|
Name |
Accession |
Description |
Interval |
E-value |
| TroA_f |
cd01139 |
Periplasmic binding protein TroA_f. These proteins are predicted to function as initial ... |
38-379 |
2.68e-152 |
|
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: 433.27 E-value: 2.68e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550139372 38 TVTDIAGREVTVNAPVKRILLGEGRQLYLIASLEPKDPLARIVAWRNDLIEADPATYAQYLEAFPKLAKLPAFPGQENGL 117
Cdd:cd01139 2 TVTDVAGRKVTLDAPVERVLLGEGRQLYALALLEGENPFARIVGWGGDLKKGDPDTYAKYKEKFPEIADIPLIGSTYNGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550139372 118 LDIESTIVQKPDVVLLNLEAMRANEDVNYIEKLAELKIPVLYIDFRHYPLKNTEPTIRLLGKIMGREARAEEIIAFRHQA 197
Cdd:cd01139 82 FSVEKVLTLKPDLVILNIWAKTTAEESGILEKLEQAGIPVVFVDFRQKPLKNTTPSMRLLGKALGREERAEEFIEFYQER 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550139372 198 MTRVADVIAQTKPERPRVFIERMGGYADDCCLSFGAENFGKYVELAGGHNIGSDVLPSTFGQLNPEQVIAANPEHVVVTS 277
Cdd:cd01139 162 IDRIRDRLAKINEPKPKVFIELGAGGPEECCSTYGNGNWGELVDAAGGDNIADGLIPGTSGELNAEYVIAANPEIIIATG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550139372 278 ADWEAYVPGGHWIPLGPGADPKVTREKLewFTSRSAYTNISAQKTQNFHGIWHQFYNSPYEFFAVQQLAKWFHPELFADL 357
Cdd:cd01139 242 GNWAKDPSGVSLGPDGTTADAKESLLRA--LLKRPGWSSLQAVKNGRVYALWHQFYRSPYNFVALEAFAKWLYPELFKDL 319
|
330 340
....*....|....*....|..
gi 1550139372 358 DPDATFAEYHRRFLPIPYKPGY 379
Cdd:cd01139 320 DPEATLQEFHRQFLPVDYSGTF 341
|
|
| PRK14048 |
PRK14048 |
ferrichrome/ferrioxamine B periplasmic transporter; Provisional |
34-383 |
1.04e-71 |
|
ferrichrome/ferrioxamine B periplasmic transporter; Provisional
Pssm-ID: 172540 [Multi-domain] Cd Length: 374 Bit Score: 229.01 E-value: 1.04e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550139372 34 QTPTTVTDIAGREVTVNAPVKRILLGEGRQLYLIASLEPkDPLARIVAWRNDLIEADPATYAQYLEAFPKLAKLPAFPGQ 113
Cdd:PRK14048 29 QWPMTVTDAVGREVTIPAPPKAVLLGSGFNLIALSLIHP-DPVSLLAGWSGDMKGDNPEIYESFLRKFPELADVPLIDDG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550139372 114 ENGLLDIESTIVQKPDVVLLNLEAMRANEDVNYIEKLAELKIPVLYIDFRHYPLKNTEPTIRLLGKIMGREARAEEIIAF 193
Cdd:PRK14048 108 SGPGLSFETILTLKADLAILANWQADTEAGQRAIEYLESIGVPVIVVDFNNEALKNTPDNMRLLGKVFEREEQAEDFARF 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550139372 194 RHQAMTRVADVIAQTKPERPRVFIERMGGyADDCCLSFGAENFGKYVELAGGHNIGSDVLPSTFGQLNPEQVIAANPEHV 273
Cdd:PRK14048 188 YEERLARIRDRVAKHSEPGPTVLMEAFPA-ADRCCWAYGRGGLGEFIALTGSRNIAEGALPRPGGMMNAEAIMAENPDVY 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550139372 274 VVTSAdweayvPGGHW--IPLGPGADPKVTREKLEWFTSRSAYTNISAQKTQNFHGIWHQFYNSPYEFFAVQQLAKWFHP 351
Cdd:PRK14048 267 IATSS------PGGKYsgFSIGPGVSAEEAETTLANVVDKPVMASIAAVRDGRVHGLWNFFNAVPLNIVAAEAFASWLRP 340
|
330 340 350
....*....|....*....|....*....|..
