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Conserved domains on  [gi|486463988|gb|EOE08312|]
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phosphate binding protein [Enterococcus faecalis EnGen0058]

Protein Classification

phosphate ABC transporter substrate-binding protein PstS( domain architecture ID 10797741)

phosphate ABC transporter substrate-binding protein PstS is part of the ABC transporter complex PstSACB involved in phosphate import and it functions as the initial receptor for phosphate

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ptsS_2 TIGR02136
phosphate binding protein; Members of this family are phosphate-binding proteins. Most are ...
1-269 1.97e-128

phosphate binding protein; Members of this family are phosphate-binding proteins. Most are found in phosphate ABC-transporter operons, but some are found in phosphate regulatory operons. This model separates members of the current family from the phosphate ABC transporter phosphate binding protein described by TIGRFAMs model TIGR00975. [Transport and binding proteins, Anions]


:

Pssm-ID: 273991 [Multi-domain]  Cd Length: 287  Bit Score: 366.38  E-value: 1.97e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486463988    1 MKKRLLLFIGLAS-ILTLTGCAKWIDRG-------ESITAVGSSALQPLVETASEEYQSQNPGRFINVQGGGSGTGLSQV 72
Cdd:TIGR02136   1 MKKRIFLLIGLAAaLLAAAGCGGAIDSGipdakgsSTITIDGSTTVAPLAEAAAEEFQKIHPGVSVTVQGAGSGTGIKAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486463988   73 QSGAVDIGNSD--LFAEE--KKGIKAEDLIDHKVAVVGITPIVN-KNVGVKDISMENLKKIFLGEVTNWKELGG--KDQK 145
Cdd:TIGR02136  81 INGTVDIGNSSrpIKDEElqKDKQKGIKLIEHKVAVDGLAVVVNkKNVPVDDLTVEQLKKIYSGEITNWKEVGGdlPNKP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486463988  146 IVILNRAAGSGTRATFEKWVLGDKTAIRAQ-EQDSSGMVRSIVSDTPGAISYTAFSYVTDEVATLSIDGVQPTDENVMNN 224
Cdd:TIGR02136 161 IVVVGRNAGSGTRDTFEEEVMGKAKIKPGKnEQESNGAVVSIVSSNPGAIGYLGLGYVDDSVKTLKVNGVEPSKENIANG 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 486463988  225 KWIIWSYEHMYTRKNPSD--LTKEFLDFMLSDDIQERVIGQLGYIPV 269
Cdd:TIGR02136 241 SYPLSRPLFMYVNGKPKKpeLVAEFIDFVLSDDGGERIVEELGYVPL 287
 
Name Accession Description Interval E-value
ptsS_2 TIGR02136
phosphate binding protein; Members of this family are phosphate-binding proteins. Most are ...
1-269 1.97e-128

phosphate binding protein; Members of this family are phosphate-binding proteins. Most are found in phosphate ABC-transporter operons, but some are found in phosphate regulatory operons. This model separates members of the current family from the phosphate ABC transporter phosphate binding protein described by TIGRFAMs model TIGR00975. [Transport and binding proteins, Anions]


Pssm-ID: 273991 [Multi-domain]  Cd Length: 287  Bit Score: 366.38  E-value: 1.97e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486463988    1 MKKRLLLFIGLAS-ILTLTGCAKWIDRG-------ESITAVGSSALQPLVETASEEYQSQNPGRFINVQGGGSGTGLSQV 72
Cdd:TIGR02136   1 MKKRIFLLIGLAAaLLAAAGCGGAIDSGipdakgsSTITIDGSTTVAPLAEAAAEEFQKIHPGVSVTVQGAGSGTGIKAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486463988   73 QSGAVDIGNSD--LFAEE--KKGIKAEDLIDHKVAVVGITPIVN-KNVGVKDISMENLKKIFLGEVTNWKELGG--KDQK 145
Cdd:TIGR02136  81 INGTVDIGNSSrpIKDEElqKDKQKGIKLIEHKVAVDGLAVVVNkKNVPVDDLTVEQLKKIYSGEITNWKEVGGdlPNKP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486463988  146 IVILNRAAGSGTRATFEKWVLGDKTAIRAQ-EQDSSGMVRSIVSDTPGAISYTAFSYVTDEVATLSIDGVQPTDENVMNN 224
Cdd:TIGR02136 161 IVVVGRNAGSGTRDTFEEEVMGKAKIKPGKnEQESNGAVVSIVSSNPGAIGYLGLGYVDDSVKTLKVNGVEPSKENIANG 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 486463988  225 KWIIWSYEHMYTRKNPSD--LTKEFLDFMLSDDIQERVIGQLGYIPV 269
Cdd:TIGR02136 241 SYPLSRPLFMYVNGKPKKpeLVAEFIDFVLSDDGGERIVEELGYVPL 287
PBP2_phosphate_like_1 cd13653
Substrate binding domain of putative ABC-type phosphate transporter, a member of the type 2 ...
27-265 4.51e-94

