|
Name |
Accession |
Description |
Interval |
E-value |
| TroA_f |
cd01139 |
Periplasmic binding protein TroA_f. These proteins are predicted to function as initial ... |
28-360 |
8.54e-99 |
|
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: 296.53 E-value: 8.54e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497339934 28 LTVTDLDGRAITLQHEPQRIILQDGRDIMAMALLDRDNPFRRVVAWNNLARKQDINTWKMLQEKWPQSAQILDMGFSDKG 107
Cdd:cd01139 1 ITVTDVAGRKVTLDAPVERVLLGEGRQLYALALLEGENPFARIVGWGGDLKKGDPDTYAKYKEKFPEIADIPLIGSTYNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497339934 108 NVDLESVISRQPDLMIAQLRAKPALEESGVISKLSALNIPVLFVDYEINPGKDTAPSIDLLGKVLNREENAKAYTDYYRQ 187
Cdd:cd01139 81 DFSVEKVLTLKPDLVILNIWAKTTAEESGILEKLEQAGIPVVFVDFRQKPLKNTTPSMRLLGKALGREERAEEFIEFYQE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497339934 188 QLDAIRQKTANIT-PKANVFVEALAGNSDACCFTHGHNGWGGLVEAVGANNIGSQLLPGASGFVSLEKVISMKPDAYIMT 266
Cdd:cd01139 161 RIDRIRDRLAKINePKPKVFIELGAGGPEECCSTYGNGNWGELVDAAGGDNIADGLIPGTSGELNAEYVIAANPEIIIAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497339934 267 GS----KRGNSQVLPLGLQADPQEvnRQAERLLSRTGVSNIPTIEAKRAYGIYHHFYNHPWNIVGMAYLAKDIYPQTFSD 342
Cdd:cd01139 241 GGnwakDPSGVSLGPDGTTADAKE--SLLRALLKRPGWSSLQAVKNGRVYALWHQFYRSPYNFVALEAFAKWLYPELFKD 318
|
330
....*....|....*...
gi 497339934 343 LNPDDSWHYIVRHFTTLP 360
Cdd:cd01139 319 LDPEATLQEFHRQFLPVD 336
|
|
| PRK14048 |
PRK14048 |
ferrichrome/ferrioxamine B periplasmic transporter; Provisional |
3-360 |
6.93e-48 |
|
ferrichrome/ferrioxamine B periplasmic transporter; Provisional
Pssm-ID: 172540 [Multi-domain] Cd Length: 374 Bit Score: 166.23 E-value: 6.93e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497339934 3 RKSVGSFILTALISTPLCSFA-AQYPLTVTDLDGRAITLQHEPQRIILQDGRDIMAMALLDRDnPFRRVVAWNNLARKQD 81
Cdd:PRK14048 6 RSLVRLVAFLAIAFLALSALAeVQWPMTVTDAVGREVTIPAPPKAVLLGSGFNLIALSLIHPD-PVSLLAGWSGDMKGDN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497339934 82 INTWKMLQEKWPQSAQILDMGFSDKGNVDLESVISRQPDLMIaqLRAKPALEESGV--ISKLSALNIPVLFVDYEINPGK 159
Cdd:PRK14048 85 PEIYESFLRKFPELADVPLIDDGSGPGLSFETILTLKADLAI--LANWQADTEAGQraIEYLESIGVPVIVVDFNNEALK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497339934 160 DTAPSIDLLGKVLNREENAKAYTDYYRQQLDAIRQKTANIT-PKANVFVEALAgNSDACCFTHGHNGWGGLVEAVGANNI 238
Cdd:PRK14048 163 NTPDNMRLLGKVFEREEQAEDFARFYEERLARIRDRVAKHSePGPTVLMEAFP-AADRCCWAYGRGGLGEFIALTGSRNI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497339934 239 GSQLLPGASGFVSLEKVISMKPDAYIMTGSKRGNSQVLPLGLQADPQEVNRQAERLLSRTGVSNIPTIEAKRAYGIYHHF 318
Cdd:PRK14048 242 AEGALPRPGGMMNAEAIMAENPDVYIATSSPGGKYSGFSIGPGVSAEEAETTLANVVDKPVMASIAAVRDGRVHGLWNFF 321
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 497339934 319 YNHPWNIVGMAYLAKDIYPQTFSDLNPDDSWHYIVRHFTTLP 360
Cdd:PRK14048 322 NAVPLNIVAAEAFASWLRPELFADIDPAATLAEINRRFAAVP 363
|
|
| FepB |
COG0614 |
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ... |
46-341 |
3.47e-43 |
|
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 440379 [Multi-domain] Cd Length: 264 Bit Score: 150.92 E-value: 3.47e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497339934 46 RIILQDGRDIMAMALLDRDNpfrRVVAWNNlarkqdintWKMLQEKWPQSAQILDMGFSDkgNVDLESVISRQPDLMIAQ 125
