|
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: 535.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714491 5 AVCRNALLLTGLFVLGLTSAAAD--DWPRQVTDSRGVHTLESKPTRIVSTSVTLTGSLLAIDAPVIASGATTPNNRVADA 82
Cdd:PRK10957 1 PLYRLALLLLGLLLSGIAAAQASaaGWPRTVTDSRGSVTLESKPQRIVSTSVTLTGTLLAIDAPVIASGATTPNTRVADD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714491 83 QGFLRQWGDIAKQRKVARLYIGEPSAEAVAAQMPDLILISATGGDSALALYDQLSAIAPTLIINYDDKSWQELLTQLGTI 162
Cdd:PRK10957 81 QGFFRQWSDVAKERGVEVLYIGEPDAEAVAAQMPDLIVISATGGDSALALYDQLSAIAPTLVIDYDDKSWQELATQLGEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714491 163 TGQETQAAERIAAFDKQLAKVKQQMKLPPQPVNAIVYTAAAHTANLWTTDSAQGKLLHQLGFTLADVPAGLHTSKSQGKR 242
Cdd:PRK10957 161 TGLEKQAAAVIAQFDAQLAEVKAKITLPPQPVSALVYNGAGHSANLWTPESAQGQLLEQLGFTLAELPAGLQASTSQGKR 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 550714491 243 HDIIQLGGENLATGLNGEGLFVFAGDQKDVDAIYANPLLAHLLSVKNKRVWALGTETFRLDYYSAMLVLQRLNSIFK 319
Cdd:PRK10957 241 HDIIQLGGENLAAGLNGETLFLFAGDDKDADAFLADPLLANLPAVQNKQVYALGTDTFRLDYYSATQLLDRLAALFG 317
|
|
| FepB |
COG4592 |
ABC-type Fe2+-enterobactin transport system, periplasmic component [Inorganic ion transport ... |
4-319 |
2.23e-178 |
|
ABC-type Fe2+-enterobactin transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443649 [Multi-domain] Cd Length: 330 Bit Score: 496.01 E-value: 2.23e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714491 4 AAVCRNALLLTG-----LFVLGLTSAAADDWPRQVTDSRGVHTLESKPTRIVSTSVTLTGSLLAIDAPVIASGATTPNNr 78
Cdd:COG4592 10 AALLAAALLLAGcssadSTASGTSTAAAGGWPRTVTTEKGTVTLPAKPQRIVSTSVTLTGSLLAIDAPVVASGATTPNN- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714491 79 VADAQGFLRQWGDIAKQRKVARLYIG-EPSAEAVAAQMPDLILISATGGDSALALYDQLSAIAPTLIINYDDKSWQELLT 157
Cdd:COG4592 89 VTDDQGFFRQWADVAKERGVKRLYIGlEPNAEAIAAAAPDLIIGSATGGDSALDLYDQLSAIAPTLVVNYDDKSWQELAT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714491 158 QLGTITGQETQAAERIAAFDKQLAKVKQQMKLPPQPVNAIVYTAAAhTANLWTTDSAQGKLLHQLGFTLADVPAGLHTSK 237
Cdd:COG4592 169 QLGEATGHEAQADAVIAAFDARVAEVKAAITLPPQPVSALVYNEDG-GANLWTPESAQGQLLQALGFTLAPLPAELATST 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714491 238 SQGKRHDIIQLGGENLATGLNGEGLFVFAGDQKDVDAIYANPLLAHLLSVKNKRVWALGTETFRLDYYSAMLVLQRLNSI 317
Cdd:COG4592 248 SQGKRGDIVQLSGENLAAALTGPTLFLFAADDKDVDALKADPLLAHLPAVQAGRVYALGPDSFRLDYYSASNLLDRLEKL 327
|
..