Substrate binding domain of putative ABC-type phosphate transporter, a member of the type 2 periplasmic binding fold superfamily; This subfamily contains uncharacterized phosphate binding domains found in PstS proteins that serve as initial receptors in the ABC transport of phosphate in eubacteria and archaea. After binding the ligand, PstS interacts 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. The PstS proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270371 [Multi-domain]  Cd Length: 240  Bit Score: 277.53  E-value: 4.51e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486463988  27 GESITAVGSSALQPLVETASEEYQSQNPGRFINVQGGGSGTGLSQVQSGAVDIGNSDLFAEEKKGIKAEDLIDHKVAVVG 106
Cdd:cd13653    1 SGTITISGSTTVAPLAEALAEAFMEKHPGVRIEVQGGGSGTGIKALIEGTADIGMASRPLKAEEKAAASGLVEHVIALDG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486463988 107 ITPIVNKNVGVKDISMENLKKIFLGEVTNWKELGGKDQKIVILNRAAGSGTRATFEKWVLGDKTAIR-AQEQDSSGMVRS 185
Cdd:cd13653   81 IAIIVNPDNPVKNLTLEQLRDIFSGKITNWKEVGGPDGPIVVISREEGSGTRETFEELVLGKKDFAKnAVVVPSNGAVVQ 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486463988 186 IVSDTPGAISYTAFSYVTDE-VATLSIDGVQPTDENVMNNKWIIWSYEHMYTRKNPSDLTKEFLDFMLSDDIQErVIGQL 264
Cdd:cd13653  161 AVAKNPNAIGYVSLGYVDDSkVKALSVDGVAPTPENIKSGKYPLSRPLYLYTKGEPSGLVKAFIDFALSPEGQA-IVEKL 239

                 .
gi 486463988 265 G 265
Cdd:cd13653  240 G 240
PstS COG0226
ABC-type phosphate transport system, periplasmic component [Inorganic ion transport and ...
29-277 1.90e-87

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


Pssm-ID: 439996 [Multi-domain]  Cd Length: 275  Bit Score: 261.74  E-value: 1.90e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486463988  29 SITAVGSSALQPLVETASEEYQSQNPGRFINVQGGGSGTGLSQVQSGAVDIGNSDLFAEEKKGIKAE----DLIDHKVAV 104
Cdd:COG0226    5 TITIAGSSTVYPLAEAWAEAFQKANPGVTINVQSGGSGGGIKQFIAGTVDIGNSSRPLKDEELEAAKengvELVEIPVAI 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486463988 105 VGITPIVNKNVGVKDISMENLKKIFLGEVTNWKELGGK--DQKIVILNRAAGSGTRATFEKWVLGDKTAIR--AQEQDSS 180
Cdd:COG0226   85 DGIAVVVNPDNPVKNLTGEQLADIFSGKITNWNDIGGKlpDEPITVVGRSDGSGTTDYFTEYLLGVGAEVRegVEGAEGN 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486463988 181 GMVRSIVSDTPGAISYTAFSYVTDE-VATLSID-----GVQPTDENVMNNKWIIWSYEHMYTRKNP---SDLTKEFLDFM 251
Cdd:COG0226  165 EGVVQAVAQTPGAIGYVGLSYAEQNkLKALAIDnkagkFVEPTAENIAAGSYPLSRPLYIYVKKEPdakAPAVKAFLDFV 244
                        250       260
                 ....*....|....*....|....*.
gi 486463988 252 LSDDIQErVIGQLGYIPVSKMEIERD 277
Cdd:COG0226  245 LSDGGQK-IVEKLGYVPLPDAVVEKV 269
PBP_like_2 pfam12849
PBP superfamily domain; This domain belongs to the periplasmic binding protein superfamily.
26-255 8.53e-37

PBP superfamily domain; This domain belongs to the periplasmic binding protein superfamily.


Pssm-ID: 432831 [Multi-domain]  Cd Length: 267  Bit Score: 131.51  E-value: 8.53e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486463988   26 RGESITAVGSSALQPLVETASEEYQSQNPGRFINVQGGGSGTGLSQVQSGAVDIGNSD--LFAEEKKGIKAE---DLIDH 100
Cdd:pfam12849   8 TVGTILIAGSSTQAPGLLDLAEAFEKKYPGAKVKVTSVGSGEGIKALLNGDVDVALVSrpLTEEEFEAFGANgagGLVEV 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486463988  101 KVAVVGITPIVNKNVGVKDISMENLKKIFLGEVTNWKElGGKDQKIVILNRAAGSGTRATFEKWVLGDKTAI-RAQEQDS 179
Cdd:pfam12849  88 PVAYDGIAIVVNKDNPANILTVEALKKIFSGKITNWND-GGPDGPIKFVSRGDNSGTTELFSTHLKEKGPWGaAGIGAAG 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486463988  180 SGMVRSIVSdTPGAISYTAFSYV-------------------TDEVATLSIDG----VQPTDENVMNNKWIIWSYEHMYT 236
Cdd:pfam12849 167 SPGVASVVA-GPGAIGYVEVSYAlanlgytladvaggtylsfAKALKVAKINPgaglVIPLEEAIADGDYPLSRPYYVIV 245
                         250       260
                  ....*....|....*....|..
gi 486463988  237 R---KNPSDLTKEFLDFMLSDD 255
Cdd:pfam12849 246 KnppKGPAPLAKAFLDFLLSDE 267
PRK10918 PRK10918
phosphate ABC transporter substrate-binding protein PstS;
28-230 6.43e-09