Cdd:COG0614 2 RIVSLSPSATELLLALGAGD---RLVGVSD---------WGYCDYPELELKDLPVVGGTG--EPNLEAILALKPDLVLAS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497339934 126 lrakPALEESGVISKLSALNIPVLFVDYeiNPGKDTAPSIDLLGKVLNREENAKAYTDYYRQQLDAIRQKTANITPKANV 205
Cdd:COG0614 68 ----SSGNDEEDYEQLEKIGIPVVVLDP--RSLEDLYESIRLLGELLGREERAEALIAEYEARLAAVRARLAGAEERPTV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497339934 206 FVEALAGNSdaCCFTHGHNGWGGLVEAVGANNIGSQlLPGASGFVSLEKVISMKPDAYIMTGSkrgnsqvlplglQADPQ 285
Cdd:COG0614 142 LYEIWSGDP--LYTAGGGSFIGELLELAGGRNVAAD-LGGGYPEVSLEQVLALDPDVIILSGG------------GYDAE 206
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 497339934 286 EVNRQAERLLSRTGVSNIPTIEAKRAYGIYHHF--YNHPWNIVGMAYLAKDIYPQTFS 341
Cdd:COG0614 207 TAEEALEALLADPGWQSLPAVKNGRVYVVPGDLlsRPGPRLLLALEDLAKALHPELFA 264
|
|
| Peripla_BP_2 |
pfam01497 |
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ... |
107-314 |
1.98e-15 |
|
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: 74.71 E-value: 1.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497339934 107 GNVDLESVISRQPDLMIAQLRAKPALEEsgvisKLSALNIPVLFV--DYEINPGKDTapsIDLLGKVLNREENAKAYTDY 184
Cdd:pfam01497 46 GEINVERLAALKPDLVILSTGYLTDEAE-----ELLSLIIPTVIFesSSTGESLKEQ---IKQLGELLGLEDEAEELVAE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497339934 185 YRQQLDAIRQKTANITPK-ANVFVEAlagnSDACCFTHGHNGWGG-LVEAVGANNIGSQLLPGASGFVSLEKVISMKPDA 262
Cdd:pfam01497 118 IDSALAAAKKAVPSLTRKpVLVFGGA----DGGGYVVAGSNTYIGdLLRILGIENIAAELSGSEYAPISFEAILSSNPDV 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 497339934 263 YIMTGSKRGNSQVlplglqadpqevnrqAERLLSRTGVSNIPTIEAKRAYGI 314
Cdd:pfam01497 194 IIVSGRDSFTKTG---------------PEFVAANPLWAGLPAVKNGRVYTL 230
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| TroA_f |
cd01139 |
Periplasmic binding protein TroA_f. These proteins are predicted to function as initial ... |
28-360 |
8.54e-99 |
|
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: 296.53 E-value: 8.54e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497339934 28 LTVTDLDGRAITLQHEPQRIILQDGRDIMAMALLDRDNPFRRVVAWNNLARKQDINTWKMLQEKWPQSAQILDMGFSDKG 107
Cdd:cd01139 1 ITVTDVAGRKVTLDAPVERVLLGEGRQLYALALLEGENPFARIVGWGGDLKKGDPDTYAKYKEKFPEIADIPLIGSTYNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497339934 108 NVDLESVISRQPDLMIAQLRAKPALEESGVISKLSALNIPVLFVDYEINPGKDTAPSIDLLGKVLNREENAKAYTDYYRQ 187
Cdd:cd01139 81 DFSVEKVLTLKPDLVILNIWAKTTAEESGILEKLEQAGIPVVFVDFRQKPLKNTTPSMRLLGKALGREERAEEFIEFYQE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497339934 188 QLDAIRQKTANIT-PKANVFVEALAGNSDACCFTHGHNGWGGLVEAVGANNIGSQLLPGASGFVSLEKVISMKPDAYIMT 266
Cdd:cd01139 161 RIDRIRDRLAKINePKPKVFIELGAGGPEECCSTYGNGNWGELVDAAGGDNIADGLIPGTSGELNAEYVIAANPEIIIAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497339934 267 GS----KRGNSQVLPLGLQADPQEvnRQAERLLSRTGVSNIPTIEAKRAYGIYHHFYNHPWNIVGMAYLAKDIYPQTFSD 342
Cdd:cd01139 241 GGnwakDPSGVSLGPDGTTADAKE--SLLRALLKRPGWSSLQAVKNGRVYALWHQFYRSPYNFVALEAFAKWLYPELFKD 318
|
330
....*....|....*...
