLVEIYQNYTQKNPAVTYQ-QATQDLAAGKAAILPLGTYAIPQIRlins 295
Cdd:pfam13416 145 ---------------DGVDLTDDGKGVEaLDEALAYLKKLKDNGKVYNTGaDAVQLFANGEVAMTVNGTWAAAAAK---- 205

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1934296053 296 DANLRFAQMPATDdaseQQLTAGDDviLTMGAHTKHEKE-AREFIGFLMNDENIKDYSKQQSAFTPYKDTYVGDE 369
Cdd:pfam13416 206 KAGKKLGAVVPKD----GSFLGGKG--LVVPAGAKDPRLaALDFIKFLTSPENQAALAEDTGYIPANKSAALSDE 274
PBP2_TMBP cd14750
The periplasmic-binding component of ABC transport systems specific for trehalose/maltose; ...
 62-380 4.29e-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: 82.34  E-value: 4.29e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934296053  62 AKEFEKTHPSIKVNVN---NSSDATTD-LRTRL-VKNREPDVITINgDINFGMLAEAGVFHDFTDDDIVDELN---PGMV 133
Cdd:cd14750    20 IAAFEKKHPDIKVEIEelpASSDDQRQqLVTALaAGSSAPDVLGLD-VIWIPEFAEAGWLLPLTEYLKEEEDDdflPATV 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934296053 134 NiakslVQTNDEskkRLYGLPYAGNASGYIINADVWEEAGEdpdNPPQTWSEFIDLLQRFKSKGIVPI---------EAS 204
Cdd:cd14750    99 E-----ANTYDG---KLYALPWFTDAGLLYYRKDLLEKYGP---EPPKTWDELLEAAKKRKAGEPGIWgyvfqgkqyEGL 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934296053 205 TADPWTLqapLASLN-STLVPESEYLSL-----KDGSKKFSDL-WGTVSDQLVEIYQNytqknpavtyQQATQDLAAGKA 277
Cdd:cd14750   168 VCNFLEL---LWSNGgDIFDDDSGKVTVdspeaLEALQFLRDLiGEGISPKGVLTYGE----------EEARAAFQAGKA 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934296053 278 AILPLGTYAIPQIRLINSD--ANLRFAQMPATDDaSEQQLTAGddvILTMG--AHTKHEKEAREFIGFLMNDENIKDYSK 353
Cdd:cd14750   235 AFMRNWPYAYALLQGPESAvaGKVGVAPLPAGPG-GGSASTLG---GWNLAisANSKHKEAAWEFVKFLTSPEVQKRRAI 310

                         330       340
                  ....*....|....*....|....*..
gi 1934296053 354 QQSAFTPYKDTYVgDEALNGVLDFYQA 380
Cdd:cd14750   311 NGGLPPTRRALYD-DPEVLEAYPFLPA 336
PBP2_GacH cd14751
The periplasmic-binding component of the putative oligosacchride ABC transporter GacHFG; ...
 44-347 1.60e-11

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: 65.48  E-value: 1.60e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934296053  44 TLDFFQFKAEAADWFTAK-AKEFEKTHPSIKVNVNNSS--DATTDLRTRLVKNREPDVITIngDINF-GMLAEAGVFHD- 118
Cdd:cd14751     1 TITFWHTSSDEEKVLYEKlIPAFEKEYPKIKVKAVRVPfdGLHNQIKTAAAGGQAPDVMRA--DIAWvPEFAKLGYLQPl 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934296053 119 ---FTDDDIVDELnPGMVNIAKslvqtndeSKKRLYGLPYAGNASGYIINADVWEEAGEDpdnPPQTWSEFIDLLQRF-K 194
Cdd:cd14751    79 dgtPAFDDIVDYL-PGPMETNR--------YNGHYYGVPQVTNTLALFYNKRLLEEAGTE---VPKTMDELVAAAKAIkK 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934296053 195 SKGIVPIEASTADPWTLQAPLASLNSTLVPE---SEYLSLKDGSKKFsdlwgtvsDQLVEIYQNY-TQKNPAVTYQQATQ 270
Cdd:cd14751   147 KKGRYGLYISGDGPYWLLPFLWSFGGDLTDEkkaTGYLNSPESVRAL--------ETIVDLYDEGaITPCASGGYPNMQD 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934296053 271 DLAAGKAAILPLGTYAIPQI---RLINSDANLRFAQMPATDDASEQQLtAGDDviLTMGAHTKHEKEAREFIGFLMNDEN 347
Cdd:cd14751   219 GFKSGRYAMIVNGPWAYADIlggKEFKDPDNLGIAPVPAGPGGSGSPV-GGED--LVIFKGSKNKDAAWKFVKFMSSAEA 295
PotD COG0687
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism];
18-372 1.67e-11

