|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10957 |
PRK10957 |
iron-enterobactin transporter periplasmic binding protein; Provisional |
5-319 |
0e+00 |
|
iron-enterobactin transporter periplasmic binding protein; Provisional
Pssm-ID: 236806 [Multi-domain] Cd Length: 317 Bit Score: 535.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490249439 5 SFCRRGALTGMLLLLGITSA--QAADWPRQVTDSYGTHTLPSQPLRIVSTSVTLTGSLLAIDAPVVASGATTPNNRVADS 82
Cdd:PRK10957 1 PLYRLALLLLGLLLSGIAAAqaSAAGWPRTVTDSRGSVTLESKPQRIVSTSVTLTGTLLAIDAPVIASGATTPNTRVADD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490249439 83 QGFLRQWSEVAKARKLARLYIGEPSAEAVAAQMPDLILVSATGGDSALPLYDQLKTIAPTLVINYDDKSWQTLLTQLGQI 162
Cdd:PRK10957 81 QGFFRQWSDVAKERGVEVLYIGEPDAEAVAAQMPDLIVISATGGDSALALYDQLSAIAPTLVIDYDDKSWQELATQLGEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490249439 163 TGHEQQASARIADFNKQLVSLKEKMKLPPQPVTALVYTAAAHSANIWTPESAQGQMLEQLGFSLATLPGGLPASHSQGKR 242
Cdd:PRK10957 161 TGLEKQAAAVIAQFDAQLAEVKAKITLPPQPVSALVYNGAGHSANLWTPESAQGQLLEQLGFTLAELPAGLQASTSQGKR 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490249439 243 HDIVQLGGENLAAGLNGQSLFLFAGDQKDADAIYANPLLAHLPAVAGKRVYPLGTETFRLDYYSALLVLQRLSSLFG 319
Cdd:PRK10957 241 HDIIQLGGENLAAGLNGETLFLFAGDDKDADAFLADPLLANLPAVQNKQVYALGTDTFRLDYYSATQLLDRLAALFG 317
|
|
| FepB |
COG4592 |
ABC-type Fe2+-enterobactin transport system, periplasmic component [Inorganic ion transport ... |
10-319 |
2.77e-177 |
|
ABC-type Fe2+-enterobactin transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443649 [Multi-domain] Cd Length: 330 Bit Score: 493.31 E-value: 2.77e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490249439 10 GALTGMLLLLGITSAQAADWPRQVTDSYGTHTLPSQPLRIVSTSVTLTGSLLAIDAPVVASGATTPNNrVADSQGFLRQW 89
Cdd:COG4592 21 GCSSADSTASGTSTAAAGGWPRTVTTEKGTVTLPAKPQRIVSTSVTLTGSLLAIDAPVVASGATTPNN-VTDDQGFFRQW 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490249439 90 SEVAKARKLARLYIG-EPSAEAVAAQMPDLILVSATGGDSALPLYDQLKTIAPTLVINYDDKSWQTLLTQLGQITGHEQQ 168
Cdd:COG4592 100 ADVAKERGVKRLYIGlEPNAEAIAAAAPDLIIGSATGGDSALDLYDQLSAIAPTLVVNYDDKSWQELATQLGEATGHEAQ 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490249439 169 ASARIADFNKQLVSLKEKMKLPPQPVTALVYTAAAhSANIWTPESAQGQMLEQLGFSLATLPGGLPASHSQGKRHDIVQL 248
Cdd:COG4592 180 ADAVIAAFDARVAEVKAAITLPPQPVSALVYNEDG-GANLWTPESAQGQLLQALGFTLAPLPAELATSTSQGKRGDIVQL 258
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490249439 249 GGENLAAGLNGQSLFLFAGDQKDADAIYANPLLAHLPAVAGKRVYPLGTETFRLDYYSALLVLQRLSSLFG 319
Cdd:COG4592 259 SGENLAAALTGPTLFLFAADDKDVDALKADPLLAHLPAVQAGRVYALGPDSFRLDYYSASNLLDRLEKLFG 329
|
|
| FhuD |
cd01146 |
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial ... |
44-313 |
2.57e-54 |
|
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial receptors in ABC transport of Fe3+-siderophores in many eubacterial species. They belong to the TroA-like superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA-like protein is comprised of two globular subdomains connected by a long alpha helix and binds its specific ligands in the cleft between these domains.
