|
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
|
|
|