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


Pssm-ID: 440451 [Multi-domain]  Cd Length: 348  Bit Score: 65.32  E-value: 1.67e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934296053  18 RALTATCAIALTAGLAGCGNSTAGTVTLDFFQFKAEAADWFtakAKEFEKTHpSIKVNV---NNSSDATTDLRTRlvkNR 94
Cdd:COG0687     4 RSLLGLAAAALAAALAGGAPAAAAEGTLNVYNWGGYIDPDV---LEPFEKET-GIKVVYdtyDSNEEMLAKLRAG---GS 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934296053  95 EPDVITINGDiNFGMLAEAGVFHDFTDDDIvdelnPGMVNIAKSLvQTNDESKKRLYGLPYAGNASGYIINADVWEEage 174
Cdd:COG0687    77 GYDVVVPSDY-FVARLIKAGLLQPLDKSKL-----PNLANLDPRF-KDPPFDPGNVYGVPYTWGTTGIAYNTDKVKE--- 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934296053 175 dpdnPPQTWSEFIDllQRFKSKGIVPIEASTadpwTLQAPLASLNstlvpeseylslKDGSKKFSDLWGTVSDQLVEIYQ 254
Cdd:COG0687   147 ----PPTSWADLWD--PEYKGKVALLDDPRE----VLGAALLYLG------------YDPNSTDPADLDAAFELLIELKP 204

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934296053 255 NytqknpAVTY----QQATQDLAAGKAAILPLGTYAIPQirLINSDANLRFAqMPatddaSEQQLTAGDdvILTMGAHTK 330
Cdd:COG0687   205 N------VRAFwsdgAEYIQLLASGEVDLAVGWSGDALA--LRAEGPPIAYV-IP-----KEGALLWFD--NMAIPKGAP 268

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 1934296053 331 HEKEAREFIGFLMNDENIKDYSKQQSAFTPYKDT--YVGDEALN 372
Cdd:COG0687   269 NPDLAYAFINFMLSPEVAAALAEYVGYAPPNKAAreLLPPELAA 312
PBP2_ABC_oligosaccharides cd13522
The periplasmic-binding component of ABC transport systems specific for maltose and related ...
 62-351 9.30e-09

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: 56.65  E-value: 9.30e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934296053  62 AKEFEKTHPSIKVNV-NNSSDATT-DLRTRLVKNREPDVITINGDiNFGMLAEAGVFHDFTDDdivdeLNPGMVNIAKSL 139
Cdd:cd13522    20 IAKFEKAYPGITVEVtYQDTEARRqFFSTAAAGGKGPDVVFGPSD-SLGPFAAAGLLAPLDEY-----VSKSGKYAPNTI 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934296053 140 vqTNDESKKRLYGLP-YAGNASGYIINADVweeagedPDNPPQTWSEFIDLLQRFKSKGIVPIEASTADPWTLQAPLASL 218
Cdd:cd13522    94 --AAMKLNGKLYGVPvSVGAHLMYYNKKLV-------PKNPPKTWQELIALAQGLKAKNVWGLVYNQNEPYFFAAWIGGF 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934296053 219 nstlvpeSEYLSLKDGSKKFSDLWGTVSDQ----LVEIYQNYTQKNPAVTYQQATQDLAAGKAAILPLGTYAIPQIRLiN 294
Cdd:cd13522   165 -------GGQVFKANNGKNNPTLDTPGAVEalqfLVDLKSKYKIMPPETDYSIADALFKAGKAAMIINGPWDLGDYRQ-A 236