Pssm-ID: 238566 [Multi-domain] Cd Length: 256 Bit Score: 177.86 E-value: 2.57e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490249439 44 SQPLRIVSTSVTLTGSLLAIDAPVVAsgattpnnrVADSQGFlRQWSEVAKARKLARLYIG---EPSAEAVAAQMPDLIL 120
Cdd:cd01146 1 AKPQRIVALDWGALETLLALGVKPVG---------VADTAGY-KPWIPEPALPLEGVVDVGtrgQPNLEAIAALKPDLIL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490249439 121 VSATGGDsalPLYDQLKTIAPTLVINY--DDKSWQTLLTQLGQITGHEQQASARIADFNKQLVSLKEKMKLPPQPVTALV 198
Cdd:cd01146 71 GSASRHD---EIYDQLSQIAPTVLLDSspWLAEWKENLRLIAKALGKEEEAEKLLAEYDQRLAELRQKLPDKGPKPVSVV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490249439 199 YTAAAHSANIWTPESAQGQMLEQLGFSLATLPgglpashSQGKRHDIVQLGGENLAAgLNGQSLFLFA-GDQKDADAIYA 277
Cdd:cd01146 148 RFSDAGSIRLYGPNSFAGSVLEDLGLQNPWAQ-------ETTNDSGFATISLERLAK-ADADVLFVFTyEDEELAQALQA 219
|
250 260 270
....*....|....*....|....*....|....*..
gi 490249439 278 NPLLAHLPAVAGKRVYPLGTET-FRLDYYSALLVLQR 313
Cdd:cd01146 220 NPLWQNLPAVKNGRVYVVDDVWwFFGGGLSAARLLLD 256
|
|
| Peripla_BP_2 |
pfam01497 |
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ... |
50-293 |
9.33e-19 |
|
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding proteins, several of which are involved in iron and cobalamin transport. Among its ligands are siderophores bacillibactin, enterobactin and iron(III)-hydroxamates (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1 https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 426291 [Multi-domain] Cd Length: 233 Bit Score: 83.57 E-value: 9.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490249439 50 VSTSVTLTGSLLAIDA--PVVASGATTPNNRVADsqgflrqwsevAKARKLARLYIGEPSAEAVAAQMPDLILVSATGGD 127
Cdd:pfam01497 1 AALSPAYTEILYALGAtdSIVGVDAYTRDPLKAD-----------AVAAIVKVGAYGEINVERLAALKPDLVILSTGYLT 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490249439 128 SALplYDQLKTIAPTLVINYDDK--SWQTLLTQLGQITGHEQQASARIADFNKQLVSLKEKMKLPPQPVTALVYTAAAHS 205
Cdd:pfam01497 70 DEA--EELLSLIIPTVIFESSSTgeSLKEQIKQLGELLGLEDEAEELVAEIDSALAAAKKAVPSLTRKPVLVFGGADGGG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490249439 206 ANIWTPESAQGQMLEQLGFSLATlpgglpASHSQGKRhdiVQLGGENLAAgLNGQSLFLFAGD---QKDADAIYANPLLA 282
Cdd:pfam01497 148 YVVAGSNTYIGDLLRILGIENIA------AELSGSEY---APISFEAILS-SNPDVIIVSGRDsftKTGPEFVAANPLWA 217
|
250
....*....|.
gi 490249439 283 HLPAVAGKRVY 293
Cdd:pfam01497 218 GLPAVKNGRVY 228
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10957 |
PRK10957 |
iron-enterobactin transporter periplasmic binding protein; Provisional |
5-319 |
0e+00 |
|
iron-enterobactin transporter periplasmic binding protein; Provisional
Pssm-ID: 236806 [Multi-domain] Cd Length: 317 Bit Score: 535.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490249439 5 SFCRRGALTGMLLLLGITSA--QAADWPRQVTDSYGTHTLPSQPLRIVSTSVTLTGSLLAIDAPVVASGATTPNNRVADS 82
Cdd:PRK10957 1 PLYRLALLLLGLLLSGIAAAqaSAAGWPRTVTDSRGSVTLESKPQRIVSTSVTLTGTLLAIDAPVIASGATTPNTRVADD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490249439 83 QGFLRQWSEVAKARKLARLYIGEPSAEAVAAQMPDLILVSATGGDSALPLYDQLKTIAPTLVINYDDKSWQTLLTQLGQI 162