gi 550714491 318 FK 319
Cdd:COG4592 328 FG 329
|
|
| FhuD |
cd01146 |
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial ... |
44-313 |
5.70e-56 |
|
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: 182.10 E-value: 5.70e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714491 44 SKPTRIVSTSVTLTGSLLAIDAPVIAsgattpnnrVADAQGFlRQWGDIAKQRK---VARLYIGEPSAEAVAAQMPDLIL 120
Cdd:cd01146 1 AKPQRIVALDWGALETLLALGVKPVG---------VADTAGY-KPWIPEPALPLegvVDVGTRGQPNLEAIAALKPDLIL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714491 121 ISATGGDsalALYDQLSAIAPTLIINY--DDKSWQELLTQLGTITGQETQAAERIAAFDKQLAKVKQQMKLPPQPVNAIV 198
Cdd:cd01146 71 GSASRHD---EIYDQLSQIAPTVLLDSspWLAEWKENLRLIAKALGKEEEAEKLLAEYDQRLAELRQKLPDKGPKPVSVV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714491 199 YTAAAHTANLWTTDSAQGKLLHQLGFTLADVPaglhtskSQGKRHDIIQLGGENLAtGLNGEGLFVFA-GDQKDVDAIYA 277
Cdd:cd01146 148 RFSDAGSIRLYGPNSFAGSVLEDLGLQNPWAQ-------ETTNDSGFATISLERLA-KADADVLFVFTyEDEELAQALQA 219
|
250 260 270
....*....|....*....|....*....|....*..
gi 550714491 278 NPLLAHLLSVKNKRVWALGTET-FRLDYYSAMLVLQR 313
Cdd:cd01146 220 NPLWQNLPAVKNGRVYVVDDVWwFFGGGLSAARLLLD 256
|
|
| Peripla_BP_2 |
pfam01497 |
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ... |
50-296 |
3.30e-18 |
|
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: 82.03 E-value: 3.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714491 50 VSTSVTLTGSLLAIDAPVIASGATTPNNRVadaqgflrqWGDIAKQRKVARLYIGEPSAEAVAAQMPDLILISATGGDSA 129
Cdd:pfam01497 1 AALSPAYTEILYALGATDSIVGVDAYTRDP---------LKADAVAAIVKVGAYGEINVERLAALKPDLVILSTGYLTDE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714491 130 LalYDQLSAIAPTLIINYDDK--SWQELLTQLGTITGQETQAAERIAAFDKQLAKVKQQMKLPPQPVNAIVYTAAAHTAN 207
Cdd:pfam01497 72 A--EELLSLIIPTVIFESSSTgeSLKEQIKQLGELLGLEDEAEELVAEIDSALAAAKKAVPSLTRKPVLVFGGADGGGYV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714491 208 LWTTDSAQGKLLHQLGFtlADVPAGLHTSKSQgkrhdiiQLGGENLATgLNGEGLFVFAGD---QKDVDAIYANPLLAHL 284
Cdd:pfam01497 150 VAGSNTYIGDLLRILGI--ENIAAELSGSEYA-------PISFEAILS-SNPDVIIVSGRDsftKTGPEFVAANPLWAGL 219
|
250
....*....|..