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1934296053 295 SDANLRFAQMP-ATDDASEQQLTAGDDVIltMGAHTKHEKEAREFIGFLMNDENIKDY 351
Cdd:cd13522   237 LKINLGVAPLPtFSGTKHAAPFVGGKGFG--INKESQNKAAAVEFVKYLTSYQAQLVL 292
PBP2_Maltose_binding_like cd13586
The periplasmic-binding component of ABC transport systems specific for maltose and related ...
 53-381 2.25e-07

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: 52.68  E-value: 2.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934296053  53 EAADWFTAKAKEFEKTHPsIKVNVNNSSDATTDLRTRLVKN--REPDVITINGDiNFGMLAEAGVFHDFTDDDIVDELNp 130
Cdd:cd13586    10 GELEYLKELAEEFEKKYG-IKVEVVYVDSGDTREKFITAGPagKGPDVFFGPHD-WLGELAAAGLLAPIPEYLAVKIKN- 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934296053 131 gmVNIAKSLVQTNDeskkRLYGLPYAGNASGYIINADVWEEagedpdnPPQTWSEFIDLLQRF--KSKGIVPIEASTADP 208
Cdd:cd13586    87 --LPVALAAVTYNG----KLYGVPVSVETIALFYNKDLVPE-------PPKTWEELIALAKKFndKAGGKYGFAYDQTNP 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934296053 209 WTLQAPLASLnstlvpeSEYLsLKDGSKKFSDLwGTVSDQLVEIYQnYTQK--------NPAVTYQQATQDLAAGKAAIL 280
Cdd:cd13586   154 YFSYPFLAAF-------GGYV-FGENGGDPTDI-GLNNEGAVKGLK-FIKDlkkkykvlPPDLDYDIADALFKEGKAAMI 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934296053 281 PLGTYAIPQIRlinsDANLRFAQMPATDDASEQQLTAGDDVILTM-GAHTKHEKEAREFIGFLMNDENIKDYSKQQSAFT 359
Cdd:cd13586   224 INGPWDLADYK----DAGINFGVAPLPTLPGGKQAAPFVGVQGAFvSAYSKNKEAAVEFAEYLTSDEAQLLLFEKTGRIP 299

                         330       340
                  ....*....|....*....|....*..
gi 1934296053 360 PYKDTYV-----GDEALNGVLDFYQAG 381
Cdd:cd13586   300 ALKDALNdaavkNDPLVKAFAEQAQYG 326
AfuA COG1840
ABC-type Fe3+ transport system, periplasmic component [Inorganic ion transport and metabolism]; ...
 62-354 4.56e-07

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


Pssm-ID: 441445 [Multi-domain]  Cd Length: 286  Bit Score: 51.09  E-value: 4.56e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934296053  62 AKEFEKTHpSIKVNVNNSSdaTTDLRTRLV---KNREPDVITINGDINFGMLAEAGVFHDFTDDDiVDELNPGMVNiaks 138
Cdd:COG1840     2 LEAFEKKT-GIKVNVVRGG--SGELLARLKaegGNPPADVVWSGDADALEQLANEGLLQPYKSPE-LDAIPAEFRD---- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934296053 139 lvqtndeSKKRLYGLpyAGNASGYIINADVWEEAGedpdnPPQTWSEFIDllQRFKSKgIVpieasTADPwtlqaPLASL 218
Cdd:COG1840    74 -------PDGYWFGF--SVRARVIVYNTDLLKELG-----VPKSWEDLLD--PEYKGK-IA-----MADP-----SSSGT 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934296053 219 NSTLVpesEYLSLKDGSKKFSDLWGTVSDQLVEIYQNYTQknpavtyqqATQDLAAGKAAILPLGTYAIpqIRLINSDAN 298
Cdd:COG1840   127 GYLLV---AALLQAFGEEKGWEWLKGLAANGARVTGSSSA---------VAKAVASGEVAIGIVNSYYA--LRAKAKGAP 192