gi 1550139372 352 ELFADLDPDATFAEYHRRFLPIPYKPGYAMSL 383
Cdd:PRK14048 341 ELFADIDPAATLAEINRRFAAVPFEGSYWISL 372
|
|
| FepB |
COG0614 |
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ... |
55-355 |
6.64e-47 |
|
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 440379 [Multi-domain] Cd Length: 264 Bit Score: 160.93 E-value: 6.64e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550139372 55 RILLGEGRQLYLIASLEPKDplaRIVAWRNDLIEADPATyaqyleafpKLAKLPAFPGQENglLDIESTIVQKPDVVLLN 134
Cdd:COG0614 2 RIVSLSPSATELLLALGAGD---RLVGVSDWGYCDYPEL---------ELKDLPVVGGTGE--PNLEAILALKPDLVLAS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550139372 135 LEAMRANEdvnyIEKLAELKIPVLYIDFRhyPLKNTEPTIRLLGKIMGREARAEEIIAFRHQAMTRVADVIAQTKpERPR 214
Cdd:COG0614 68 SSGNDEED----YEQLEKIGIPVVVLDPR--SLEDLYESIRLLGELLGREERAEALIAEYEARLAAVRARLAGAE-ERPT 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550139372 215 VFIERmgGYADDCCLSFGAENFGKYVELAGGHNIGSDvLPSTFGQLNPEQVIAANPEHVVVTsadweayvpgghwiplGP 294
Cdd:COG0614 141 VLYEI--WSGDPLYTAGGGSFIGELLELAGGRNVAAD-LGGGYPEVSLEQVLALDPDVIILS----------------GG 201
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1550139372 295 GADPKVTREKLEWFTSRSAYTNISAQKTQNFHGIWHQF--YNSPYEFFAVQQLAKWFHPELFA 355
Cdd:COG0614 202 GYDAETAEEALEALLADPGWQSLPAVKNGRVYVVPGDLlsRPGPRLLLALEDLAKALHPELFA 264
|
|
| Peripla_BP_2 |
pfam01497 |
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ... |
116-281 |
7.35e-09 |
|
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: 55.84 E-value: 7.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550139372 116 GLLDIESTIVQKPDVVLLNLEAMRANedvnyIEKLAELKIPVLYIDFRHYPLKNTEpTIRLLGKIMGREARAEEIIAFRH 195
Cdd:pfam01497 46 GEINVERLAALKPDLVILSTGYLTDE-----AEELLSLIIPTVIFESSSTGESLKE-QIKQLGELLGLEDEAEELVAEID 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550139372 196 QAMTRVADVIAQTKPERPRVFierMGGYADDCCLSFGAENFGKYVELAGGHNIGSDVLPSTFGQLNPEQVIAANPEHVVV 275
Cdd:pfam01497 120 SALAAAKKAVPSLTRKPVLVF---GGADGGGYVVAGSNTYIGDLLRILGIENIAAELSGSEYAPISFEAILSSNPDVIIV 196
|
....*.