Cdd:PRK10957 81 QGFFRQWSDVAKERGVEVLYIGEPDAEAVAAQMPDLIVISATGGDSALALYDQLSAIAPTLVIDYDDKSWQELATQLGEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490249439 163 TGHEQQASARIADFNKQLVSLKEKMKLPPQPVTALVYTAAAHSANIWTPESAQGQMLEQLGFSLATLPGGLPASHSQGKR 242
Cdd:PRK10957 161 TGLEKQAAAVIAQFDAQLAEVKAKITLPPQPVSALVYNGAGHSANLWTPESAQGQLLEQLGFTLAELPAGLQASTSQGKR 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490249439 243 HDIVQLGGENLAAGLNGQSLFLFAGDQKDADAIYANPLLAHLPAVAGKRVYPLGTETFRLDYYSALLVLQRLSSLFG 319
Cdd:PRK10957 241 HDIIQLGGENLAAGLNGETLFLFAGDDKDADAFLADPLLANLPAVQNKQVYALGTDTFRLDYYSATQLLDRLAALFG 317
|
|
| FepB |
COG4592 |
ABC-type Fe2+-enterobactin transport system, periplasmic component [Inorganic ion transport ... |
10-319 |
2.77e-177 |
|
ABC-type Fe2+-enterobactin transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443649 [Multi-domain] Cd Length: 330 Bit Score: 493.31 E-value: 2.77e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490249439 10 GALTGMLLLLGITSAQAADWPRQVTDSYGTHTLPSQPLRIVSTSVTLTGSLLAIDAPVVASGATTPNNrVADSQGFLRQW 89
Cdd:COG4592 21 GCSSADSTASGTSTAAAGGWPRTVTTEKGTVTLPAKPQRIVSTSVTLTGSLLAIDAPVVASGATTPNN-VTDDQGFFRQW 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490249439 90 SEVAKARKLARLYIG-EPSAEAVAAQMPDLILVSATGGDSALPLYDQLKTIAPTLVINYDDKSWQTLLTQLGQITGHEQQ 168
Cdd:COG4592 100 ADVAKERGVKRLYIGlEPNAEAIAAAAPDLIIGSATGGDSALDLYDQLSAIAPTLVVNYDDKSWQELATQLGEATGHEAQ 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490249439 169 ASARIADFNKQLVSLKEKMKLPPQPVTALVYTAAAhSANIWTPESAQGQMLEQLGFSLATLPGGLPASHSQGKRHDIVQL 248
Cdd:COG4592 180 ADAVIAAFDARVAEVKAAITLPPQPVSALVYNEDG-GANLWTPESAQGQLLQALGFTLAPLPAELATSTSQGKRGDIVQL 258
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490249439 249 GGENLAAGLNGQSLFLFAGDQKDADAIYANPLLAHLPAVAGKRVYPLGTETFRLDYYSALLVLQRLSSLFG 319
Cdd:COG4592 259 SGENLAAALTGPTLFLFAADDKDVDALKADPLLAHLPAVQAGRVYALGPDSFRLDYYSASNLLDRLEKLFG 329
|
|
| FhuD |
cd01146 |
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial ... |
44-313 |
2.57e-54 |
|
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial receptors in ABC transport of Fe3+-siderophores in many eubacterial species. They belong to the TroA-like superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA-like protein is comprised of two globular subdomains connected by a long alpha helix and binds its specific ligands in the cleft between these domains.
Pssm-ID: 238566 [Multi-domain] Cd Length: 256 Bit Score: 177.86 E-value: 2.57e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490249439 44 SQPLRIVSTSVTLTGSLLAIDAPVVAsgattpnnrVADSQGFlRQWSEVAKARKLARLYIG---EPSAEAVAAQMPDLIL 120
Cdd:cd01146 1 AKPQRIVALDWGALETLLALGVKPVG---------VADTAGY-KPWIPEPALPLEGVVDVGtrgQPNLEAIAALKPDLIL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490249439 121 VSATGGDsalPLYDQLKTIAPTLVINY--DDKSWQTLLTQLGQITGHEQQASARIADFNKQLVSLKEKMKLPPQPVTALV 198
Cdd:cd01146 71 GSASRHD---EIYDQLSQIAPTVLLDSspWLAEWKENLRLIAKALGKEEEAEKLLAEYDQRLAELRQKLPDKGPKPVSVV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490249439 199 YTAAAHSANIWTPESAQGQMLEQLGFSLATLPgglpashSQGKRHDIVQLGGENLAAgLNGQSLFLFA-GDQKDADAIYA 277
Cdd:cd01146 148 RFSDAGSIRLYGPNSFAGSVLEDLGLQNPWAQ-------ETTNDSGFATISLERLAK-ADADVLFVFTyEDEELAQALQA 219
|
250 260 270
....*....|....*....|....*....|....*..