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1934296053 299 LRFAqMPAtddaseqqltagDDVILTMG-----AHTKHEKEAREFIGFLMNDENIKDYSKQ 354
Cdd:COG1840   193 VEVV-FPE------------DGTLVNPSgaailKGAPNPEAAKLFIDFLLSDEGQELLAEE 240
PBP2_Maltodextrin cd13657
The periplasmic binding component of ABC transport system specific for maltodextrin; This ...
 55-197 1.73e-05

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: 46.60  E-value: 1.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934296053  55 ADWFTAKAKEFEKTHPSIKVNV--NNSSDATTDLRTRLVKNREPDVITINGDiNFGMLAEAGVF---HDFTDDDIVDELN 129
Cdd:cd13657    13 EDALQQIIDEFEAKYPVPNVKVpfEKKPDLQNKLLTAIPAGEGPDLFIWAHD-WIGQFAEAGLLvpiSDYLSEDDFENYL 91

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1934296053 130 PGMVNIAkslvqtndESKKRLYGLPYAGNASGYIINADVWeeagedpDNPPQTWSEFIDLLQRFKSKG 197
Cdd:cd13657    92 PTAVEAV--------TYKGKVYGLPEAYETVALIYNKALV-------DQPPETTDELLAIMKDHTDPA 144
PBP2_AlgQ_like_3 cd13582
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 43-196 4.40e-04

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: 42.31  E-value: 4.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934296053  43 VTLDFFQFKAEAA--DWFTAKAKEF-EKThpsiKVNVN---NSSDATTDLRTRLVKNREPDVITINGDINfgMLAEAGVF 116
Cdd:cd13582     2 ITFTFFSADSNATpdDFKTPVAKKItELT----GVTLEieyLVGGEKQKIGLMIASGDLPDLIYAKGDTD--KLIEAGAL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934296053 117 HDFtdDDIVDELNPgmvNIaKSLVQTNDESKKR-----LYGLPYAGNAS-------GYIINADVWEEAGedpdnPPQ--T 182
Cdd:cd13582    76 VPL--DDLIEKYGP---NI-KKWYGDYLLKKLRsedghIYYLPNYRVEDapwypngGFWLQHDVLKELG-----YPKikT 144

                         170
                  ....*....|....
gi 1934296053 183 WSEFIDLLQRFKSK 196
Cdd:cd13582   145 LDDYENLIKDYKKK 158
PBP2_AlgQ_like cd13521
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 62-346 4.60e-04

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: 42.44  E-value: 4.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934296053  62 AKEFEK-THPSIKVNVNNSSDATTDLRTRLVKNREPDVITINGDINFGMLA-EAGVFHDFTDDdiVDElnpgMVNIAKSL 139
Cdd:cd13521    23 AKEIEKlTNVKLEIVAVTAATSQQKLNLMLASGDLPDIVGADYLKDKFIAYgMEGAFLPLSKY--IDQ----YPNLKAFF 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934296053 140 VQTND------ESKKRLYGLPY----AGNASGYIINADVWEEAGEdpdNPPQTWSEFIDLLQRFKSKGIV----PIEAST 205
Cdd:cd13521    97 KQHPDvlrastASDGKIYLIPYeppkDVPNQGYFIRKDWLDKLNL---KTPKTLDELYNVLKAFKEKDPNgngkADEIPF 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934296053 206 ADPWTLQAPLASLNST------LVPESEYlSLKDGskKFSDLWGTVSDQLVEIYQNYTQKN-------PAVTYQQATQDL 272
Cdd:cd13521   174 IDRDPLYGAFRLINSWgarsagGSTDSDW-YEDNG--KFKHPFASEEYKDGMKYMNKLYTEglidkesFTQKDDQAEQKF 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934296053 273 AAGKAAILPLGTYAIP-QIRLINSDANLRFAQ---MPATDDASEQQL-----TAGDDVILTmgAHTKHEKEAREFIGFLM 343
Cdd:cd13521   251 SNGKLGGFTHNWFASDnLFTAQLGKEKPMYILlpiAPAGNVKGRREEdspgyTGPDGVAIS--KKAKNPVAALKFFDWLA 328