phosphate ABC transporter substrate-binding protein PstS;


Pssm-ID: 182837  Cd Length: 346  Bit Score: 55.99  E-value: 6.43e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486463988  28 ESITAVGSSALQPLVETASEEYQSQNpGRFINVQGGGSGTGLSQVQSGAVDIGNSDL-FAEEKkgIKAEDLIDHKVAVVG 106
Cdd:PRK10918  27 ASLTGAGATFPAPVYAKWADTYQKET-GNKVNYQGIGSSGGVKQIIANTVDFGASDApLSDEK--LAQEGLFQFPTVIGG 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486463988 107 ITPIVNKNvGVKD----ISMENLKKIFLGEVTNWKE---------LGGKDQKIVILNRAAGSGTRATFEKWVlgdkTAIR 173
Cdd:PRK10918 104 VVLAVNIP-GLKSgelvLDGKTLGDIYLGKIKKWNDeaiaklnpgVKLPSQNIAVVRRADGSGTSFVFTSYL----AKVN 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486463988 174 AQEQDSSGM-----------------VRSIVSDTPGAISYTAFSYVTDEVAT----LSIDG--VQPTDENVMN-NKWIIW 229
Cdd:PRK10918 179 EEWKSKVGAgstvnwptglggkgndgIAAFVQRLPGAIGYVEYAYAKQNNLAytklISADGkpVSPTEESFSNaAKGADW 258

                 .
gi 486463988 230 S 230
Cdd:PRK10918 259 S 259
 
Name Accession Description Interval E-value
ptsS_2 TIGR02136
phosphate binding protein; Members of this family are phosphate-binding proteins. Most are ...
1-269 1.97e-128

phosphate binding protein; Members of this family are phosphate-binding proteins. Most are found in phosphate ABC-transporter operons, but some are found in phosphate regulatory operons. This model separates members of the current family from the phosphate ABC transporter phosphate binding protein described by TIGRFAMs model TIGR00975. [Transport and binding proteins, Anions]


Pssm-ID: 273991 [Multi-domain]  Cd Length: 287  Bit Score: 366.38  E-value: 1.97e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486463988    1 MKKRLLLFIGLAS-ILTLTGCAKWIDRG-------ESITAVGSSALQPLVETASEEYQSQNPGRFINVQGGGSGTGLSQV 72
Cdd:TIGR02136   1 MKKRIFLLIGLAAaLLAAAGCGGAIDSGipdakgsSTITIDGSTTVAPLAEAAAEEFQKIHPGVSVTVQGAGSGTGIKAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486463988   73 QSGAVDIGNSD--LFAEE--KKGIKAEDLIDHKVAVVGITPIVN-KNVGVKDISMENLKKIFLGEVTNWKELGG--KDQK 145
Cdd:TIGR02136  81 INGTVDIGNSSrpIKDEElqKDKQKGIKLIEHKVAVDGLAVVVNkKNVPVDDLTVEQLKKIYSGEITNWKEVGGdlPNKP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486463988  146 IVILNRAAGSGTRATFEKWVLGDKTAIRAQ-EQDSSGMVRSIVSDTPGAISYTAFSYVTDEVATLSIDGVQPTDENVMNN 224
Cdd:TIGR02136 161 IVVVGRNAGSGTRDTFEEEVMGKAKIKPGKnEQESNGAVVSIVSSNPGAIGYLGLGYVDDSVKTLKVNGVEPSKENIANG 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 486463988  225 KWIIWSYEHMYTRKNPSD--LTKEFLDFMLSDDIQERVIGQLGYIPV 269
Cdd:TIGR02136 241 SYPLSRPLFMYVNGKPKKpeLVAEFIDFVLSDDGGERIVEELGYVPL 287
PBP2_phosphate_like_1 cd13653
Substrate binding domain of putative ABC-type phosphate transporter, a member of the type 2 ...
27-265 4.51e-94