gi 497339934 343 LNPDDSWHYIVRHFTTLP 360
Cdd:cd01139 319 LDPEATLQEFHRQFLPVD 336
|
|
| PRK14048 |
PRK14048 |
ferrichrome/ferrioxamine B periplasmic transporter; Provisional |
3-360 |
6.93e-48 |
|
ferrichrome/ferrioxamine B periplasmic transporter; Provisional
Pssm-ID: 172540 [Multi-domain] Cd Length: 374 Bit Score: 166.23 E-value: 6.93e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497339934 3 RKSVGSFILTALISTPLCSFA-AQYPLTVTDLDGRAITLQHEPQRIILQDGRDIMAMALLDRDnPFRRVVAWNNLARKQD 81
Cdd:PRK14048 6 RSLVRLVAFLAIAFLALSALAeVQWPMTVTDAVGREVTIPAPPKAVLLGSGFNLIALSLIHPD-PVSLLAGWSGDMKGDN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497339934 82 INTWKMLQEKWPQSAQILDMGFSDKGNVDLESVISRQPDLMIaqLRAKPALEESGV--ISKLSALNIPVLFVDYEINPGK 159
Cdd:PRK14048 85 PEIYESFLRKFPELADVPLIDDGSGPGLSFETILTLKADLAI--LANWQADTEAGQraIEYLESIGVPVIVVDFNNEALK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497339934 160 DTAPSIDLLGKVLNREENAKAYTDYYRQQLDAIRQKTANIT-PKANVFVEALAgNSDACCFTHGHNGWGGLVEAVGANNI 238
Cdd:PRK14048 163 NTPDNMRLLGKVFEREEQAEDFARFYEERLARIRDRVAKHSePGPTVLMEAFP-AADRCCWAYGRGGLGEFIALTGSRNI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497339934 239 GSQLLPGASGFVSLEKVISMKPDAYIMTGSKRGNSQVLPLGLQADPQEVNRQAERLLSRTGVSNIPTIEAKRAYGIYHHF 318
Cdd:PRK14048 242 AEGALPRPGGMMNAEAIMAENPDVYIATSSPGGKYSGFSIGPGVSAEEAETTLANVVDKPVMASIAAVRDGRVHGLWNFF 321
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 497339934 319 YNHPWNIVGMAYLAKDIYPQTFSDLNPDDSWHYIVRHFTTLP 360
Cdd:PRK14048 322 NAVPLNIVAAEAFASWLRPELFADIDPAATLAEINRRFAAVP 363
|
|
| FepB |
COG0614 |
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ... |
46-341 |
3.47e-43 |
|
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 440379 [Multi-domain] Cd Length: 264 Bit Score: 150.92 E-value: 3.47e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497339934 46 RIILQDGRDIMAMALLDRDNpfrRVVAWNNlarkqdintWKMLQEKWPQSAQILDMGFSDkgNVDLESVISRQPDLMIAQ 125
Cdd:COG0614 2 RIVSLSPSATELLLALGAGD---RLVGVSD---------WGYCDYPELELKDLPVVGGTG--EPNLEAILALKPDLVLAS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497339934 126 lrakPALEESGVISKLSALNIPVLFVDYeiNPGKDTAPSIDLLGKVLNREENAKAYTDYYRQQLDAIRQKTANITPKANV 205
Cdd:COG0614 68 ----SSGNDEEDYEQLEKIGIPVVVLDP--RSLEDLYESIRLLGELLGREERAEALIAEYEARLAAVRARLAGAEERPTV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497339934 206 FVEALAGNSdaCCFTHGHNGWGGLVEAVGANNIGSQlLPGASGFVSLEKVISMKPDAYIMTGSkrgnsqvlplglQADPQ 285