                  ...
gi 1934296053 344 NDE 346
Cdd:cd13521   329 SEE 331
PBP2_polyamine_1 cd13588
The periplasmic-binding component of an uncharacterized ABC transporter involved in uptake of ...
 44-196 2.20e-03

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: 39.59  E-value: 2.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934296053  44 TLDFFQFKAEAADWFTakaKEFEKTHpSIKVNV---NNSSDATTDLRTrlvKNREPDVITINGDInFGMLAEAGvfhdft 120
Cdd:cd13588     1 ELNVLTWPGYADPDWV---TAFEEAT-GCKVVVkffGSEDEMVAKLRS---GGGDYDVVTPSGDA-LLRLIAAG------ 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934296053 121 dddIVDELN----PGMVNIAKSLVQTNDESK-KRLYGLPYAGNASGYIINADVweeagedPDNPPQTWsefIDLL--QRF 193
Cdd:cd13588    67 ---LVQPIDtskiPNYANIDPRLRNLPWLTVdGKVYGVPYDWGANGLAYNTKK-------VKTPPTSW---LALLwdPKY 133


                  ...
gi 1934296053 194 KSK 196
Cdd:cd13588   134 KGR 136
PBP2_AlgQ_like_1 cd13580
Periplasmic-binding component of alginate-specific ABC uptake system-like; contains the type 2 ...
 72-349 5.37e-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: 270298 [Multi-domain]  Cd Length: 471  Bit Score: 38.85  E-value: 5.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934296053  72 IKVNVNN--SSDATTDLRTRLVKNREPDVITINGDINFGMLAEAGVFHDFTddDIVDELNPgmvNIAKSLVQTNDESKKR 149
Cdd:cd13580    34 IDVKVKWvpDSSYDEKLNLALASGDLPDIVVVNDPQLSITLVKQGALWDLT--DYLDKYYP---NLKKIIEQEGWDSASV 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934296053 150 ---LYGLP---YAGNASGYIINADVWEEAGEdpdNPPQTWSEFIDLLQRFKSKGivPIEASTADPWTLQAPLASLNSTL- 222
Cdd:cd13580   109 dgkIYGIPrkrPLIGRNGLWIRKDWLDKLGL---EVPKTLDELYEVAKAFTEKD--PDGNGKKDTYGLTDTKDLIGSGFt 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934296053 223 -------VPESEYLSLKDGskKFSdlWGTVSDQ-------LVEIYQN-YTQKNPAVT-YQQATQDLAAGKAAIL--PLGT 284
Cdd:cd13580   184 glfgafgAPPNNWWKDEDG--KLV--PGSIQPEmkealkfLKKLYKEgLIDPEFAVNdGTKANEKFISGKAGIFvgNWWD 259

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1934296053 285 YAIPQIRLINSDANLRFAQMPA-TDDASEQ--QLTAGDDVILTMGAHTKHEKEAREFIGFLMNDENIK 349
Cdd:cd13580   260 PAWPQASLKKNDPDAEWVAVPIpSGPDGKYgvWAESGVNGFFVIPKKSKKPEAILKLLDFLSDPEVQK 327
 
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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