gi 1550139372 276 TSADWE 281
Cdd:pfam01497 197 SGRDSF 202
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| TroA_f |
cd01139 |
Periplasmic binding protein TroA_f. These proteins are predicted to function as initial ... |
38-379 |
2.68e-152 |
|
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: 433.27 E-value: 2.68e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550139372 38 TVTDIAGREVTVNAPVKRILLGEGRQLYLIASLEPKDPLARIVAWRNDLIEADPATYAQYLEAFPKLAKLPAFPGQENGL 117
Cdd:cd01139 2 TVTDVAGRKVTLDAPVERVLLGEGRQLYALALLEGENPFARIVGWGGDLKKGDPDTYAKYKEKFPEIADIPLIGSTYNGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550139372 118 LDIESTIVQKPDVVLLNLEAMRANEDVNYIEKLAELKIPVLYIDFRHYPLKNTEPTIRLLGKIMGREARAEEIIAFRHQA 197
Cdd:cd01139 82 FSVEKVLTLKPDLVILNIWAKTTAEESGILEKLEQAGIPVVFVDFRQKPLKNTTPSMRLLGKALGREERAEEFIEFYQER 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550139372 198 MTRVADVIAQTKPERPRVFIERMGGYADDCCLSFGAENFGKYVELAGGHNIGSDVLPSTFGQLNPEQVIAANPEHVVVTS 277
Cdd:cd01139 162 IDRIRDRLAKINEPKPKVFIELGAGGPEECCSTYGNGNWGELVDAAGGDNIADGLIPGTSGELNAEYVIAANPEIIIATG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550139372 278 ADWEAYVPGGHWIPLGPGADPKVTREKLewFTSRSAYTNISAQKTQNFHGIWHQFYNSPYEFFAVQQLAKWFHPELFADL 357
Cdd:cd01139 242 GNWAKDPSGVSLGPDGTTADAKESLLRA--LLKRPGWSSLQAVKNGRVYALWHQFYRSPYNFVALEAFAKWLYPELFKDL 319
|
330 340
....*....|....*....|..
gi 1550139372 358 DPDATFAEYHRRFLPIPYKPGY 379
Cdd:cd01139 320 DPEATLQEFHRQFLPVDYSGTF 341
|
|
| PRK14048 |
PRK14048 |
ferrichrome/ferrioxamine B periplasmic transporter; Provisional |
34-383 |
1.04e-71 |
|
ferrichrome/ferrioxamine B periplasmic transporter; Provisional
Pssm-ID: 172540 [Multi-domain] Cd Length: 374 Bit Score: 229.01 E-value: 1.04e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550139372 34 QTPTTVTDIAGREVTVNAPVKRILLGEGRQLYLIASLEPkDPLARIVAWRNDLIEADPATYAQYLEAFPKLAKLPAFPGQ 113
Cdd:PRK14048 29 QWPMTVTDAVGREVTIPAPPKAVLLGSGFNLIALSLIHP-DPVSLLAGWSGDMKGDNPEIYESFLRKFPELADVPLIDDG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550139372 114 ENGLLDIESTIVQKPDVVLLNLEAMRANEDVNYIEKLAELKIPVLYIDFRHYPLKNTEPTIRLLGKIMGREARAEEIIAF 193
Cdd:PRK14048 108 SGPGLSFETILTLKADLAILANWQADTEAGQRAIEYLESIGVPVIVVDFNNEALKNTPDNMRLLGKVFEREEQAEDFARF 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550139372 194 RHQAMTRVADVIAQTKPERPRVFIERMGGyADDCCLSFGAENFGKYVELAGGHNIGSDVLPSTFGQLNPEQVIAANPEHV 273
Cdd:PRK14048 188 YEERLARIRDRVAKHSEPGPTVLMEAFPA-ADRCCWAYGRGGLGEFIALTGSRNIAEGALPRPGGMMNAEAIMAENPDVY 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550139372 274 VVTSAdweayvPGGHW--IPLGPGADPKVTREKLEWFTSRSAYTNISAQKTQNFHGIWHQFYNSPYEFFAVQQLAKWFHP 351
Cdd:PRK14048 267 IATSS------PGGKYsgFSIGPGVSAEEAETTLANVVDKPVMASIAAVRDGRVHGLWNFFNAVPLNIVAAEAFASWLRP 340
|
330 340 350
....*....|....*....|....*....|..