Cdd:COG0614 142 LYEIWSGDP--LYTAGGGSFIGELLELAGGRNVAAD-LGGGYPEVSLEQVLALDPDVIILSGG------------GYDAE 206
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 497339934 286 EVNRQAERLLSRTGVSNIPTIEAKRAYGIYHHF--YNHPWNIVGMAYLAKDIYPQTFS 341
Cdd:COG0614 207 TAEEALEALLADPGWQSLPAVKNGRVYVVPGDLlsRPGPRLLLALEDLAKALHPELFA 264
|
|
| TroA_e |
cd01142 |
Periplasmic binding protein TroA_e. These proteins are predicted to function as initial ... |
21-345 |
2.39e-21 |
|
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: 92.80 E-value: 2.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497339934 21 SFAAQYPLTVTDLDGRAITLQHEPQRI-ILQDGRDIMAMALLDRDnpfrRVVAwnnlarkqdiNTWKMLQEKW-----PQ 94
Cdd:cd01142 1 PAATAATRTITDMAGRKVTIPDEVKRIaALWGAGNAVVAALGGGK----LIVA----------TTSTVQQEPWlyrlaPS 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497339934 95 SAQILDMGFSDKGNVdlESVISRQPDLMIAQLRAKPaleESG--VISKLSALNIPVLFVDyeinpgkDTAPSIDLLGKVL 172
Cdd:cd01142 67 LENVATGGTGNDVNI--EELLALKPDVVIVWSTDGK---EAGkaVLRLLNALSLRDAELE-------EVKLTIALLGELL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497339934 173 NREENAKAYTDYYRQQLDAIRQKTANI--TPKANVFVEALAGNSDACcfTHGHNGWggLVEAVGANNIGSQLLPGASGFV 250
Cdd:cd01142 135 GRQEKAEALVAYFDDNLAYVAARTKKLpdSERPRVYYAGPDPLTTDG--TGSITNS--WIDLAGGINVASEATKKGSGEV 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497339934 251 SLEKVISMKPDAYI-MTGSKRGnsqvlplGLQADPQevnrqaerllsrtgVSNIPTIEAKRAYGIYHHFYnhPW------ 323
Cdd:cd01142 211 SLEQLLKWNPDVIIvGNADTKA-------AILADPR--------------WQNLRAVKNGRVYVNPEGAF--WWdrpsae 267
|
330 340
....*....|....*....|..
gi 497339934 324 NIVGMAYLAKDIYPQTFSDLNP 345
Cdd:cd01142 268 EALLGLWLAKTLYPERFTDDDM 289
|
|
| HemV-2 |
cd01147 |
Metal binding protein HemV-2. These proteins are predicted to function as initial receptors ... |
107-267 |
1.25e-15 |
|
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: 75.83 E-value: 1.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497339934 107 GNVDLESVISRQPDLMIAQLRAKPALEESGVISKLsalNIPVLFVDYEINPgKDTAPSIDLLGKVLNREENAKAYTDYYR 186
Cdd:cd01147 63 NTPNYEKIAALKPDVVIDVGSDDPTSIADDLQKKT---GIPVVVLDGGDSL-EDTPEQIRLLGKVLGKEERAEELISFIE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497339934 187 QQLDAIRQKTANI--TPKANVFVEALaGNSDACCFTHGHNGWGGLVEAVGANNIGSQLLPGASGFVSLEKVISMKPDaYI 264
Cdd:cd01147 139 SILADVEERTKDIpdEEKPTVYFGRI-GTKGAAGLESGLAGSIEVFELAGGINVADGLGGGGLKEVSPEQILLWNPD-VI 216
|
...