Substrate binding domain of putative ABC-type phosphate transporter, a member of the type 2 periplasmic binding fold superfamily; This subfamily contains uncharacterized phosphate binding domains found in PstS proteins that serve as initial receptors in the ABC transport of phosphate in eubacteria and archaea. After binding the ligand, PstS interacts 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. The PstS proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270371 [Multi-domain]  Cd Length: 240  Bit Score: 277.53  E-value: 4.51e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486463988  27 GESITAVGSSALQPLVETASEEYQSQNPGRFINVQGGGSGTGLSQVQSGAVDIGNSDLFAEEKKGIKAEDLIDHKVAVVG 106
Cdd:cd13653    1 SGTITISGSTTVAPLAEALAEAFMEKHPGVRIEVQGGGSGTGIKALIEGTADIGMASRPLKAEEKAAASGLVEHVIALDG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486463988 107 ITPIVNKNVGVKDISMENLKKIFLGEVTNWKELGGKDQKIVILNRAAGSGTRATFEKWVLGDKTAIR-AQEQDSSGMVRS 185
Cdd:cd13653   81 IAIIVNPDNPVKNLTLEQLRDIFSGKITNWKEVGGPDGPIVVISREEGSGTRETFEELVLGKKDFAKnAVVVPSNGAVVQ 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486463988 186 IVSDTPGAISYTAFSYVTDE-VATLSIDGVQPTDENVMNNKWIIWSYEHMYTRKNPSDLTKEFLDFMLSDDIQErVIGQL 264
Cdd:cd13653  161 AVAKNPNAIGYVSLGYVDDSkVKALSVDGVAPTPENIKSGKYPLSRPLYLYTKGEPSGLVKAFIDFALSPEGQA-IVEKL 239

                 .
gi 486463988 265 G 265
Cdd:cd13653  240 G 240
PstS COG0226
ABC-type phosphate transport system, periplasmic component [Inorganic ion transport and ...
29-277 1.90e-87

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


Pssm-ID: 439996 [Multi-domain]  Cd Length: 275  Bit Score: 261.74  E-value: 1.90e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486463988  29 SITAVGSSALQPLVETASEEYQSQNPGRFINVQGGGSGTGLSQVQSGAVDIGNSDLFAEEKKGIKAE----DLIDHKVAV 104
Cdd:COG0226    5 TITIAGSSTVYPLAEAWAEAFQKANPGVTINVQSGGSGGGIKQFIAGTVDIGNSSRPLKDEELEAAKengvELVEIPVAI 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486463988 105 VGITPIVNKNVGVKDISMENLKKIFLGEVTNWKELGGK--DQKIVILNRAAGSGTRATFEKWVLGDKTAIR--AQEQDSS 180
Cdd:COG0226   85 DGIAVVVNPDNPVKNLTGEQLADIFSGKITNWNDIGGKlpDEPITVVGRSDGSGTTDYFTEYLLGVGAEVRegVEGAEGN 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486463988 181 GMVRSIVSDTPGAISYTAFSYVTDE-VATLSID-----GVQPTDENVMNNKWIIWSYEHMYTRKNP---SDLTKEFLDFM 251
Cdd:COG0226  165 EGVVQAVAQTPGAIGYVGLSYAEQNkLKALAIDnkagkFVEPTAENIAAGSYPLSRPLYIYVKKEPdakAPAVKAFLDFV 244
                        250       260
                 ....*....|....*....|....*.
gi 486463988 252 LSDDIQErVIGQLGYIPVSKMEIERD 277
Cdd:COG0226  245 LSDGGQK-IVEKLGYVPLPDAVVEKV 269
PBP2_phosphate cd13566
Substrate binding domain of putative ABC-type phosphate transporter, a member of the type 2 ...
28-265 4.38e-82

Substrate binding domain of putative ABC-type phosphate transporter, a member of the type 2 periplasmic binding fold superfamily; This subfamily contains uncharacterized phosphate binding domains found in PstS proteins that serve as initial receptors in the ABC transport of phosphate in eubacteria and archaea. After binding the ligand, PstS interacts 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. The PstS proteins belong to the PBPII superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270284 [Multi-domain]  Cd Length: 245  Bit Score: 247.11  E-value: 4.38e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486463988  28 ESITAVGSSALQPLVETASEEYQSQNPGRFINVQGGGSGTGLSQVQSGAVDIGNS--DLFAEEKKGIKAE--DLIDHKVA 103
Cdd:cd13566    2 GTITIAGSSTVAPLAEALAEEFMKKHPGVRVTVQGGGSGAGIKALIAGTADIAMAsrPLKDEEKAAAEANgiELVEFVIA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486463988 104 VVGITPIVNKNVGVKDISMENLKKIFLGEVTNWKELGGKDQKIVILNRAAGSGTRATFEKWVLGDKTAIR-AQEQDSSGM 182
Cdd:cd13566   82 YDGIAVIVNPDNPVASLTLEQLRDIFTGKITNWSEVGGPDEPIVVYGRDEGSGTRDYFEELVLGKGEFIRnAVVAPSNGA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486463988 183 VRSIVSDTPGAISYTAFSYVTD--EVATLSIDGVQPTDENVMNNKWIIWSYEHMYTRKNPSDLTKEFLDFMLSDDIQErV 260
Cdd:cd13566  162 LVQAVAGDPNAIGYVGLGYVDEnkKVKALKVDGVAPTVENIKSGKYPLSRPLFLYTKGEPSPAVKAFIDFALSPEGQK-I 240

                 ....*
gi 486463988 261 IGQLG 265
Cdd:cd13566  241 IEEVG 245
PBP_like_2 pfam12849
PBP superfamily domain; This domain belongs to the periplasmic binding protein superfamily.
26-255 8.53e-37

PBP superfamily domain; This domain belongs to the periplasmic binding protein superfamily.


