|
Name |
Accession |
Description |
Interval |
E-value |
| TroA_e |
cd01142 |
Periplasmic binding protein TroA_e. These proteins are predicted to function as initial ... |
14-304 |
1.80e-76 |
|
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: 236.48 E-value: 1.80e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901432 14 AFPTLATRQVVDDAGHTVTVPTQVQRIADSWFAHHSVLMTLGAGRQIVATVNHPQSQPWMFKINPSLNQ-ALQIHGTSFN 92
Cdd:cd01142 1 PAATAATRTITDMAGRKVTIPDEVKRIAALWGAGNAVVAALGGGKLIVATTSTVQQEPWLYRLAPSLENvATGGTGNDVN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901432 93 SEALLALHTDVLFVAKGKGdaqsyNQAGIPTLEMAFTDYPS-MEKS-VTTTADVLGTDQAR-ARAVAYNQFLTRTIADVR 169
Cdd:cd01142 81 IEELLALKPDVVIVWSTDG-----KEAGKAVLRLLNALSLRdAELEeVKLTIALLGELLGRqEKAEALVAYFDDNLAYVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901432 170 AKTATLAENQRPRVLHIQSlNPLKVDGRNTLIDTWIALSGGRNVAGE-VDGNMKEVSPERVLYWQPEVIILGAGCG--DI 246
Cdd:cd01142 156 ARTKKLPDSERPRVYYAGP-DPLTTDGTGSITNSWIDLAGGINVASEaTKKGSGEVSLEQLLKWNPDVIIVGNADTkaAI 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 851901432 247 ASSPyaaLFKELNAVKQGKVWRNPAGVFPWDRYGTESALQLQWAASKLHPALFGGLDM 304
Cdd:cd01142 235 LADP---RWQNLRAVKNGRVYVNPEGAFWWDRPSAEEALLGLWLAKTLYPERFTDDDM 289
|
|
| FepB |
COG0614 |
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ... |
39-299 |
4.44e-43 |
|
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 440379 [Multi-domain] Cd Length: 264 Bit Score: 149.38 E-value: 4.44e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901432 39 RIADSWFAHHSVLMTLGAGRQIVATVNHPQSQ-PWMfkinpSLNQALQIHGT-SFNSEALLALHTDVLFVAKGKGDAQSY 116
Cdd:COG0614 2 RIVSLSPSATELLLALGAGDRLVGVSDWGYCDyPEL-----ELKDLPVVGGTgEPNLEAILALKPDLVLASSSGNDEEDY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901432 117 NQ---AGIPTLEMAFTDYPSMEKSVTTTADVLGTdQARARAVAynQFLTRTIADVRAKTATLAEnqRPRVLH-IQSLNPL 192
Cdd:COG0614 77 EQlekIGIPVVVLDPRSLEDLYESIRLLGELLGR-EERAEALI--AEYEARLAAVRARLAGAEE--RPTVLYeIWSGDPL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901432 193 KVDGRNTLIDTWIALSGGRNVAGEVDGNMKEVSPERVLYWQPEVIILgAGCGDIASSPYAA--------LFKELNAVKQG 264
Cdd:COG0614 152 YTAGGGSFIGELLELAGGRNVAADLGGGYPEVSLEQVLALDPDVIIL-SGGGYDAETAEEAlealladpGWQSLPAVKNG 230
|
250 260 270
....*....|....*....|....*....|....*
gi 851901432 265 KVWRNPAGVfpWDRYGTESALQLQWAASKLHPALF 299
Cdd:COG0614 231 RVYVVPGDL--LSRPGPRLLLALEDLAKALHPELF 263
|
|
| Peripla_BP_2 |
pfam01497 |
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ... |
48-271 |
6.70e-16 |
|
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: 75.87 E-value: 6.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901432 48 HSVLMTLGAGRQIVA---TVNHPQSQPWMFKInPSLNQALQIhgtsfNSEALLALHTDVLFVAKGKGDAQSYNQ--AGIP 122