gi 497339934 265 MTG 267
Cdd:cd01147 217 FLD 219
|
|
| TroA-like |
cd00636 |
Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function ... |
107-207 |
1.27e-15 |
|
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: 73.36 E-value: 1.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497339934 107 GNVDLESVISRQPDLMIAQLRAKPALEEsgvisKLSALNIPVLFVDYEINPGKDTAP-SIDLLGKVLNREENAKAYTDYY 185
Cdd:cd00636 50 YEPNLEKIAALKPDLIIANGSGLEAWLD-----KLSKIAIPVVVVDEASELSLENIKeSIRLIGKALGKEENAEELIAEL 124
|
90 100
....*....|....*....|..
gi 497339934 186 RQQLDAIRQKTANITPKANVFV 207
Cdd:cd00636 125 DARLAELRAKLAKIPKKKVSLV 146
|
|
| Peripla_BP_2 |
pfam01497 |
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ... |
107-314 |
1.98e-15 |
|
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: 74.71 E-value: 1.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497339934 107 GNVDLESVISRQPDLMIAQLRAKPALEEsgvisKLSALNIPVLFV--DYEINPGKDTapsIDLLGKVLNREENAKAYTDY 184
Cdd:pfam01497 46 GEINVERLAALKPDLVILSTGYLTDEAE-----ELLSLIIPTVIFesSSTGESLKEQ---IKQLGELLGLEDEAEELVAE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497339934 185 YRQQLDAIRQKTANITPK-ANVFVEAlagnSDACCFTHGHNGWGG-LVEAVGANNIGSQLLPGASGFVSLEKVISMKPDA 262
Cdd:pfam01497 118 IDSALAAAKKAVPSLTRKpVLVFGGA----DGGGYVVAGSNTYIGdLLRILGIENIAAELSGSEYAPISFEAILSSNPDV 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 497339934 263 YIMTGSKRGNSQVlplglqadpqevnrqAERLLSRTGVSNIPTIEAKRAYGI 314
Cdd:pfam01497 194 IIVSGRDSFTKTG---------------PEFVAANPLWAGLPAVKNGRVYTL 230
|
|
| TroA_a |
cd01148 |
Metal binding protein TroA_a. These proteins are predicted to function as initial receptors ... |
26-273 |
4.33e-14 |
|
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: 71.99 E-value: 4.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497339934 26 YPLTVtDLDGRAITLQHEPQRIILQDGR--DIM-AMALLDRdnpfrrvVAWNNLARKQDINTWKMLQEKWPQSAqildmg 102
Cdd:cd01148 1 YPLTV-ENCGRSVTFDKAPQRVVSNDQNttEMMlALGLQDR-------MVGTAGIDNKDLPELKAKYDKVPELA------ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497339934 103 fsdKGNVDLESVISRQPDLMIAQLRAKPALEESGVISKLSALNIPVlFVDYEINPGKDTAPSIDL-------LGKVLNRE 175
Cdd:cd01148 67 ---KKYPSKETVLAARPDLVFGGWSYGFDKGGLGTPDSLAELGIKT-YILPESCGQRRGEATLDDvyndirnLGKIFDVE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497339934 176 ENAKAYTDYYRQQLDAIRQKTANITPKANVFVEALAGNSDaccFTHGHNGWGG-LVEAVGANNIGSQlLPGASGFVSLEK 254
Cdd:cd01148 143 DRADKLVADLKARLAEISAKVKGDGKKVAVFVYDSGEDKP---FTSGRGGIPNaIITAAGGRNVFAD-VDESWTTVSWET 218
|
250
....*....|....*....
gi 497339934 255 VISMKPDAYIMTGSKRGNS 273
Cdd:cd01148 219 VIARNPDVIVIIDYGDQNA 237
|
|
| YvrC |
cd01143 |
Periplasmic binding protein YvrC. These proteins are predicted to function as initial ... |
107-264 |
1.40e-12 |
|
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: 65.76 E-value: 1.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497339934 107 GNVDLESVISRQPDLMIAQLRAKPALEEsgvisKLSALNIPVLFVDYEiNPGKDTAPSIDLLGKVLNREENAKAYTDYYR 186
Cdd:cd01143 49 SNPNVEKIVALKPDLVIVSSSSLAELLE-----KLKDAGIPVVVLPAA-SSLDEIYDQIELIGKITGAEEEAEKLVKEMK 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497339934 187 QQLDAIRQKTANItPKANVFVEAlagnSDACCFTHGHNGW-GGLVEAVGANNIgsqlLPGASGF--VSLEKVISMKPDAY 263
Cdd:cd01143 123 QKIDKVKDKGKTI-KKSKVYIEV----SLGGPYTAGKNTFiNELIRLAGAKNI----AADSGGWpqVSPEEILKANPDVI 193
|
.