gi 490249439 278 NPLLAHLPAVAGKRVYPLGTET-FRLDYYSALLVLQR 313
Cdd:cd01146 220 NPLWQNLPAVKNGRVYVVDDVWwFFGGGLSAARLLLD 256
|
|
| FecB |
COG4594 |
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and ... |
1-295 |
4.94e-36 |
|
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443650 [Multi-domain] Cd Length: 316 Bit Score: 131.97 E-value: 4.94e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490249439 1 MNFFSFcRRGALTGMLLLLG-------ITSAQAADWPRQVTDSYGTHTLPSQPLRIVSTSVTLTGSLLAID-APVvasGa 72
Cdd:COG4594 1 MKKLLL-LLILLLALLLLAAcgssssdSSSSEAAAGARTVKHAMGETTIPGTPKRVVVLEWSFADALLALGvTPV---G- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490249439 73 ttpnnrVADSQGFLRqWseVAKARKLARLY--IG---EPSAEAVAAQMPDLILVSATGGDSalpLYDQLKTIAPTLVINY 147
Cdd:COG4594 76 ------IADDNDYDR-W--VPYLRDLIKGVtsVGtrsQPNLEAIAALKPDLIIADKSRHEA---IYDQLSKIAPTVLFKS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490249439 148 DDKSWQTLLTQ---LGQITGHEQQASARIADFNKQLVSLKEKMKLPPQPVTALVYTAAAHSANIWTPESAQGQMLEQLGF 224
Cdd:COG4594 144 RNGDYQENLESfktIAKALGKEEEAEAVLADHDQRIAEAKAKLAAADKGKKVAVGQFRADGLRLYTPNSFAGSVLAALGF 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490249439 225 SlatlpggLPASHSQGKRHDIVQLGGENLAAgLNGQSLFLFA-GDQKDADAIYANPLLAHLPAVAGKRVYPL 295
Cdd:COG4594 224 E-------NPPKQSKDNGYGYSEVSLEQLPA-LDPDVLFIATyDDPSILKEWKNNPLWKNLKAVKNGRVYEV 287
|
|
| FepB |
COG0614 |
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ... |
48-312 |
1.69e-31 |
|
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 440379 [Multi-domain] Cd Length: 264 Bit Score: 118.56 E-value: 1.69e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490249439 48 RIVSTSVTLTGSLLAIDAP--VVAsgattpnnrVADSQGFLRQWSEVAKARKLARlyIGEPSAEAVAAQMPDLILVSATG 125
Cdd:COG0614 2 RIVSLSPSATELLLALGAGdrLVG---------VSDWGYCDYPELELKDLPVVGG--TGEPNLEAILALKPDLVLASSSG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490249439 126 GDSALplYDQLKTI-APTLVINYDD-KSWQTLLTQLGQITGHEQQASARIADFNKQLVSLKEKMKLPPQPVTALVYTAAA 203
Cdd:COG0614 71 NDEED--YEQLEKIgIPVVVLDPRSlEDLYESIRLLGELLGREERAEALIAEYEARLAAVRARLAGAEERPTVLYEIWSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490249439 204 HSANIWTPESAQGQMLEQLGFS--LATLPGGLPashsqgkrhdivQLGGENLAAgLNGQSLFLFAGD------QKDADAI 275
Cdd:COG0614 149 DPLYTAGGGSFIGELLELAGGRnvAADLGGGYP------------EVSLEQVLA-LDPDVIILSGGGydaetaEEALEAL 215
|
250 260 270
....*....|....*....|....*....|....*..
gi 490249439 276 YANPLLAHLPAVAGKRVYPLGTETFRldYYSALLVLQ 312
Cdd:COG0614 216 LADPGWQSLPAVKNGRVYVVPGDLLS--RPGPRLLLA 250
|
|
| FeuA |
cd01138 |
Periplasmic binding protein FeuA. These proteins have predicted to function as initial ... |
38-293 |
1.21e-20 |
|
Periplasmic binding protein FeuA. These proteins have predicted to function as initial receptors in ABC transport of metal ions in some eubacterial species. They belong to the TroA superfamily of periplasmic metal binding proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind their ligands in the cleft between these domains.
Pssm-ID: 238558 [Multi-domain] Cd Length: 248 Bit Score: 88.93 E-value: 1.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490249439 38 GTHTLPSQPLRIVSTSVTLTGsLLAIDAPVVASGATTPNNRVADSQGFLRQWSEVAkarklarlyigEPSAEAVAAQMPD 117
Cdd:cd01138 1 GEVEIPAKPKRIVALSGETEG-LALLGIKPVGAASIGGKNPYYKKKTLAKVVGIVD-----------EPNLEKVLELKPD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490249439 118 LILVSatggDSALPLYDQLKTIAPTLVINYDDKSWQTLLTQLGQITGHEQQASARIADFNKQLVSLKEKMKLPPQPVTAL 197
Cdd:cd01138 69 LIIVS----SKQEENYEKLSKIAPTVPVSYNSSDWEEQLKEIGKLLNKEDEAEKWLADYKQKAKEAKEKIKKKLGNDKSV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490249439 198 vytaaahsANIWTpesaQGQML---EQLGFSLATLPG--GLPAS---HSQGKRHDIVQLGGENLAAgLNGQSLFLFAGDQ 269
Cdd:cd01138 145 --------AVLRG----RKQIYvfgEDGRGGGPILYAdlGLKAPekvKEIEDKPGYAAISLEVLPE-FDADYIFLLFFTG 211
|
250 260
....*....|....*....|....*
gi 490249439 270 KDADAIY-ANPLLAHLPAVAGKRVY 293
Cdd:cd01138 212 PEAKADFeSLPIWKNLPAVKNNHVY 236
|
|
| Peripla_BP_2 |
pfam01497 |
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ... |
50-293 |
9.33e-19 |
|