gi 550714491 285 LSVKNKRVWALG 296
Cdd:pfam01497 220 PAVKNGRVYTLP 231
|
|
| |
|
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: 535.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714491 5 AVCRNALLLTGLFVLGLTSAAAD--DWPRQVTDSRGVHTLESKPTRIVSTSVTLTGSLLAIDAPVIASGATTPNNRVADA 82
Cdd:PRK10957 1 PLYRLALLLLGLLLSGIAAAQASaaGWPRTVTDSRGSVTLESKPQRIVSTSVTLTGTLLAIDAPVIASGATTPNTRVADD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714491 83 QGFLRQWGDIAKQRKVARLYIGEPSAEAVAAQMPDLILISATGGDSALALYDQLSAIAPTLIINYDDKSWQELLTQLGTI 162
Cdd:PRK10957 81 QGFFRQWSDVAKERGVEVLYIGEPDAEAVAAQMPDLIVISATGGDSALALYDQLSAIAPTLVIDYDDKSWQELATQLGEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714491 163 TGQETQAAERIAAFDKQLAKVKQQMKLPPQPVNAIVYTAAAHTANLWTTDSAQGKLLHQLGFTLADVPAGLHTSKSQGKR 242
Cdd:PRK10957 161 TGLEKQAAAVIAQFDAQLAEVKAKITLPPQPVSALVYNGAGHSANLWTPESAQGQLLEQLGFTLAELPAGLQASTSQGKR 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 550714491 243 HDIIQLGGENLATGLNGEGLFVFAGDQKDVDAIYANPLLAHLLSVKNKRVWALGTETFRLDYYSAMLVLQRLNSIFK 319
Cdd:PRK10957 241 HDIIQLGGENLAAGLNGETLFLFAGDDKDADAFLADPLLANLPAVQNKQVYALGTDTFRLDYYSATQLLDRLAALFG 317
|
|
| FepB |
COG4592 |
ABC-type Fe2+-enterobactin transport system, periplasmic component [Inorganic ion transport ... |
4-319 |
2.23e-178 |
|
ABC-type Fe2+-enterobactin transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443649 [Multi-domain] Cd Length: 330 Bit Score: 496.01 E-value: 2.23e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714491 4 AAVCRNALLLTG-----LFVLGLTSAAADDWPRQVTDSRGVHTLESKPTRIVSTSVTLTGSLLAIDAPVIASGATTPNNr 78
Cdd:COG4592 10 AALLAAALLLAGcssadSTASGTSTAAAGGWPRTVTTEKGTVTLPAKPQRIVSTSVTLTGSLLAIDAPVVASGATTPNN- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714491 79 VADAQGFLRQWGDIAKQRKVARLYIG-EPSAEAVAAQMPDLILISATGGDSALALYDQLSAIAPTLIINYDDKSWQELLT 157
Cdd:COG4592 89 VTDDQGFFRQWADVAKERGVKRLYIGlEPNAEAIAAAAPDLIIGSATGGDSALDLYDQLSAIAPTLVVNYDDKSWQELAT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714491 158 QLGTITGQETQAAERIAAFDKQLAKVKQQMKLPPQPVNAIVYTAAAhTANLWTTDSAQGKLLHQLGFTLADVPAGLHTSK 237
Cdd:COG4592 169 QLGEATGHEAQADAVIAAFDARVAEVKAAITLPPQPVSALVYNEDG-GANLWTPESAQGQLLQALGFTLAPLPAELATST 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714491 238 SQGKRHDIIQLGGENLATGLNGEGLFVFAGDQKDVDAIYANPLLAHLLSVKNKRVWALGTETFRLDYYSAMLVLQRLNSI 317
Cdd:COG4592 248 SQGKRGDIVQLSGENLAAALTGPTLFLFAADDKDVDALKADPLLAHLPAVQAGRVYALGPDSFRLDYYSASNLLDRLEKL 327
|
..
gi 550714491 318 FK 319
Cdd:COG4592 328 FG 329
|
|
| FhuD |
cd01146 |
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial ... |
44-313 |
5.70e-56 |
|
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: 182.10 E-value: 5.70e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714491 44 SKPTRIVSTSVTLTGSLLAIDAPVIAsgattpnnrVADAQGFlRQWGDIAKQRK---VARLYIGEPSAEAVAAQMPDLIL 120
Cdd:cd01146 1 AKPQRIVALDWGALETLLALGVKPVG---------VADTAGY-KPWIPEPALPLegvVDVGTRGQPNLEAIAALKPDLIL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714491 121 ISATGGDsalALYDQLSAIAPTLIINY--DDKSWQELLTQLGTITGQETQAAERIAAFDKQLAKVKQQMKLPPQPVNAIV 198
Cdd:cd01146 71 GSASRHD---EIYDQLSQIAPTVLLDSspWLAEWKENLRLIAKALGKEEEAEKLLAEYDQRLAELRQKLPDKGPKPVSVV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714491 199 YTAAAHTANLWTTDSAQGKLLHQLGFTLADVPaglhtskSQGKRHDIIQLGGENLAtGLNGEGLFVFA-GDQKDVDAIYA 277
Cdd:cd01146 148 RFSDAGSIRLYGPNSFAGSVLEDLGLQNPWAQ-------ETTNDSGFATISLERLA-KADADVLFVFTyEDEELAQALQA 219
|
250 260 270
....*....|....*....|....*....|....*..