gi 497339934 264 I 264
Cdd:cd01143 194 I 194
|
|
| BtuF |
cd01144 |
Cobalamin binding protein BtuF. These proteins have been shown to function as initial ... |
92-264 |
9.72e-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: 64.24 E-value: 9.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497339934 92 WPQSAQILDMGFSDKgNVDLESVISRQPDLMIAQLRAKPALeesgVISKLSALNIPVLFVdyEINPGKDTAPSIDLLGKV 171
Cdd:cd01144 32 YPPEAKKLPRVGGFY-QLDLERVLALKPDLVIAWDDCNVCA----VVDQLRAAGIPVLVS--EPQTLDDILADIRRLGTL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497339934 172 LNREENAKAYTDYYRQQLDAIRQKTANITPKaNVFVEAlagnSDACCFTHGHNGWGGLVEAVGANNIGSQlLPGASGFVS 251
Cdd:cd01144 105 AGRPARAEELAEALRRRLAALRKQYASKPPP-RVFYQE----WIDPLMTAGGDWVPELIALAGGVNVFAD-AGERSPQVS 178
|
170
....*....|...
gi 497339934 252 LEKVISMKPDAYI 264
Cdd:cd01144 179 WEDVLAANPDVIV 191
|
|
| HutB |
cd01149 |
Hemin binding protein HutB. These proteins have been shown to function as initial receptors ... |
112-266 |
2.36e-11 |
|
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: 63.05 E-value: 2.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497339934 112 ESVISRQPDLMIAQLRAKPALeesgVISKLSALNIPVLFVdyeinPGKDT----APSIDLLGKVLNREENAKAYTDYYRQ 187
Cdd:cd01149 52 EGVLSLKPTLVIASDEAGPPE----ALDQLRAAGVPVVTV-----PSTPTldglLTKIRQVAQALGVPEKGEALAQEVRQ 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497339934 188 QLDAIRQKTANIT-PKANVFVEALAG--------NSDAccfthghngwGGLVEAVGANNIGSqllpGASGF--VSLEKVI 256
Cdd:cd01149 123 RLAALRKTVAAHKkPPRVLFLLSHGGgaamaagrNTAA----------DAIIALAGAVNAAA----GFRGYkpLSAEALI 188
|
170
....*....|
gi 497339934 257 SMKPDAYIMT 266
Cdd:cd01149 189 AAQPDVILVM 198
|
|
| FhuD |
cd01146 |
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial ... |
110-265 |
3.47e-10 |
|
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: 59.99 E-value: 3.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497339934 110 DLESVISRQPDLMIA-QLRAKPALEesgvisKLSAlnI-PVLFVDYeINPGKDTAPSIDLLGKVLNREENAKAYTDYYRQ 187
Cdd:cd01146 57 NLEAIAALKPDLILGsASRHDEIYD------QLSQ--IaPTVLLDS-SPWLAEWKENLRLIAKALGKEEEAEKLLAEYDQ 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497339934 188 QLDAIRQKTANITPKANVFVEALAGNSdacCFTHGHNGW-GGLVEAVGANNIGSQLLPGASGF--VSLEKVisMKPDAYI 264
Cdd:cd01146 128 RLAELRQKLPDKGPKPVSVVRFSDAGS---IRLYGPNSFaGSVLEDLGLQNPWAQETTNDSGFatISLERL--AKADADV 202
|
.
gi 497339934 265 M 265
Cdd:cd01146 203 L 203
|
|
| FecB |
COG4594 |
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and ... |
110-266 |
2.90e-09 |
|
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443650 [Multi-domain] Cd Length: 316 Bit Score: 57.62 E-value: 2.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497339934 110 DLESVISRQPDLMIA-QLRAKpaleesGVISKLSAlnI-PVLFVDYEINPGKDTAPSIDLLGKVLNREENAKAYTDYYRQ 187
Cdd:COG4594 106 NLEAIAALKPDLIIAdKSRHE------AIYDQLSK--IaPTVLFKSRNGDYQENLESFKTIAKALGKEEEAEAVLADHDQ 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497339934 188 QLDAIRQKTANITPKANV-FVEALAGNSDAccftHGHNGW-GGLVEAVGANNIGSQLLPGASGF--VSLEKVISMKPD-A 262
Cdd:COG4594 178 RIAEAKAKLAAADKGKKVaVGQFRADGLRL----YTPNSFaGSVLAALGFENPPKQSKDNGYGYseVSLEQLPALDPDvL 253
|
....