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding proteins, several of which are involved in iron and cobalamin transport. Among its ligands are siderophores bacillibactin, enterobactin and iron(III)-hydroxamates (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1 https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 426291 [Multi-domain] Cd Length: 233 Bit Score: 83.57 E-value: 9.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490249439 50 VSTSVTLTGSLLAIDA--PVVASGATTPNNRVADsqgflrqwsevAKARKLARLYIGEPSAEAVAAQMPDLILVSATGGD 127
Cdd:pfam01497 1 AALSPAYTEILYALGAtdSIVGVDAYTRDPLKAD-----------AVAAIVKVGAYGEINVERLAALKPDLVILSTGYLT 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490249439 128 SALplYDQLKTIAPTLVINYDDK--SWQTLLTQLGQITGHEQQASARIADFNKQLVSLKEKMKLPPQPVTALVYTAAAHS 205
Cdd:pfam01497 70 DEA--EELLSLIIPTVIFESSSTgeSLKEQIKQLGELLGLEDEAEELVAEIDSALAAAKKAVPSLTRKPVLVFGGADGGG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490249439 206 ANIWTPESAQGQMLEQLGFSLATlpgglpASHSQGKRhdiVQLGGENLAAgLNGQSLFLFAGD---QKDADAIYANPLLA 282
Cdd:pfam01497 148 YVVAGSNTYIGDLLRILGIENIA------AELSGSEY---APISFEAILS-SNPDVIIVSGRDsftKTGPEFVAANPLWA 217
|
250
....*....|.
gi 490249439 283 HLPAVAGKRVY 293
Cdd:pfam01497 218 GLPAVKNGRVY 228
|
|
| fecB |
PRK11411 |
iron-dicitrate transporter substrate-binding subunit; Provisional |
9-230 |
2.56e-18 |
|
iron-dicitrate transporter substrate-binding subunit; Provisional
Pssm-ID: 183123 [Multi-domain] Cd Length: 303 Bit Score: 83.57 E-value: 2.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490249439 9 RGALTGMLLLLGITSAQAADwprqVTDSYGTHTLPSQPLRIVSTSVTLTGSLLAID-APVVASGATTPNNRVADSQGFLR 87
Cdd:PRK11411 6 RLLFAGLLLLSGSSHAFAVT----VQDEQGTFTLEKTPQRIVVLELSFVDALAAVGvSPVGVADDNDAKRILPEVRAHLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490249439 88 QWSEVAkARklarlyiGEPSAEAVAAQMPDLIlVSATGGDSAlpLYDQLKTIAPTLVINYDDKSWQTLL---TQLGQITG 164
Cdd:PRK11411 82 PWQSVG-TR-------SQPSLEAIAALKPDLI-IADSSRHAG--VYIALQKIAPTLLLKSRNETYQENLqsaAIIGEVLG 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490249439 165 HEQQASARIADFNKQLVSLKEKMklpPQPVTALVYTAAAHSANIWTPESAQGQMLEQLGFSLATLP 230
Cdd:PRK11411 151 KKREMQARIEQHKERMAQFASQL---PKGTRVAFGTSREQQFNLHSPESYTGSVLAALGLNVPKAP 213
|
|
| TroA-like |
cd00636 |
Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function ... |
47-198 |
1.96e-17 |
|
Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function in the ABC transport of ferric siderophores and metal ions such as Mn2+, Fe3+, Cu2+ and/or Zn2+. Their ligand binding site is formed in the interface between two globular domains linked by a single helix. Many of these proteins also possess a low complexity region containing a metal-binding histidine-rich motif (repetitive HDH sequence). The TroA-like proteins differ in their fold and ligand-binding mechanism from the PBPI and PBPII proteins, but are structurally similar, however, to the beta-subunit of the nitrogenase molybdenum-iron protein MoFe. Most TroA-like proteins are encoded by ABC-type operons and appear to function as periplasmic components of ABC transporters in metal ion uptake.
Pssm-ID: 238347 [Multi-domain] Cd Length: 148 Bit Score: 77.60 E-value: 1.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490249439 47 LRIVSTSVTLTGSLLAIDAPVVASGATTPNNRVADSQGFLRQWSEVakarklarLYIGEPSAEAVAAQMPDLILVSATGG 126
Cdd:cd00636 1 KRVVALDPGATELLLALGGDDKPVGVADPSGYPPEAKALLEKVPDV--------GHGYEPNLEKIAALKPDLIIANGSGL 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490249439 127 DsalPLYDQLKTIA-PTLVIN----YDDKSWQTLLTQLGQITGHEQQASARIADFNKQLVSLKEKMKLPPQPVTALV 198
Cdd:cd00636 73 E---AWLDKLSKIAiPVVVVDeaseLSLENIKESIRLIGKALGKEENAEELIAELDARLAELRAKLAKIPKKKVSLV 146
|
|
| FatB |
cd01140 |
Siderophore binding protein FatB. These proteins have been shown to function as ABC-type ... |
35-300 |
2.00e-17 |
|
Siderophore binding protein FatB. These proteins have been shown to function as ABC-type initial receptors in the siderophore-mediated iron uptake in some eubacterial species. They belong to the TroA superfamily of periplasmic metal binding proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind their ligands in the cleft between these domains.