gi 550714491 278 NPLLAHLLSVKNKRVWALGTET-FRLDYYSAMLVLQR 313
Cdd:cd01146 220 NPLWQNLPAVKNGRVYVVDDVWwFFGGGLSAARLLLD 256
|
|
| FecB |
COG4594 |
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and ... |
10-319 |
2.83e-35 |
|
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443650 [Multi-domain] Cd Length: 316 Bit Score: 130.04 E-value: 2.83e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714491 10 ALLLTGLFVLGLTSAAADDW-------PRQVTDSRGVHTLESKPTRIVSTSVTLTGSLLAID-APViasGattpnnrVAD 81
Cdd:COG4594 9 ILLLALLLLAACGSSSSDSSsseaaagARTVKHAMGETTIPGTPKRVVVLEWSFADALLALGvTPV---G-------IAD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714491 82 AQGFLRqWGDIAKQRKVARLYIG---EPSAEAVAAQMPDLILISATGGDsalALYDQLSAIAPTLIINYDDKSWQELLTQ 158
Cdd:COG4594 79 DNDYDR-WVPYLRDLIKGVTSVGtrsQPNLEAIAALKPDLIIADKSRHE---AIYDQLSKIAPTVLFKSRNGDYQENLES 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714491 159 LGTI---TGQETQAAERIAAFDKQLAKVKQQMKLPPQPVNAIVYTAAAHTANLWTTDSAQGKLLHQLGFTLADvpaglht 235
Cdd:COG4594 155 FKTIakaLGKEEEAEAVLADHDQRIAEAKAKLAAADKGKKVAVGQFRADGLRLYTPNSFAGSVLAALGFENPP------- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714491 236 SKSQGKRHDIIQLGGENLATgLNGEGLFVFA-GDQKDVDAIYANPLLAHLLSVKNKRV-------WALGTETFrldyySA 307
Cdd:COG4594 228 KQSKDNGYGYSEVSLEQLPA-LDPDVLFIATyDDPSILKEWKNNPLWKNLKAVKNGRVyevdgdlWTRGRGPL-----AA 301
|
330
....*....|..
gi 550714491 308 MLVLQRLNSIFK 319
Cdd:COG4594 302 ELMADDLVEILL 313
|
|
| FepB |
COG0614 |
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ... |
48-312 |
6.27e-27 |
|
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 440379 [Multi-domain] Cd Length: 264 Bit Score: 106.24 E-value: 6.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714491 48 RIVSTSVTLTGSLLAIDAP--VIAsgattpnnrVADAQGFLRQWGDIAKQRKVARlyIGEPSAEAVAAQMPDLILISATG 125
Cdd:COG0614 2 RIVSLSPSATELLLALGAGdrLVG---------VSDWGYCDYPELELKDLPVVGG--TGEPNLEAILALKPDLVLASSSG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714491 126 GDSALalYDQLSAI-APTLIINYDD-KSWQELLTQLGTITGQETQAAERIAAFDKQLAKVKQQMKLPPQPVNAIVYTAAA 203
Cdd:COG0614 71 NDEED--YEQLEKIgIPVVVLDPRSlEDLYESIRLLGELLGREERAEALIAEYEARLAAVRARLAGAEERPTVLYEIWSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714491 204 HTANLWTTDSAQGKLLHQLGFT--LADVPAGlhtsksqgkrhdIIQLGGENLATgLNGEGLFVFAGD------QKDVDAI 275
Cdd:COG0614 149 DPLYTAGGGSFIGELLELAGGRnvAADLGGG------------YPEVSLEQVLA-LDPDVIILSGGGydaetaEEALEAL 215
|
250 260 270
....*....|....*....|....*....|....*..