gi 497339934 263 YIMT 266
Cdd:COG4594 254 FIAT 257
|
|
| btuF |
PRK09534 |
corrinoid ABC transporter substrate-binding protein; Reviewed |
18-266 |
2.64e-08 |
|
corrinoid ABC transporter substrate-binding protein; Reviewed
Pssm-ID: 236552 [Multi-domain] Cd Length: 359 Bit Score: 54.91 E-value: 2.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497339934 18 PLCSFaaqyPLTVTDLDGRAITLQHEPQRIILQDGRDIMAM-ALLDRDnpfrRVVAWNNLARKQDintwkmlqekwpQSA 96
Cdd:PRK09534 38 RACSF----PVTETDATGTEITLDERPERVVTLNPSAAQTMwELGARD----RVVGVTQYASYLD------------GAE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497339934 97 QILDMGFSDKGNVDLESVISRQPDLMIAqlrakPALEESGVISKLSALNIPVlfvdYEINPG---KDTAPSIDLLGKVLN 173
Cdd:PRK09534 98 ERTNVSGGQPFGVNVEAVVGLDPDLVLA-----PNAVAGDTVTRLREAGITV----FHFPAAtsiEDVAEKTATIGRLTG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497339934 174 REENAKAYTDYYRQQLDAIRQKTANITPKANVFVEaLAGNsdaccFTHGHNGW-GGLVEAVGANNIGSQllPGASGF--V 250
Cdd:PRK09534 169 NCEAAAETNAEMRDRVDAVEDRTADVDDRPRVLYP-LGDG-----YTAGGNTFiGALIEAAGGHNVAAD--ATTDGYpqL 240
|
250
....*....|....*.
gi 497339934 251 SLEKVISMKPDAYIMT 266
Cdd:PRK09534 241 SEEVIVQQDPDVIVVA 256
|
|
| PRK10957 |
PRK10957 |
iron-enterobactin transporter periplasmic binding protein; Provisional |
10-313 |
5.30e-08 |
|
iron-enterobactin transporter periplasmic binding protein; Provisional
Pssm-ID: 236806 [Multi-domain] Cd Length: 317 Bit Score: 53.82 E-value: 5.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497339934 10 ILTALISTPLCSFAAQ----YPLTVTDLDGrAITLQHEPQRII----------LQDGRDIMAMAL------LDRDNPFRR 69
Cdd:PRK10957 7 LLLLGLLLSGIAAAQAsaagWPRTVTDSRG-SVTLESKPQRIVstsvtltgtlLAIDAPVIASGAttpntrVADDQGFFR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497339934 70 vvAWNNLARKQDIntwkmlqEKWPQsaqildmgfsdkGNVDLESVISRQPDLMIAQLR-AKPALEEsgvISKLSALnIPV 148
Cdd:PRK10957 86 --QWSDVAKERGV-------EVLYI------------GEPDAEAVAAQMPDLIVISATgGDSALAL---YDQLSAI-APT 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497339934 149 LFVDYEINPGKDTApsiDLLGKVLNREENAKAYTDYYRQQLDAIRQKtanITPKANVfVEALAGNSDAccftHGHNGWgg 228
Cdd:PRK10957 141 LVIDYDDKSWQELA---TQLGEATGLEKQAAAVIAQFDAQLAEVKAK---ITLPPQP-VSALVYNGAG----HSANLW-- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497339934 229 lvEAVGANnigSQLLpGASGFvSLEKVismkPDAYIMTGSKRGNSQVLPLGLQADPQEVN-----------RQAERLLSR 297
Cdd:PRK10957 208 --TPESAQ---GQLL-EQLGF-TLAEL----PAGLQASTSQGKRHDIIQLGGENLAAGLNgetlflfagddKDADAFLAD 276
|
330
....*....|....*.