Pssm-ID: 238560 [Multi-domain] Cd Length: 270 Bit Score: 80.38 E-value: 2.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490249439 35 DSYGTHTLPSQPLRIVSTSVTLTGSLLAIDAPVVA--SGATTPNNrvadsqgflrqwseVAKARKLARLYIG---EPSAE 109
Cdd:cd01140 1 HALGETKVPKNPEKVVVFDVGALDTLDALGVKVVGvpKSSTLPEY--------------LKKYKDDKYANVGtlfEPDLE 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490249439 110 AVAAQMPDLILVSATGGDSalplYDQLKTIAPTLVINYD-DKSWQTLLTQ---LGQITGHEQQASARIADFNKQLVSLKE 185
Cdd:cd01140 67 AIAALKPDLIIIGGRLAEK----YDELKKIAPTIDLGADlKNYLESVKQNietLGKIFGKEEEAKELVAEIDASIAEAKS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490249439 186 KMKLPPqpvTALVYTAAAHSANIWTPESAQGQMLEQLGFSlatlpgglPAShsqgkrhdivqlggENLAAGLNGQS---- 261
Cdd:cd01140 143 AAKGKK---KALVVLVNGGKLSAFGPGSRFGWLHDLLGFE--------PAD--------------ENIKASSHGQPvsfe 197
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 490249439 262 ---------LFLFAGDQ------KDADAIYANPLLAHLPAVAGKRVYPLGTETF 300
Cdd:cd01140 198 yileanpdwLFVIDRGAaigaegSSAKEVLDNDLVKNTTAWKNGKVIYLDPDLW 251
|
|
| HemV-2 |
cd01147 |
Metal binding protein HemV-2. These proteins are predicted to function as initial receptors ... |
48-300 |
1.79e-12 |
|
Metal binding protein HemV-2. These proteins are predicted to function as initial receptors in ABC transport of metal ions. They belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind the metal ion in the cleft between these domains. In addition, these proteins sometimes have a low complexity region containing a metal-binding histidine-rich motif (repetitive HDH sequence).
Pssm-ID: 238567 [Multi-domain] Cd Length: 262 Bit Score: 66.20 E-value: 1.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490249439 48 RIVSTSVTLTGSLLAIDAP--VVASGATTpnnRVADSQGFLRQWSEVAKARKLARLYIG-EPSAEAVAAQMPDLILvsAT 124
Cdd:cd01147 7 RVVAAGPGALRLLYALAAPdkIVGVDDAE---KSDEGRPYFLASPELKDLPVIGRGGRGnTPNYEKIAALKPDVVI--DV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490249439 125 GGDSALPLYDQLKTIA--PTLVINY--DDKSWQTLLTQLGQITGHEQQASARIADFNKQLVSLKEKMK-LPPQPVTAlVY 199
Cdd:cd01147 82 GSDDPTSIADDLQKKTgiPVVVLDGgdSLEDTPEQIRLLGKVLGKEERAEELISFIESILADVEERTKdIPDEEKPT-VY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490249439 200 TAAAHSANIWtpesaqgqmleqlGFSlATLPGGLPAshsqgkrhdIVQLGGENLAAGLNGQSLF--------------LF 265
Cdd:cd01147 161 FGRIGTKGAA-------------GLE-SGLAGSIEV---------FELAGGINVADGLGGGGLKevspeqillwnpdvIF 217
|
250 260 270
....*....|....*....|....*....|....*....
gi 490249439 266 AGDQKDADAIY----ANPLLAHLPAVAGKRVYPLGTETF 300
Cdd:cd01147 218 LDTGSFYLSLEgyakNRPFWQSLKAVKNGRVYLLPALPF 256
|
|
| TroA_e |
cd01142 |
Periplasmic binding protein TroA_e. These proteins are predicted to function as initial ... |
22-314 |
1.59e-11 |
|
Periplasmic binding protein TroA_e. These proteins are predicted to function as initial receptors in the ABC metal ion uptake in eubacteria and archaea. They belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind their ligands in the cleft between these domains.