gi 550714491 276 YANPLLAHLLSVKNKRVWALGTETFRldYYSAMLVLQ 312
Cdd:COG0614 216 LADPGWQSLPAVKNGRVYVVPGDLLS--RPGPRLLLA 250
|
|
| FeuA |
cd01138 |
Periplasmic binding protein FeuA. These proteins have predicted to function as initial ... |
44-292 |
8.52e-19 |
|
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: 83.92 E-value: 8.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714491 44 SKPTRIVSTSVTLTGSLLAIDAPViasGATTPNNRVADAQGflrqwgdiaKQRKVARLYIGEPSAEAVAAQMPDLILISa 123
Cdd:cd01138 7 AKPKRIVALSGETEGLALLGIKPV---GAASIGGKNPYYKK---------KTLAKVVGIVDEPNLEKVLELKPDLIIVS- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714491 124 tggDSALALYDQLSAIAPTLIINYDDKSWQELLTQLGTITGQETQAAERIAAFDKQLAKVKQQMKlppqpvNAIVYTAAa 203
Cdd:cd01138 74 ---SKQEENYEKLSKIAPTVPVSYNSSDWEEQLKEIGKLLNKEDEAEKWLADYKQKAKEAKEKIK------KKLGNDKS- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714491 204 hTANLWTTDSAQ---------GKLLHQ-LGFtlaDVPAGLHTsKSQGKRHDIIQLggENLATgLNGEGLFVFAGDQKDVD 273
Cdd:cd01138 144 -VAVLRGRKQIYvfgedgrggGPILYAdLGL---KAPEKVKE-IEDKPGYAAISL--EVLPE-FDADYIFLLFFTGPEAK 215
|
250 260
....*....|....*....|
gi 550714491 274 AIY-ANPLLAHLLSVKNKRV 292
Cdd:cd01138 216 ADFeSLPIWKNLPAVKNNHV 235
|
|
| fecB |
PRK11411 |
iron-dicitrate transporter substrate-binding subunit; Provisional |
10-232 |
2.02e-18 |
|
iron-dicitrate transporter substrate-binding subunit; Provisional
Pssm-ID: 183123 [Multi-domain] Cd Length: 303 Bit Score: 83.95 E-value: 2.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714491 10 ALLLTGLFVLGLTSAAAddwpRQVTDSRGVHTLESKPTRIVSTSVTLTGSLLAID-APVIASGATTPNNRVADAQGFLRQ 88
Cdd:PRK11411 7 LLFAGLLLLSGSSHAFA----VTVQDEQGTFTLEKTPQRIVVLELSFVDALAAVGvSPVGVADDNDAKRILPEVRAHLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714491 89 WGDIAKQrkvarlyiGEPSAEAVAAQMPDLILisatgGDSA--LALYDQLSAIAPTLIINYDDKSWQELL---TQLGTIT 163
Cdd:PRK11411 83 WQSVGTR--------SQPSLEAIAALKPDLII-----ADSSrhAGVYIALQKIAPTLLLKSRNETYQENLqsaAIIGEVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 550714491 164 GQETQAAERIAAFDKQLAKVKQQMklpPQPVNAIVYTAAAHTANLWTTDSAQGKLLHQLGFTLADVPAG 232
Cdd:PRK11411 150 GKKREMQARIEQHKERMAQFASQL---PKGTRVAFGTSREQQFNLHSPESYTGSVLAALGLNVPKAPMN 215
|
|
| Peripla_BP_2 |
pfam01497 |
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ... |
50-296 |
3.30e-18 |
|
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: 82.03 E-value: 3.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714491 50 VSTSVTLTGSLLAIDAPVIASGATTPNNRVadaqgflrqWGDIAKQRKVARLYIGEPSAEAVAAQMPDLILISATGGDSA 129
Cdd:pfam01497 1 AALSPAYTEILYALGATDSIVGVDAYTRDP---------LKADAVAAIVKVGAYGEINVERLAALKPDLVILSTGYLTDE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714491 130 LalYDQLSAIAPTLIINYDDK--SWQELLTQLGTITGQETQAAERIAAFDKQLAKVKQQMKLPPQPVNAIVYTAAAHTAN 207
Cdd:pfam01497 72 A--EELLSLIIPTVIFESSSTgeSLKEQIKQLGELLGLEDEAEELVAEIDSALAAAKKAVPSLTRKPVLVFGGADGGGYV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714491 208 LWTTDSAQGKLLHQLGFtlADVPAGLHTSKSQgkrhdiiQLGGENLATgLNGEGLFVFAGD---QKDVDAIYANPLLAHL 284
Cdd:pfam01497 150 VAGSNTYIGDLLRILGI--ENIAAELSGSEYA-------PISFEAILS-SNPDVIIVSGRDsftKTGPEFVAANPLWAGL 219
|
250
....*....|..