Pssm-ID: 432831 [Multi-domain]  Cd Length: 267  Bit Score: 131.51  E-value: 8.53e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486463988   26 RGESITAVGSSALQPLVETASEEYQSQNPGRFINVQGGGSGTGLSQVQSGAVDIGNSD--LFAEEKKGIKAE---DLIDH 100
Cdd:pfam12849   8 TVGTILIAGSSTQAPGLLDLAEAFEKKYPGAKVKVTSVGSGEGIKALLNGDVDVALVSrpLTEEEFEAFGANgagGLVEV 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486463988  101 KVAVVGITPIVNKNVGVKDISMENLKKIFLGEVTNWKElGGKDQKIVILNRAAGSGTRATFEKWVLGDKTAI-RAQEQDS 179
Cdd:pfam12849  88 PVAYDGIAIVVNKDNPANILTVEALKKIFSGKITNWND-GGPDGPIKFVSRGDNSGTTELFSTHLKEKGPWGaAGIGAAG 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486463988  180 SGMVRSIVSdTPGAISYTAFSYV-------------------TDEVATLSIDG----VQPTDENVMNNKWIIWSYEHMYT 236
Cdd:pfam12849 167 SPGVASVVA-GPGAIGYVEVSYAlanlgytladvaggtylsfAKALKVAKINPgaglVIPLEEAIADGDYPLSRPYYVIV 245
                         250       260
                  ....*....|....*....|..
gi 486463988  237 R---KNPSDLTKEFLDFMLSDD 255
Cdd:pfam12849 246 KnppKGPAPLAKAFLDFLLSDE 267
PBP2_PstS cd13565
Substrate binding domain of ABC-type phosphate transporter, a member of the type 2 ...
29-254 1.82e-30

Substrate binding domain of ABC-type phosphate transporter, a member of the type 2 periplasmic-binding fold superfamily; This subfamily contians phosphate binding domain found in PstS proteins that serve as initial receptors in the ABC transport of phosphate in eubacteria and archaea. After binding the ligand, PstS interacts 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. The PstS proteins belong to the PBPII superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270283 [Multi-domain]  Cd Length: 254  Bit Score: 114.64  E-value: 1.82e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486463988  29 SITAVGSSALQPLVETASEEYQSQNPGRFINVQGGGSGTGLSQVQSGAVDIGNSD--LFAEEKKGIKAEdLIDHKVAVVG 106
Cdd:cd13565    3 TLTGAGATFPAPLYQKWIDEYKKAHPGVKINYQSIGSGAGIKQFIAGTVDFGASDapLSDAELAKAGGG-LLQIPTVIGA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486463988 107 ITPIVNKNvGVKD---ISMENLKKIFLGEVTNWKELGGK---------DQKIVILNRAAGSGTRATF--------EKWvl 166
Cdd:cd13565   82 VVVAYNLP-GVKGlllLSGEVLADIFLGKITKWNDPAIAalnpgvnlpDTPITVVHRSDGSGTTFIFtdylsavsPEW-- 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486463988 167 gdKTAIRAQEQDS---------SGMVRSIVSDTPGAISYTAFSYVTDevATLSIDGVQPtdenvmnnkWIIWSYEHMYTR 237
Cdd:cd13565  159 --KDKVGAGKSVAwpvglggkgNEGVAAAVKQTPGSIGYVELSYALQ--NGLPAAALYP---------IVGFTYILVKKD 225
                        250       260
                 ....*....|....*....|
gi 486463988 238 KNPS---DLTKEFLDFMLSD 254
Cdd:cd13565  226 YKDAekaKAVKKFLKWALTE 245
PBP2_phosphate_like_2 cd13654
Substrate binding domain of putative ABC-type phosphate transporter, a member of the type 2 ...
29-254 3.64e-25