Pssm-ID: 238562 [Multi-domain] Cd Length: 289 Bit Score: 63.91 E-value: 1.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490249439 22 TSAQAADwpRQVTDSYGTH-TLPSQPLRIVSTSVTLTGSLLAIDAPVVASGATTPNNRVADSQGFLRQWSEVAKARKLAr 100
Cdd:cd01142 1 PAATAAT--RTITDMAGRKvTIPDEVKRIAALWGAGNAVVAALGGGKLIVATTSTVQQEPWLYRLAPSLENVATGGTGN- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490249439 101 lyigEPSAEAVAAQMPDLILVSATGGDSALplyDQLKTIAPTLVINYDDKS-WQTLLTQLGQITGHEQQASARIADFNKQ 179
Cdd:cd01142 78 ----DVNIEELLALKPDVVIVWSTDGKEAG---KAVLRLLNALSLRDAELEeVKLTIALLGELLGRQEKAEALVAYFDDN 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490249439 180 LVSLKEKMKLPPQPVTALVYTAAAHSANIWTPESAQGQMLEqlgfslatLPGGLP-ASHSQGKRHDIVQLggENLAAgLN 258
Cdd:cd01142 151 LAYVAARTKKLPDSERPRVYYAGPDPLTTDGTGSITNSWID--------LAGGINvASEATKKGSGEVSL--EQLLK-WN 219
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 490249439 259 GQslFLFAGDQKDADAIYANPLLAHLPAVAGKRVYPLGTETFRLDYYSALLVLQRL 314
Cdd:cd01142 220 PD--VIIVGNADTKAAILADPRWQNLRAVKNGRVYVNPEGAFWWDRPSAEEALLGL 273
|
|
| YvrC |
cd01143 |
Periplasmic binding protein YvrC. These proteins are predicted to function as initial ... |
44-223 |
1.26e-09 |
|
Periplasmic binding protein YvrC. These proteins are predicted to function as initial receptors in ABC transport of metal ions in eubacteria and archaea. They belong to the TroA superfamily of periplasmic metal binding proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind the metal ion in the cleft between these domains.
Pssm-ID: 238563 [Multi-domain] Cd Length: 195 Bit Score: 56.90 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490249439 44 SQPLRIVSTSVTLTGSLLAIDA--PVVASGATT---PNNRVADSQGflrqwsevakarklarlYIGEPSAEAVAAQMPDL 118
Cdd:cd01143 1 KEPERIVSLSPSITEILFALGAgdKIVGVDTYSnypKEVRKKPKVG-----------------SYSNPNVEKIVALKPDL 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490249439 119 ILVSATGGDSalpLYDQLKTIAPTLVINYDDKSWQTLL---TQLGQITGHEQQASARIADFNKQLVSLKEKMKLPPQPVT 195
Cdd:cd01143 64 VIVSSSSLAE---LLEKLKDAGIPVVVLPAASSLDEIYdqiELIGKITGAEEEAEKLVKEMKQKIDKVKDKGKTIKKSKV 140
|
170 180 190
....*....|....*....|....*....|.
gi 490249439 196 -ALVYTaaahsANIWT--PESAQGQMLEQLG 223
Cdd:cd01143 141 yIEVSL-----GGPYTagKNTFINELIRLAG 166
|
|
| ChuT |
COG4558 |
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism] ... |
93-295 |
2.44e-07 |
|
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443619 [Multi-domain] Cd Length: 285 Bit Score: 51.35 E-value: 2.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490249439 93 AKARKLARL-YIGEPSAEAVAAQMPDLILVSATGG-DSALplyDQLKTIAPTLVINYDDKSWQTLL---TQLGQITGHEQ 167
Cdd:COG4558 61 AAAKALPDVgYMRQLSAEGILSLKPTLVLASEGAGpPEVL---DQLRAAGVPVVVVPAAPSLEGVLakiRAVAAALGVPE 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490249439 168 QASARIADFNKQLVSLKEKMKLPPQPVTAL-VYTAAAHSANIWTPESAQGQMLEqlgfslatlpgglpashsqgkrhdiv 246
Cdd:COG4558 138 AGEALAARLEADLAALAARVAAIGKPPRVLfLLSRGGGRPMVAGRGTAADALIR-------------------------- 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490249439 247 QLGGENLAAGLNG--------------QSLFLFAGDQK---DADAIYANPLLAHLPAVAGKRVYPL 295
Cdd:COG4558 192 LAGGVNAAAGFEGykplsaealiaaapDVILVMTRGLEslgGVDGLLALPGLAQTPAGKNKRIVAM 257
|
|
| HutB |
cd01149 |
Hemin binding protein HutB. These proteins have been shown to function as initial receptors ... |
46-295 |
2.13e-05 |
|
Hemin binding protein HutB. These proteins have been shown to function as initial receptors in ABC transport of hemin and hemoproteins in many eubacterial species. They belong to the TroA superfamily of periplasmic metal binding proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind the metal ion in the cleft between these domains.