gi 550714491 285 LSVKNKRVWALG 296
Cdd:pfam01497 220 PAVKNGRVYTLP 231
|
|
| TroA-like |
cd00636 |
Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function ... |
47-200 |
4.02e-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: 76.83 E-value: 4.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714491 47 TRIVSTSVTLTGSLLAIDAPVIASGATTPNNRVADAQGFLRQWGDIakqrkvarLYIGEPSAEAVAAQMPDLILISATGG 126
Cdd:cd00636 1 KRVVALDPGATELLLALGGDDKPVGVADPSGYPPEAKALLEKVPDV--------GHGYEPNLEKIAALKPDLIIANGSGL 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 550714491 127 DsalALYDQLSAIA-PTLIIN----YDDKSWQELLTQLGTITGQETQAAERIAAFDKQLAKVKQQMKLPPQPVNAIVYT 200
Cdd:cd00636 73 E---AWLDKLSKIAiPVVVVDeaseLSLENIKESIRLIGKALGKEENAEELIAELDARLAELRAKLAKIPKKKVSLVVG 148
|
|
| TroA_e |
cd01142 |
Periplasmic binding protein TroA_e. These proteins are predicted to function as initial ... |
24-314 |
4.12e-15 |
|
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: 74.31 E-value: 4.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714491 24 AAADDWPRQVTDSRGVH-TLESKPTRIVSTSVTLTGSLLAIDAPviasgattpnnRVADAQGFLRQWGDIAKQR-----K 97
Cdd:cd01142 1 PAATAATRTITDMAGRKvTIPDEVKRIAALWGAGNAVVAALGGG-----------KLIVATTSTVQQEPWLYRLapsleN 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714491 98 VARLYIG-EPSAEAVAAQMPDLILISATGGDSALAlydQLSAIAPTLIINYDDKS-WQELLTQLGTITGQETQAAERIAA 175
Cdd:cd01142 70 VATGGTGnDVNIEELLALKPDVVIVWSTDGKEAGK---AVLRLLNALSLRDAELEeVKLTIALLGELLGRQEKAEALVAY 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714491 176 FDKQLAKVKQQmklppqpvnaivytaaahTANLwtTDSAQGKLLHQLgftladvPAGLHTSKSQGKRHDIIQL-GGENLA 254
Cdd:cd01142 147 FDDNLAYVAAR------------------TKKL--PDSERPRVYYAG-------PDPLTTDGTGSITNSWIDLaGGINVA 199
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 550714491 255 TGLNGEGL--------------FVFAGDQKDVDAIYANPLLAHLLSVKNKRVWALGTETFRLDYYSAMLVLQRL 314
Cdd:cd01142 200 SEATKKGSgevsleqllkwnpdVIIVGNADTKAAILADPRWQNLRAVKNGRVYVNPEGAFWWDRPSAEEALLGL 273
|
|
| FatB |
cd01140 |
Siderophore binding protein FatB. These proteins have been shown to function as ABC-type ... |
35-188 |
4.67e-15 |
|
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: 73.83 E-value: 4.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714491 35 DSRGVHTLESKPTRIVSTSVTLTGSLLAIDAPVIA--SGATTPNnRVADAQGflrqwgdiAKQRKVARLYigEPSAEAVA 112