gi 1550139372 352 ELFADLDPDATFAEYHRRFLPIPYKPGYAMSL 383
Cdd:PRK14048 341 ELFADIDPAATLAEINRRFAAVPFEGSYWISL 372
|
|
| FepB |
COG0614 |
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ... |
55-355 |
6.64e-47 |
|
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 440379 [Multi-domain] Cd Length: 264 Bit Score: 160.93 E-value: 6.64e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550139372 55 RILLGEGRQLYLIASLEPKDplaRIVAWRNDLIEADPATyaqyleafpKLAKLPAFPGQENglLDIESTIVQKPDVVLLN 134
Cdd:COG0614 2 RIVSLSPSATELLLALGAGD---RLVGVSDWGYCDYPEL---------ELKDLPVVGGTGE--PNLEAILALKPDLVLAS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550139372 135 LEAMRANEdvnyIEKLAELKIPVLYIDFRhyPLKNTEPTIRLLGKIMGREARAEEIIAFRHQAMTRVADVIAQTKpERPR 214
Cdd:COG0614 68 SSGNDEED----YEQLEKIGIPVVVLDPR--SLEDLYESIRLLGELLGREERAEALIAEYEARLAAVRARLAGAE-ERPT 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550139372 215 VFIERmgGYADDCCLSFGAENFGKYVELAGGHNIGSDvLPSTFGQLNPEQVIAANPEHVVVTsadweayvpgghwiplGP 294
Cdd:COG0614 141 VLYEI--WSGDPLYTAGGGSFIGELLELAGGRNVAAD-LGGGYPEVSLEQVLALDPDVIILS----------------GG 201
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1550139372 295 GADPKVTREKLEWFTSRSAYTNISAQKTQNFHGIWHQF--YNSPYEFFAVQQLAKWFHPELFA 355
Cdd:COG0614 202 GYDAETAEEALEALLADPGWQSLPAVKNGRVYVVPGDLlsRPGPRLLLALEDLAKALHPELFA 264
|
|
| HemV-2 |
cd01147 |
Metal binding protein HemV-2. These proteins are predicted to function as initial receptors ... |
49-276 |
4.51e-26 |
|
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: 105.49 E-value: 4.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550139372 49 VNAPVKRIL-LGEGRQLYLIASLEPKdplaRIVAW-RNDLIEADpatyAQYLEAFPKLAKLPAF-PGQENGLLDIESTIV 125
Cdd:cd01147 1 VPKPVERVVaAGPGALRLLYALAAPD----KIVGVdDAEKSDEG----RPYFLASPELKDLPVIgRGGRGNTPNYEKIAA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550139372 126 QKPDVVLlnleaMRANEDVNYIEKLAELK--IPVLYIDFRHYpLKNTEPTIRLLGKIMGREARAEEIIAFRHQAMTRVAD 203
Cdd:cd01147 73 LKPDVVI-----DVGSDDPTSIADDLQKKtgIPVVVLDGGDS-LEDTPEQIRLLGKVLGKEERAEELISFIESILADVEE 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1550139372 204 VIAQTKPE-RPRVFIERMGGYADDcCLSFGAENFGKYVELAGGHNIGSDVLPSTFGQLNPEQVIAANPEHVVVT 276
Cdd:cd01147 147 RTKDIPDEeKPTVYFGRIGTKGAA-GLESGLAGSIEVFELAGGINVADGLGGGGLKEVSPEQILLWNPDVIFLD 219
|
|
| TroA_e |
cd01142 |
Periplasmic binding protein TroA_e. These proteins are predicted to function as initial ... |
38-359 |
1.88e-22 |
|
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: 95.88 E-value: 1.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550139372 38 TVTDIAGREVTVNAPVKRILLGEGRQLYLIASLEPKDPL-ARIVAWRNDlieadpatyAQYLEAFPKLAKLPAfPGQENG 116