Pssm-ID: 238569 [Multi-domain] Cd Length: 235 Bit Score: 44.95 E-value: 2.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490249439 46 PLRIVSTSVTLTGSLLAIDAP--VVASGATTpnnrvadsqgflrQWSEVAKarKLARL-YIGEPSAEAVAAQMPDLILVS 122
Cdd:cd01149 1 PERIVSLGGSVTEIVYALGAGdrLVGVDSTS-------------TYPEAAA--KLPDVgYMRQLSAEGVLSLKPTLVIAS 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490249439 123 A-TGGDSALplyDQLKTIAPTLVINYDDKSWQTLLT---QLGQITGHEQQASARIADFNKQLVSL-KEKMKLPPQPVTAL 197
Cdd:cd01149 66 DeAGPPEAL---DQLRAAGVPVVTVPSTPTLDGLLTkirQVAQALGVPEKGEALAQEVRQRLAALrKTVAAHKKPPRVLF 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490249439 198 VYTAAAHSANIWTPESAQGQMLEqlgfsLAtlpgglpashsqgkrhdivqlGGENLAAGLNGQS---------------L 262
Cdd:cd01149 143 LLSHGGGAAMAAGRNTAADAIIA-----LA---------------------GAVNAAAGFRGYKplsaealiaaqpdviL 196
|
250 260 270
....*....|....*....|....*....|....*
gi 490249439 263 FLFAGDQKDA--DAIYANPLLAHLPAVAGKRVYPL 295
Cdd:cd01149 197 VMSRGLDAVGgvDGLLKLPGLAQTPAGRNKRILAM 231
|
|
| PRK10576 |
PRK10576 |
Fe(3+)-hydroxamate ABC transporter substrate-binding protein FhuD; |
105-292 |
1.80e-04 |
|
Fe(3+)-hydroxamate ABC transporter substrate-binding protein FhuD;
Pssm-ID: 236719 Cd Length: 292 Bit Score: 42.69 E-value: 1.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490249439 105 EPSAEAVAAQMPDLILVSATGGDSAlplyDQLKTIAPTLVINYDD-----KSWQTLLTQLGQITGHEQQASARIADFNKQ 179
Cdd:PRK10576 83 EPNLELLTQMKPSLILWSAGYGPSP----EKLARIAPGRGFAFSDgkkplAVARKSLVELAQRLNLEAAAETHLAQFDDF 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490249439 180 LVSLKEKM-KLPPQPVTALVYTAAAHsANIWTPESAQGQMLEQLGFSLATlpgglpashsQGKRH----DIVqlGGENLA 254
Cdd:PRK10576 159 IASAKPRLaGRGQRPLLLTSLIDPRH-ALVFGPNSLFQEVLDELGIENAW----------QGETNfwgsTVV--GIERLA 225
|
170 180 190
....*....|....*....|....*....|....*...
gi 490249439 255 AGLNGQSLFLFAGDQKDADAIYANPLLAHLPAVAGKRV 292
Cdd:PRK10576 226 AYKDADVICFDHGNSKDMQQLMATPLWQAMPFVRAGRF 263
|
|
| TroA_f |
cd01139 |
Periplasmic binding protein TroA_f. These proteins are predicted to function as initial ... |
33-295 |
6.49e-04 |
|
Periplasmic binding protein TroA_f. These proteins are predicted to function as initial receptors in the ABC metal ion uptake in eubacteria and archaea. They belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind their ligands in the cleft between these domains.
Pssm-ID: 238559 [Multi-domain] Cd Length: 342 Bit Score: 41.14 E-value: 6.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490249439 33 VTDSYG-THTLPSQPLRIV--STSVTLTGSLLAIDAPVvasgattpnNRVADSQGFLRQWSE------VAKARKLARL-- 101
Cdd:cd01139 3 VTDVAGrKVTLDAPVERVLlgEGRQLYALALLEGENPF---------ARIVGWGGDLKKGDPdtyakyKEKFPEIADIpl 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490249439 102 --YIGEP--SAEAVAAQMPDLILV--SATGGDSALPLYDQL-KTIAPTLVI---NYDDKSWQTLLTQLGQITGHEQQASA 171
Cdd:cd01139 74 igSTYNGdfSVEKVLTLKPDLVILniWAKTTAEESGILEKLeQAGIPVVFVdfrQKPLKNTTPSMRLLGKALGREERAEE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490249439 172 RIADFNKQLVSLKEKMK--LPPQPVTALVYTAAAHSANIWT-PESAQGQMLEQLGFS------LATLPGGLPASHSQGKR 242
Cdd:cd01139 154 FIEFYQERIDRIRDRLAkiNEPKPKVFIELGAGGPEECCSTyGNGNWGELVDAAGGDniadglIPGTSGELNAEYVIAAN 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 490249439 243 HDIVQLGGENLAAGLNGQSLFLFAGDQKDADAIYAN----PLLAHLPAVAGKRVYPL 295
Cdd:cd01139 234 PEIIIATGGNWAKDPSGVSLGPDGTTADAKESLLRAllkrPGWSSLQAVKNGRVYAL 290
|
|
| |