Substrate binding domain of putative ABC-type phosphate transporter, a member of the type 2 periplasmic binding fold superfamily; This subfamily contains uncharacterized phosphate binding domains found in PstS proteins that serve as initial receptors in the ABC transport of phosphate in eubacteria and archaea. After binding the ligand, PstS interacts 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. The PstS proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270372  Cd Length: 259  Bit Score: 100.79  E-value: 3.64e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486463988  29 SITAVGSSALQPLVETASEEYQSQNPGRFINVQGGGSGTGLSQVQSGAVDIGNS-----DLFAE--EKKGIkaeDLIDHK 101
Cdd:cd13654    3 QIRIDGSSTVYPITEAVAEEFGKSGPGVTVTVGSSGTGGGFKKFCAGETDISNAsrpikDSEAElcEANGI---EYIELP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486463988 102 VAVVGITPIVNK-NVGVKDISMENLKKIFL--GEVTNWKELGGK--DQKIVILNRAAGSGTRATFEKWVLGDKTAIR--- 173
Cdd:cd13654   80 VAYDGLTVVVNPaNDWAKCLTELELKSIWAaeSPITTWSDVRPSwpDEPIELYGPGTDSGTFDYFTEAIVGEGGSIRedy 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486463988 174 -AQEQDsSGMVRSIVSDtPGAISYTAFSYV---TDEVATLSIDGVQPT----DENVMNNK--------WIIWSYEHMYTR 237
Cdd:cd13654  160 tASEDD-NVLVQGVAGD-KNALGFFGYAYYeenGDKLKAVKIDGGEGTvapsAETTISGGyyplsrplFIYVKKASLAEK 237
                        250
                 ....*....|....*..
gi 486463988 238 KnpsdLTKEFLDFMLSD 254
Cdd:cd13654  238 P----AVAAFVKFYLEN 250
PBP2_phosphate_binding cd01006
Substrate binding domain of ABC-type phosphate transporter, a member of the type 2 ...
29-254 6.27e-24

Substrate binding domain of ABC-type phosphate transporter, a member of the type 2 periplasmic-binding fold superfamily; This phosphate-binding domain shows significant homology to the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. 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: 270227 [Multi-domain]  Cd Length: 253  Bit Score: 97.33  E-value: 6.27e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486463988  29 SITAVGSSALQPLVETASEEYQSQNPGRFINVQGGGSGTGLSQVQSGAVDIGNSDLFAEEKKgIKAEDLIDHKVAVVGIT 108
Cdd:cd01006    3 ELTISGSTSVAPI*DVWAEKYNQQHPETYVAVQGVGSTAGISQLKAGTVDIGASDAYLSESE-AANKGLHTFTLAIDGLA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486463988 109 PIVNKnVGVKD---ISMENLKKIFLGEVTNWKELG---------GKDQKIVILNRAAGSGTRATF---------EKWVLG 167
Cdd:cd01006   82 IVVNQ-PGPVTnltLNGKQLYGIYKGQIKNWDDVGiaalnpgvnLPDQKIAVVTREDGSGTRFSFtsylgktktEKDGKG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486463988 168 -----DKTAIRAQEQDSSGMVrSIVSDTPGAISYTAFSYVtdevatlsidgvqptDENVMNNK--WIIWSYEHMYTRKNP 240
Cdd:cd01006  161 ttevsDVAPTALGVNGNSG*K-TLVNHNPGAVGYISIGSV---------------DQSSLKAIqlYPISRPFLILHYSDQ 224
                        250
                 ....*....|....*....
gi 486463988 241 SDL-----TKEFLDFMLSD 254
Cdd:cd01006  225 KDAatdeqTKEFIAWAKSE 243
PBP_like pfam12727
PBP superfamily domain; This family belongs to the periplasmic binding domain superfamily. It ...
46-251 8.35e-15

PBP superfamily domain; This family belongs to the periplasmic binding domain superfamily. It is often associated with a helix-turn-helix domain.


Pssm-ID: 463683 [Multi-domain]  Cd Length: 192  Bit Score: 71.07  E-value: 8.35e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486463988   46 SEEYQSQNPGRFINVQGGGSGTGLSQVQSGAVDIGNSDLFAEEKKGIKA----EDLIDHKVAVVgitPIVNKNVGVkDIS 121
Cdd:pfam12727   1 AEELARKHPGVRLAVAYVGSLGGLAALRRGEAHIAGIHLLDPETGEYNLpflrRLLPGIPVVLI---NLAYREQGL-VVA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486463988  122 MENLKKIflgevTNWKELGgkDQKIVILNRAAGSGTRATFEKWVLG---DKTAIR--AQEQDSSGMVRSIVSDTPGAISY 196
Cdd:pfam12727  77 PGNPKGI-----TGWEDLA--RPGLRFVNRQRGSGTRVLLDELLRKagiDPSDINgyDREERSHLAVAAAVASGRADAGL 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 486463988  197 tafsyvtdevatlsidGVQPTDENVMN---NKWIIWSYEHMYTRKN-PSDLTKEFLDFM 251
Cdd:pfam12727 150 ----------------GIEAAARALGGldfIPLARERYDLVIPKEAlDDPAVQALLEVL 192
PRK10918 PRK10918
phosphate ABC transporter substrate-binding protein PstS;
28-230 6.43e-09

phosphate ABC transporter substrate-binding protein PstS;