Cdd:cd01142 9 TITDMAGRKVTIPDEVKRIAALWGAGNAVVAALGGGKLIvATTSTVQQE---------PWLYRLAPSLENVAT-GGTGND 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550139372 117 LLdIESTIVQKPDVVLLNleAMRANEdvnYIEKLAELkIPVLYIDFRhyPLKNTEPTIRLLGKIMGREARAEEIIAFRHQ 196
Cdd:cd01142 79 VN-IEELLALKPDVVIVW--STDGKE---AGKAVLRL-LNALSLRDA--ELEEVKLTIALLGELLGRQEKAEALVAYFDD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550139372 197 AMTRVADVIAQTK-PERPRVFIERMGGYADDCCLSFGAEnfgkYVELAGGHNIGSDVLPSTFGQLNPEQVIAANPEHVVV 275
Cdd:cd01142 150 NLAYVAARTKKLPdSERPRVYYAGPDPLTTDGTGSITNS----WIDLAGGINVASEATKKGSGEVSLEQLLKWNPDVIIV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550139372 276 TSADweayvpgghwiplgpGADPkvtreklewFTSRSAYTNISAQKTQNFHGI------WHqfYNSPYEFFAVQQLAKWF 349
Cdd:cd01142 226 GNAD---------------TKAA---------ILADPRWQNLRAVKNGRVYVNpegafwWD--RPSAEEALLGLWLAKTL 279
|
330
....*....|
gi 1550139372 350 HPELFADLDP 359
Cdd:cd01142 280 YPERFTDDDM 289
|
|
| YvrC |
cd01143 |
Periplasmic binding protein YvrC. These proteins are predicted to function as initial ... |
118-271 |
5.65e-14 |
|
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: 70.00 E-value: 5.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550139372 118 LDIESTIVQKPDVVLLNLEAMRANedvnyIEKLAELKIPVLYIdfrhyPLKNT----EPTIRLLGKIMGREARAEEIIaf 193
Cdd:cd01143 51 PNVEKIVALKPDLVIVSSSSLAEL-----LEKLKDAGIPVVVL-----PAASSldeiYDQIELIGKITGAEEEAEKLV-- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550139372 194 rHQAMTRVADVIAQTK-PERPRVFIErmggYADDCCLSFGAENF-GKYVELAGGHNIGSDVlpSTFGQLNPEQVIAANPE 271
Cdd:cd01143 119 -KEMKQKIDKVKDKGKtIKKSKVYIE----VSLGGPYTAGKNTFiNELIRLAGAKNIAADS--GGWPQVSPEEILKANPD 191
|
|
| TroA-like |
cd00636 |
Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function ... |
54-217 |
9.71e-14 |
|
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: 67.97 E-value: 9.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550139372 54 KRILLGEGRQLYLIASLEPKDplaRIVAWrndlieADPATYAQYleAFPKLAKLPAFPGQENglLDIESTIVQKPDVVLL 133
Cdd:cd00636 1 KRVVALDPGATELLLALGGDD---KPVGV------ADPSGYPPE--AKALLEKVPDVGHGYE--PNLEKIAALKPDLIIA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550139372 134 NLEAMRAnedvnYIEKLAELKIPVLYIDFR-HYPLKNTEPTIRLLGKIMGREARAEEIIAFRHQAMTRVADVIAQTKPER 212
Cdd:cd00636 68 NGSGLEA-----WLDKLSKIAIPVVVVDEAsELSLENIKESIRLIGKALGKEENAEELIAELDARLAELRAKLAKIPKKK 142
|
....*
gi 1550139372 213 PRVFI 217
Cdd:cd00636 143 VSLVV 147
|
|
| TroA_a |
cd01148 |
Metal binding protein TroA_a. These proteins are predicted to function as initial receptors ... |
44-325 |
6.94e-13 |
|
Metal binding protein TroA_a. These proteins are predicted to function as initial receptors in ABC transport of metal ions in eubacteria. 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.