gi 497339934 298 TGVSNIPTIEAKRAYG 313
Cdd:PRK10957 277 PLLANLPAVQNKQVYA 292
|
|
| FatB |
cd01140 |
Siderophore binding protein FatB. These proteins have been shown to function as ABC-type ... |
108-261 |
2.85e-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: 2.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497339934 108 NVDLESVISRQPDLMIAQLRAKPALEEsgvISKLSalNIPVLFVDYEiNPGKDTAPSIDLLGKVLNREENAKAYTDYYRQ 187
Cdd:cd01140 62 EPDLEAIAALKPDLIIIGGRLAEKYDE---LKKIA--PTIDLGADLK-NYLESVKQNIETLGKIFGKEEEAKELVAEIDA 135
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497339934 188 QLDAIRQKTANitpKANVFVEALAGNSDACCFTHGHNGWggLVEAVGANNIGSQLLPGASGF-VSLEKVISMKPD 261
Cdd:cd01140 136 SIAEAKSAAKG---KKKALVVLVNGGKLSAFGPGSRFGW--LHDLLGFEPADENIKASSHGQpVSFEYILEANPD 205
|
|
| CeuA |
COG4607 |
ABC-type enterochelin transport system, periplasmic component [Inorganic ion transport and ... |
110-198 |
1.14e-04 |
|
ABC-type enterochelin transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443657 [Multi-domain] Cd Length: 310 Bit Score: 43.63 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497339934 110 DLESVISRQPDLMIAQLRAKPALEEsgvISKLSalniPVLFVDyeiNPGKDTAPS----IDLLGKVLNREENAKAYTDYY 185
Cdd:COG4607 102 DLEAIAALKPDLIIIGGRSAKKYDE---LSKIA----PTIDLT---VDGEDYLESlkrnTETLGEIFGKEDEAEELVADL 171
|
90
....*....|...
gi 497339934 186 RQQLDAIRQKTAN 198
Cdd:COG4607 172 DAKIAALKAAAAG 184
|
|
| FeuA |
cd01138 |
Periplasmic binding protein FeuA. These proteins have predicted to function as initial ... |
94-207 |
3.86e-04 |
|
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: 41.55 E-value: 3.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497339934 94 QSAQILDMGFSDKGNVDLESVISRQPDLMIAQLRAKPALEEsgvISKLSalniPVLFVDYEinpGKDTAPSIDLLGKVLN 173
Cdd:cd01138 42 YKKKTLAKVVGIVDEPNLEKVLELKPDLIIVSSKQEENYEK---LSKIA----PTVPVSYN---SSDWEEQLKEIGKLLN 111
|
90 100 110
....*....|....*....|....*....|....*
gi 497339934 174 REENAKAYTDYYRQQLDAIRQKTAN-ITPKANVFV 207
Cdd:cd01138 112 KEDEAEKWLADYKQKAKEAKEKIKKkLGNDKSVAV 146
|
|
| PRK03379 |
PRK03379 |
vitamin B12-transporter protein BtuF; Provisional |
92-269 |
1.11e-03 |
|
vitamin B12-transporter protein BtuF; Provisional
Pssm-ID: 179575 [Multi-domain] Cd Length: 260 Bit Score: 40.44 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497339934 92 WPQSAQILDMGFSDKGnVDLESVISRQPDLMIAQLRAKPaleeSGVISKLSALNIPVLFVDYEINpgKDTAPSIDLLGKV 171
Cdd:PRK03379 47 YPPQAKKIEQVATWQG-MNLERIVALKPDLVLAWRGGNA----ERQVDQLASLGIKVMWVDATSI--EQIANALRQLAPW 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497339934 172 LNREENAKAYTDYYRQQLDAIRQKTANITPKaNVFVEAlaGNSDAccFTHG-HNGWGGLVEAVGANNI--GSQLlPGASg 248
Cdd:PRK03379 120 SPQPEKAEQAAQSLLQQYAALKAQYADKPKK-RVFLQF--GTNPL--FTSGkHSIQSQVLSLCGGENIfaDSRV-PWPQ- 192
|
170 180
....*....|....*....|.
gi 497339934 249 fVSLEKVISMKPDAYIMTGSK 269
Cdd:PRK03379 193 -VSREQVLARKPQAIVITGGP 212
|
|
| |