Cdd:cd01140 1 HALGETKVPKNPEKVVVFDVGALDTLDALGVKVVGvpKSSTLPE-YLKKYKD--------DKYANVGTLF--EPDLEAIA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714491 113 AQMPDLILISATGGDSalalYDQLSAIAPTLIINYD-DKSWQELLTQ---LGTITGQETQAAERIAAFDKQLAKVKQQMK 188
Cdd:cd01140 70 ALKPDLIIIGGRLAEK----YDELKKIAPTIDLGADlKNYLESVKQNietLGKIFGKEEEAKELVAEIDASIAEAKSAAK 145
|
|
| HemV-2 |
cd01147 |
Metal binding protein HemV-2. These proteins are predicted to function as initial receptors ... |
47-300 |
2.45e-14 |
|
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: 71.60 E-value: 2.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714491 47 TRIVSTSVTLTGSLLAIDAP--VIASGATTpnnRVADAQGFLRQWGDIAKQRKVARLYIG-EPSAEAVAAQMPDLILIsa 123
Cdd:cd01147 6 ERVVAAGPGALRLLYALAAPdkIVGVDDAE---KSDEGRPYFLASPELKDLPVIGRGGRGnTPNYEKIAALKPDVVID-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714491 124 TGGDSALALYDQLSAIA--PTLIINY--DDKSWQELLTQLGTITGQETQAAERIAAFDKQLAKVKQQMKLPPQPVNAIVY 199
Cdd:cd01147 81 VGSDDPTSIADDLQKKTgiPVVVLDGgdSLEDTPEQIRLLGKVLGKEERAEELISFIESILADVEERTKDIPDEEKPTVY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714491 200 TAAAHTANlwttdsaqgkllhqlgftladvPAGLHTSKSqGKRHDIIQLGGENLATGLNGEGLF--------------VF 265
Cdd:cd01147 161 FGRIGTKG----------------------AAGLESGLA-GSIEVFELAGGINVADGLGGGGLKevspeqillwnpdvIF 217
|
250 260 270
....*....|....*....|....*....|....*....
gi 550714491 266 AGDQK--DVDAIYA--NPLLAHLLSVKNKRVWALGTETF 300
Cdd:cd01147 218 LDTGSfyLSLEGYAknRPFWQSLKAVKNGRVYLLPALPF 256
|
|
| YvrC |
cd01143 |
Periplasmic binding protein YvrC. These proteins are predicted to function as initial ... |
44-205 |
1.48e-10 |
|
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: 59.60 E-value: 1.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714491 44 SKPTRIVSTSVTLTGSLLAIDA--PVIasGATTPNNRVADAQgflrqwgdiaKQRKVARLYigEPSAEAVAAQMPDLILI 121
Cdd:cd01143 1 KEPERIVSLSPSITEILFALGAgdKIV--GVDTYSNYPKEVR----------KKPKVGSYS--NPNVEKIVALKPDLVIV 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714491 122 SATGGDSalaLYDQLSAIAPTLIINYDDKSWQELL---TQLGTITGQETQAAERIAAFDKQLAKVKQQMKLPPQPVNAIV 198
Cdd:cd01143 67 SSSSLAE---LLEKLKDAGIPVVVLPAASSLDEIYdqiELIGKITGAEEEAEKLVKEMKQKIDKVKDKGKTIKKSKVYIE 143
|
170
....*....|...