Pssm-ID: 238568 [Multi-domain] Cd Length: 284 Bit Score: 68.52 E-value: 6.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550139372 44 GREVTVNAPVKRILLGEGRQLYLIASLEPKDPLARIVAWRNDLIEadpaTYAQYLEAFPKLA-KLPAFpgqenglldiES 122
Cdd:cd01148 9 GRSVTFDKAPQRVVSNDQNTTEMMLALGLQDRMVGTAGIDNKDLP----ELKAKYDKVPELAkKYPSK----------ET 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550139372 123 TIVQKPDVVLLNLEAMRANEDVNYIEKLAELKIPVlYI-------DFRHYPLKNTEPTIRLLGKIMGREARAEEIIAfrh 195
Cdd:cd01148 75 VLAARPDLVFGGWSYGFDKGGLGTPDSLAELGIKT-YIlpescgqRRGEATLDDVYNDIRNLGKIFDVEDRADKLVA--- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550139372 196 QAMTRVADVIAQTK--PERPRVFIERMGGYADDCCLSFGAENFgkYVELAGGHNIGSDVLPStFGQLNPEQVIAANPEHV 273
Cdd:cd01148 151 DLKARLAEISAKVKgdGKKVAVFVYDSGEDKPFTSGRGGIPNA--IITAAGGRNVFADVDES-WTTVSWETVIARNPDVI 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1550139372 274 VVTSADweayvpgghwiplgpgaDPKVTREKLEWFTSRSAYTNISAQKTQNF 325
Cdd:cd01148 228 VIIDYG-----------------DQNAAEQKIKFLKENPALKNVPAVKNNRF 262
|
|
| ChuT |
COG4558 |
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism] ... |
118-282 |
1.83e-12 |
|
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443619 [Multi-domain] Cd Length: 285 Bit Score: 67.14 E-value: 1.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550139372 118 LDIESTIVQKPDVVLLNLEAMraNEDVnyIEKLAELKIPVLYIDfRHYPLKNTEPTIRLLGKIMGREARAEEIIAFRHQA 197
Cdd:COG4558 75 LSAEGILSLKPTLVLASEGAG--PPEV--LDQLRAAGVPVVVVP-AAPSLEGVLAKIRAVAAALGVPEAGEALAARLEAD 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550139372 198 MTRVADVIAQTkPERPRV-FIERMGG---YAddcclsFGAENFG-KYVELAGGHNIGSDVlpSTFGQLNPEQVIAANPEH 272
Cdd:COG4558 150 LAALAARVAAI-GKPPRVlFLLSRGGgrpMV------AGRGTAAdALIRLAGGVNAAAGF--EGYKPLSAEALIAAAPDV 220
|
170
....*....|
gi 1550139372 273 VVVTSADWEA 282
Cdd:COG4558 221 ILVMTRGLES 230
|
|
| BtuF |
cd01144 |
Cobalamin binding protein BtuF. These proteins have been shown to function as initial ... |
118-283 |
4.75e-12 |
|
Cobalamin binding protein BtuF. These proteins have been shown to function as initial receptors in ABC transport of vitamin B12 (cobalamin) in eubacterial and some archaeal species. 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: 238564 [Multi-domain] Cd Length: 245 Bit Score: 65.40 E-value: 4.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550139372 118 LDIESTIVQKPDVVLLNLEAMRANEdvnyIEKLAELKIPVLYidFRHYPLKNTEPTIRLLGKIMGREARAEEII-AFRhq 196
Cdd:cd01144 48 LDLERVLALKPDLVIAWDDCNVCAV----VDQLRAAGIPVLV--SEPQTLDDILADIRRLGTLAGRPARAEELAeALR-- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550139372 197 amTRVADVIAQTKP-ERPRVFIErmggYADDCCLSFGAENFGKYVELAGGHNIGSDvLPSTFGQLNPEQVIAANPEHVVV 275
Cdd:cd01144 120 --RRLAALRKQYASkPPPRVFYQ----EWIDPLMTAGGDWVPELIALAGGVNVFAD-AGERSPQVSWEDVLAANPDVIVL 192
|
....*...