Pssm-ID: 182837  Cd Length: 346  Bit Score: 55.99  E-value: 6.43e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486463988  28 ESITAVGSSALQPLVETASEEYQSQNpGRFINVQGGGSGTGLSQVQSGAVDIGNSDL-FAEEKkgIKAEDLIDHKVAVVG 106
Cdd:PRK10918  27 ASLTGAGATFPAPVYAKWADTYQKET-GNKVNYQGIGSSGGVKQIIANTVDFGASDApLSDEK--LAQEGLFQFPTVIGG 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486463988 107 ITPIVNKNvGVKD----ISMENLKKIFLGEVTNWKE---------LGGKDQKIVILNRAAGSGTRATFEKWVlgdkTAIR 173
Cdd:PRK10918 104 VVLAVNIP-GLKSgelvLDGKTLGDIYLGKIKKWNDeaiaklnpgVKLPSQNIAVVRRADGSGTSFVFTSYL----AKVN 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486463988 174 AQEQDSSGM-----------------VRSIVSDTPGAISYTAFSYVTDEVAT----LSIDG--VQPTDENVMN-NKWIIW 229
Cdd:PRK10918 179 EEWKSKVGAgstvnwptglggkgndgIAAFVQRLPGAIGYVEYAYAKQNNLAytklISADGkpVSPTEESFSNaAKGADW 258

                 .
gi 486463988 230 S 230
Cdd:PRK10918 259 S 259
ModA COG0725
ABC-type molybdate transport system, periplasmic Mo-binding protein ModA [Inorganic ion ...
3-270 5.78e-07

ABC-type molybdate transport system, periplasmic Mo-binding protein ModA [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, periplasmic Mo-binding protein ModA is part of the Pathway/BioSystem: Molybdopterin biosynthesis


Pssm-ID: 440489 [Multi-domain]  Cd Length: 253  Bit Score: 49.48  E-value: 5.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486463988   3 KRLLLFIGLASILTLTGCAKwIDRGESIT-AVGSSaLQPLVETASEEYQSQNPGRFINVQGGGSGTGLSQVQSGA-VDI- 79
Cdd:COG0725    1 RRLLLLALLLLALLLAGASA-AAAAAELTvFAAAS-LKEALEELAAAFEKEHPGVKVELSFGGSGALARQIEQGApADVf 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486463988  80 --GNSDLF--AEEKKGIKAEDLIDhkVAVVGITPIVNKNVGVKdismenlkkiflgeVTNWKELGGKDQKIVILN-RAAG 154
Cdd:COG0725   79 isADEKYMdkLAKKGLILAGSRVV--FATNRLVLAVPKGNPAD--------------ISSLEDLAKPGVRIAIGDpKTVP 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486463988 155 SGTRA--TFEKWVLGDKTAIRAQEQDSSGMVRSIVSDtpGAISYtAFSYVTDEVATLSIDGVQPTDENVmnNKWIIwsye 232
Cdd:COG0725  143 YGKYAkeALEKAGLWDALKPKLVLGENVRQVLAYVES--GEADA-GIVYLSDALAAKGVLVVVELPAEL--YAPIV---- 213
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 486463988 233 hmY------TRKNPsDLTKEFLDFMLSDDIQErVIGQLGYIPVS 270
Cdd:COG0725  214 --YpaavlkGAKNP-EAAKAFLDFLLSPEAQA-ILEKYGFEPPK 253
PBP2_ModA_like_1 cd13538
Substrate binding domain of putative molybdate-binding protein;the type 2 periplasmic binding ...
29-267 7.11e-05

Substrate binding domain of putative molybdate-binding protein;the type 2 periplasmic binding protein fold; This subfamily contains domains found in ModA proteins of putative ABC-type transporter. Molybdate transport system is comprised of a periplasmic binding protein, an integral membrane protein, and an energizer protein. These three proteins are coded by modA, modB, and modC genes, respectively. ModA proteins serve as initial receptors in the ABC transport of molybdate mostly in eubacteria and archaea. After binding molybdate with high affinity, they interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The ModA proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270256 [Multi-domain]  Cd Length: 230  Bit Score: 43.06  E-value: 7.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486463988  29 SITAVGSSALQPLVETASEEYQSQNPGRFINVQGGGSGTGLSQVQSGAvdigNSDLFAE-EKKGIKAedLIDHKVAVVGI 107
Cdd:cd13538    1 TLTVFAAASLTDAFTEIGEQFEKSNPGVKVTFNFAGSQALVTQIEQGA----PADVFASaDTANMDA--LVKAGLLVDTP 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486463988 108 TPIVnKNVGVKDISMENLKKIflgevTNWKELGGKDQKIVILNRA--AGSGTRATFEK----WVLGDKTAIRA----QEQ 177
Cdd:cd13538   75 TIFA-TNKLVVIVPKDNPAKI-----TSLADLAKPGVKIVIGAPEvpVGTYTRRVLDKagndYAYGYKEAVLAnvvsEET 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486463988 178 DssgmVRSIVS-------DtpgaisyTAFSYVTDevATLSIDGVQ----PTDENVMNNkwiiWSYEHMYTRKNPsDLTKE 246
Cdd:cd13538  149 N----VRDVVTkvalgeaD-------AGFVYVTD--AKAASEKLKvitiPEEYNVTAT----YPIAVLKASKNP-ELARA 210
                        250       260
                 ....*....|....*....|.
gi 486463988 247 FLDFMLSDDIQeRVIGQLGYI 267
Cdd:cd13538  211 FVDFLLSEEGQ-AILAEYGFG 230
SBP_bac_11 pfam13531
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ...
31-258 1.48e-04