gi 550714491 199 ------YTAAAHT 205
Cdd:cd01143 144 vslggpYTAGKNT 156
|
|
| ChuT |
COG4558 |
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism] ... |
102-295 |
1.02e-07 |
|
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443619 [Multi-domain] Cd Length: 285 Bit Score: 52.50 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714491 102 YIGEPSAEAVAAQMPDLILISATGGdSALALyDQLSAIA-PTLIINyDDKSWQELL---TQLGTITGQETQAAERIAAFD 177
Cdd:COG4558 71 YMRQLSAEGILSLKPTLVLASEGAG-PPEVL-DQLRAAGvPVVVVP-AAPSLEGVLakiRAVAAALGVPEAGEALAARLE 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714491 178 KQLAKVKQQMKLPPQPVNAIVYtaaahtanlwttdsaqgkLLHQLGFTLAdvpAGLHTSKsqgkrHDIIQL-GGENLATG 256
Cdd:COG4558 148 ADLAALAARVAAIGKPPRVLFL------------------LSRGGGRPMV---AGRGTAA-----DALIRLaGGVNAAAG 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 550714491 257 LNG------EGL--------FVFAGDQK---DVDAIYANPLLAHLLSVKNKRVWAL 295
Cdd:COG4558 202 FEGykplsaEALiaaapdviLVMTRGLEslgGVDGLLALPGLAQTPAGKNKRIVAM 257
|
|
| TroA_d |
cd01141 |
Periplasmic binding protein TroA_d. These proteins are predicted to function as initial ... |
41-219 |
9.56e-05 |
|
Periplasmic binding protein TroA_d. 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: 238561 [Multi-domain] Cd Length: 186 Bit Score: 42.41 E-value: 9.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714491 41 TLESKPTRIVSTSVTLTGSLLAIDAPVIASGATTPNNRVADAqgflrqwgDIAKQRKVARLYIGEPSAEAVAAQMPDLIL 120
Cdd:cd01141 3 TIKVPPKRIVVLSPTHVDLLLALDKADKIVGVSASAYDLNTP--------AVKERIDIQVGPTGSLNVELIVALKPDLVI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714491 121 ISATGgdSALALYDQLSAIA-PTLIINYDDKSWQEL----LTQLGTITGQETQAAERIAAFDKQLAKVKQQMKLPPQPVN 195
Cdd:cd01141 75 LYGGF--QAQTILDKLEQLGiPVLYVNEYPSPLGRAewikFAAAFYGVGKEDKADEAFAQIAGRYRDLAKKVSNLNKPTV 152
|
170 180
....*....|....*....|....*..
gi 550714491 196 AIvytaAAHTANLW---TTDSAQGKLL 219
Cdd:cd01141 153 AI----GKPVKGLWympGGNSYVAKML 175
|
|
| PRK10576 |
PRK10576 |
Fe(3+)-hydroxamate ABC transporter substrate-binding protein FhuD; |
105-187 |
2.61e-04 |
|
Fe(3+)-hydroxamate ABC transporter substrate-binding protein FhuD;
Pssm-ID: 236719 Cd Length: 292 Bit Score: 41.92 E-value: 2.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714491 105 EPSAEAVAAQMPDLILISATGGDSAlalyDQLSAIAPTLIINYDD-----KSWQELLTQLGTITGQETQAAERIAAFDKQ 179
Cdd:PRK10576 83 EPNLELLTQMKPSLILWSAGYGPSP----EKLARIAPGRGFAFSDgkkplAVARKSLVELAQRLNLEAAAETHLAQFDDF 158
|
....*...
gi 550714491 180 LAKVKQQM 187
Cdd:PRK10576 159 IASAKPRL 166
|
|
| HutB |
cd01149 |
Hemin binding protein HutB. These proteins have been shown to function as initial receptors ... |
107-295 |
5.04e-04 |
|
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: 40.71 E-value: 5.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714491 107 SAEAVAAQMPDLILISATGGdSALALyDQLSAIAPTLIINYDDKSWQELLT---QLGTITGQETQAAERIAAFDKQLAKV 183
Cdd:cd01149 50 SAEGVLSLKPTLVIASDEAG-PPEAL-DQLRAAGVPVVTVPSTPTLDGLLTkirQVAQALGVPEKGEALAQEVRQRLAAL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714491 184 KQQMKLPPQPVNAI-VYTAAAHTANLWTTDSAQGKLLhqlgfTLAdvpaglhtsksqgkrhdiiqlGGENLATGLNG--- 259
Cdd:cd01149 128 RKTVAAHKKPPRVLfLLSHGGGAAMAAGRNTAADAII-----ALA---------------------GAVNAAAGFRGykp 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 550714491 260 ---EGLFVFAGD-----------QKDVDAIYANPLLAHLLSVKNKRVWAL 295
Cdd:cd01149 182 lsaEALIAAQPDvilvmsrgldaVGGVDGLLKLPGLAQTPAGRNKRILAM 231
|
|
| |