gi 1550139372 276 TsadWEAY 283
Cdd:cd01144 193 S---PCGF 197
|
|
| HutB |
cd01149 |
Hemin binding protein HutB. These proteins have been shown to function as initial receptors ... |
118-282 |
1.05e-10 |
|
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: 61.13 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550139372 118 LDIESTIVQKPDVVLlNLEAMRANEdvnYIEKLAELKIPVLYIDfRHYPLKNTEPTIRLLGKIMGREARAEEIIAFRHQA 197
Cdd:cd01149 49 LSAEGVLSLKPTLVI-ASDEAGPPE---ALDQLRAAGVPVVTVP-STPTLDGLLTKIRQVAQALGVPEKGEALAQEVRQR 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550139372 198 MTRVADVIAQTKPERPRVFIERMGGYAddcCLSFGAENFGK-YVELAGGHNIGSDVlpSTFGQLNPEQVIAANPEHVVVT 276
Cdd:cd01149 124 LAALRKTVAAHKKPPRVLFLLSHGGGA---AMAAGRNTAADaIIALAGAVNAAAGF--RGYKPLSAEALIAAQPDVILVM 198
|
....*.
gi 1550139372 277 SADWEA 282
Cdd:cd01149 199 SRGLDA 204
|
|
| Peripla_BP_2 |
pfam01497 |
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ... |
116-281 |
7.35e-09 |
|
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: 55.84 E-value: 7.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550139372 116 GLLDIESTIVQKPDVVLLNLEAMRANedvnyIEKLAELKIPVLYIDFRHYPLKNTEpTIRLLGKIMGREARAEEIIAFRH 195
Cdd:pfam01497 46 GEINVERLAALKPDLVILSTGYLTDE-----AEELLSLIIPTVIFESSSTGESLKE-QIKQLGELLGLEDEAEELVAEID 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550139372 196 QAMTRVADVIAQTKPERPRVFierMGGYADDCCLSFGAENFGKYVELAGGHNIGSDVLPSTFGQLNPEQVIAANPEHVVV 275
Cdd:pfam01497 120 SALAAAKKAVPSLTRKPVLVF---GGADGGGYVVAGSNTYIGDLLRILGIENIAAELSGSEYAPISFEAILSSNPDVIIV 196
|
....*.
gi 1550139372 276 TSADWE 281
Cdd:pfam01497 197 SGRDSF 202
|
|
| btuF |
PRK09534 |
corrinoid ABC transporter substrate-binding protein; Reviewed |
36-278 |
2.99e-07 |
|
corrinoid ABC transporter substrate-binding protein; Reviewed
Pssm-ID: 236552 [Multi-domain] Cd Length: 359 Bit Score: 51.83 E-value: 2.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550139372 36 PTTVTDIAGREVTVNAPVKRILLGEGRQLYLIASLEPKDPLARIVAWRNDLIEADPATYAQYLEAFPklaklpafpgqen 115
Cdd:PRK09534 43 PVTETDATGTEITLDERPERVVTLNPSAAQTMWELGARDRVVGVTQYASYLDGAEERTNVSGGQPFG------------- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550139372 116 glLDIESTIVQKPDVVLlnleAMRANEDvNYIEKLAELKIPVLyidfrHYPLKNTEPTIR----LLGKIMGREARAEEII 191
Cdd:PRK09534 110 --VNVEAVVGLDPDLVL----APNAVAG-DTVTRLREAGITVF-----HFPAATSIEDVAektaTIGRLTGNCEAAAETN 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550139372 192 AFRHQAMTRVADVIAQTKpERPRVFIERMGGYADdcclsfGAENF-GKYVELAGGHNIGSDVLPSTFGQLNPEQVIAANP 270
Cdd:PRK09534 178 AEMRDRVDAVEDRTADVD-DRPRVLYPLGDGYTA------GGNTFiGALIEAAGGHNVAADATTDGYPQLSEEVIVQQDP 250
|
....*...