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


Pssm-ID: 463911 [Multi-domain]  Cd Length: 225  Bit Score: 42.25  E-value: 1.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486463988   31 TAVGSSALQPLVETASEEYQsQNPGRFINVQGGGSGTGLSQVQSGA-VDI---GNSDLFAEekkgIKAEDLIDH-KVAVV 105
Cdd:pfam13531   1 TVAAAGGLAAALRELAAAFE-AETGVKVVVSYGGSGKLAKQIANGApADVfisADSAWLDK----LAAAGLVVPgSRVPL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486463988  106 GITPIVnknVGVKDismENLKKIflgevTNWKELGGKDQKIVILN-RAAGSG--TRATFEKWVLGDK--TAIRAQEQDSS 180
Cdd:pfam13531  76 AYSPLV---IAVPK---GNPKDI-----SGLADLLKPGVRLAVADpKTAPSGraALELLEKAGLLKAleKKVVVLGENVR 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486463988  181 GMVRSIVS-DTPGAISYTAFSYVTDEVATLSI----DGVQPTDENVMNnkwiiwsyehmYTRKNP-SDLTKEFLDFMLSD 254
Cdd:pfam13531 145 QALTAVASgEADAGIVYLSEALFPENGPGLEVvplpEDLNLPLDYPAA-----------VLKKAAhPEAARAFLDFLLSP 213

                  ....
gi 486463988  255 DIQE 258
Cdd:pfam13531 214 EAQA 217
PBP2_YvgL_like cd13537
Substrate binding domain of putative molybdate-binding protein YvgL and similar proteins;the ...
47-132 3.91e-03

Substrate binding domain of putative molybdate-binding protein YvgL and similar proteins;the type 2 periplasmic binding protein fold; This subfamily contains domains found in ModA proteins of putative ABC-type transporter. ModA proteins serve as initial receptors in the ABC transport of molybdate in eubacteria and archaea. Bacteria and archaea import molybdenum and tungsten from the environment in the form of the oxyanions molybdate (MoO(4) (2-)) and tungstate (WO(4) (2-)). After binding molybdate and tungstate with high affinity, they interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The ModA proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270255 [Multi-domain]  Cd Length: 225  Bit Score: 37.65  E-value: 3.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486463988  47 EEYQSQNPGRFINVQGGGSGTGLSQVQSGA-VDI----GNSDLFAEEKKG-IKAE---DLIDHKVAVvgitpIVNKNVGV 117
Cdd:cd13537   19 TEYEKENPGVKITFNFGGSGTLQKQIESGApADVffsaAKKQMDALEDKGlIDAStrkNLLKNKLVL-----IVPKDSDS 93
                         90
                 ....*....|....*....
gi 486463988 118 KDISMENL----KKIFLGE 132
Cdd:cd13537   94 KISSFDLTkddvKKIAIGE 112
PBP2_TbpA cd13545
Substrate binding domain of thiamin transporter, a member of the type 2 periplasmic binding ...
181-258 5.88e-03

Substrate binding domain of thiamin transporter, a member of the type 2 periplasmic binding fold superfamily; Thiamin-binding protein TbpA is the periplasmic component of ABC-type transporter in E. coli, while the transmembrane permease and ATPase are ThiP and ThiQ, respectively. Thiamin (vitamin B1) is an essential confactor in all living systems that most prokaryotes, plants, and fungi can synthesized thiamin. However, in vertebrates, thiamine cannot be synthesized and must therefore be obtained through dietary absorption. In addition to thiamin biosynthesis, most organisms can import thiamin using specific transporters. After binding thiamine with high affinity, TbpA interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The thiamine-binding proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270263 [Multi-domain]  Cd Length: 269  Bit Score: 37.66  E-value: 5.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 486463988 181 GMVRSIVSDTPG-AISYTAF---------SYVTDEVATLSIDGVQPTDENVMNN-KWIiwSYEHM---YTRKNPsDLTKE 246
Cdd:cd13545  168 KLKANGVTVTPGwSEAYGLFttgeapmvvSYATSPAYHVYYEKDLRYTAVIFPEgHYR--QVEGAgilKGAKNP-ELAKK 244
                         90
                 ....*....|..
gi 486463988 247 FLDFMLSDDIQE 258
Cdd:cd13545  245 FVDFLLSPEFQE 256
 
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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