gi 1550139372 271 EHVVVTSA 278
Cdd:PRK09534 251 DVIVVATA 258
|
|
| FatB |
cd01140 |
Siderophore binding protein FatB. These proteins have been shown to function as ABC-type ... |
103-275 |
3.06e-07 |
|
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: 51.10 E-value: 3.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550139372 103 KLAKLPAFPGQENGLL---DIESTIVQKPDVVLLnleAMRANEDVNYIEKLAElkIPVLYIDFRHYpLKNTEPTIRLLGK 179
Cdd:cd01140 45 YLKKYKDDKYANVGTLfepDLEAIAALKPDLIII---GGRLAEKYDELKKIAP--TIDLGADLKNY-LESVKQNIETLGK 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550139372 180 IMGREARAEEIIAfrhQAMTRVADVIAQTKPERPRVFIERMGGYaddccLSFGAEN--FGKYVELAGGHNIGSDVLPSTF 257
Cdd:cd01140 119 IFGKEEEAKELVA---EIDASIAEAKSAAKGKKKALVVLVNGGK-----LSAFGPGsrFGWLHDLLGFEPADENIKASSH 190
|
170
....*....|....*....
gi 1550139372 258 GQ-LNPEQVIAANPEHVVV 275
Cdd:cd01140 191 GQpVSFEYILEANPDWLFV 209
|
|
| FhuD |
cd01146 |
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial ... |
89-216 |
2.45e-06 |
|
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: 48.44 E-value: 2.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550139372 89 ADPATYAQYLEAFPKLAKLPAFPGQEnGLLDIESTIVQKPDVVLLNleAMRANEDVNYIEKLAelkiPVLYIDFRHyPLK 168
Cdd:cd01146 28 ADTAGYKPWIPEPALPLEGVVDVGTR-GQPNLEAIAALKPDLILGS--ASRHDEIYDQLSQIA----PTVLLDSSP-WLA 99
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1550139372 169 NTEPTIRLLGKIMGREARAEEIIAfRHQAmtRVADVIAQTKPERPRVF 216
Cdd:cd01146 100 EWKENLRLIAKALGKEEEAEKLLA-EYDQ--RLAELRQKLPDKGPKPV 144
|
|
| TroA_d |
cd01141 |
Periplasmic binding protein TroA_d. These proteins are predicted to function as initial ... |
46-245 |
3.66e-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: 43.95 E-value: 3.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550139372 46 EVTVNAPVKRILLGEGRQLYLIASLEPKDPLARIVAWRndlieadpatyaqYLEAFPKLAKLPAFPGQENGLLDIESTIV 125
Cdd:cd01141 1 AKTIKVPPKRIVVLSPTHVDLLLALDKADKIVGVSASA-------------YDLNTPAVKERIDIQVGPTGSLNVELIVA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550139372 126 QKPDVVLLNleAMRANEDVnyIEKLAELKIPVLYIDFRHYPLKNTEpTIRLLGKIMG--REARAEEIIAFRHQAMTRVAD 203
Cdd:cd01141 68 LKPDLVILY--GGFQAQTI--LDKLEQLGIPVLYVNEYPSPLGRAE-WIKFAAAFYGvgKEDKADEAFAQIAGRYRDLAK 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1550139372 204 VIAQTKpeRPRVFIERM--GGYADDCclsfGAENFGKYVELAGG 245
Cdd:cd01141 143 KVSNLN--KPTVAIGKPvkGLWYMPG----GNSYVAKMLRDAGG 180
|
|
| PRK10957 |
PRK10957 |
iron-enterobactin transporter periplasmic binding protein; Provisional |
115-213 |
4.12e-03 |
|
iron-enterobactin transporter periplasmic binding protein; Provisional
Pssm-ID: 236806 [Multi-domain] Cd Length: 317 Bit Score: 38.80 E-value: 4.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1550139372 115 NGLLDIESTIVQKPDVVLLNleAMRANEDVNYIEKLAELKiPVLYIDfrhYPLKNTEPTIRLLGKIMGREARAEEIIAFR 194
Cdd:PRK10957 101 IGEPDAEAVAAQMPDLIVIS--ATGGDSALALYDQLSAIA-PTLVID---YDDKSWQELATQLGEATGLEKQAAAVIAQF 174
|
90
....*....|....*....
gi 1550139372 195 HQAMTRVADVIaqTKPERP 213
Cdd:PRK10957 175 DAQLAEVKAKI--TLPPQP 191
|
|
| |