Cdd:pfam01497 8 TEILYALGATDSIVGvdaYTRDPLKADAVAAI-VKVGAYGEI-----NVERLAALKPDLVILSTGYLTDEAEELlsLIIP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901432 123 TLEMAFTDYPSmekSVTTTADVLGTD-QARARAVAYNQFLTRTIADVRAKTATlaENQRPRVLHIQSLN-PLKVDGRNTL 200
Cdd:pfam01497 82 TVIFESSSTGE---SLKEQIKQLGELlGLEDEAEELVAEIDSALAAAKKAVPS--LTRKPVLVFGGADGgGYVVAGSNTY 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 851901432 201 IDTWIALSGGRNVAGEVDGNM-KEVSPERVLYWQPEVIILGAGCGD-------IASSPyaaLFKELNAVKQGKVWRNPA 271
Cdd:pfam01497 157 IGDLLRILGIENIAAELSGSEyAPISFEAILSSNPDVIIVSGRDSFtktgpefVAANP---LWAGLPAVKNGRVYTLPS 232
|
|
| btuF |
PRK09534 |
corrinoid ABC transporter substrate-binding protein; Reviewed |
14-253 |
3.22e-06 |
|
corrinoid ABC transporter substrate-binding protein; Reviewed
Pssm-ID: 236552 [Multi-domain] Cd Length: 359 Bit Score: 48.37 E-value: 3.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901432 14 AFPTLATrqvvDDAGHTVTVPTQVQRIADSWFAHHSVLMTLGAGRQIVATVnhpQSQPWMFKINPSLNqALQIHGTSFNS 93
Cdd:PRK09534 41 SFPVTET----DATGTEITLDERPERVVTLNPSAAQTMWELGARDRVVGVT---QYASYLDGAEERTN-VSGGQPFGVNV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901432 94 EALLALHTD-VLFVAKGKGDA-QSYNQAGIPTLEMAF-TDYPSMEKSVTTTADVLGTDQArarAVAYNQFLTRTIADVRA 170
Cdd:PRK09534 113 EAVVGLDPDlVLAPNAVAGDTvTRLREAGITVFHFPAaTSIEDVAEKTATIGRLTGNCEA---AAETNAEMRDRVDAVED 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901432 171 KTATLaeNQRPRVLHiqSLNPLKVDGRNTLIDTWIALSGGRNVAGEVDGN-MKEVSPERVLYWQPEVIILGAGCGDIA-S 248
Cdd:PRK09534 190 RTADV--DDRPRVLY--PLGDGYTAGGNTFIGALIEAAGGHNVAADATTDgYPQLSEEVIVQQDPDVIVVATASALVAeT 265
|
....*
gi 851901432 249 SPYAA 253
Cdd:PRK09534 266 EPYAS 270
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| TroA_e |
cd01142 |
Periplasmic binding protein TroA_e. These proteins are predicted to function as initial ... |
14-304 |
1.80e-76 |
|
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: 236.48 E-value: 1.80e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901432 14 AFPTLATRQVVDDAGHTVTVPTQVQRIADSWFAHHSVLMTLGAGRQIVATVNHPQSQPWMFKINPSLNQ-ALQIHGTSFN 92
Cdd:cd01142 1 PAATAATRTITDMAGRKVTIPDEVKRIAALWGAGNAVVAALGGGKLIVATTSTVQQEPWLYRLAPSLENvATGGTGNDVN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901432 93 SEALLALHTDVLFVAKGKGdaqsyNQAGIPTLEMAFTDYPS-MEKS-VTTTADVLGTDQAR-ARAVAYNQFLTRTIADVR 169
Cdd:cd01142 81 IEELLALKPDVVIVWSTDG-----KEAGKAVLRLLNALSLRdAELEeVKLTIALLGELLGRqEKAEALVAYFDDNLAYVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901432 170 AKTATLAENQRPRVLHIQSlNPLKVDGRNTLIDTWIALSGGRNVAGE-VDGNMKEVSPERVLYWQPEVIILGAGCG--DI 246
Cdd:cd01142 156 ARTKKLPDSERPRVYYAGP-DPLTTDGTGSITNSWIDLAGGINVASEaTKKGSGEVSLEQLLKWNPDVIIVGNADTkaAI 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 851901432 247 ASSPyaaLFKELNAVKQGKVWRNPAGVFPWDRYGTESALQLQWAASKLHPALFGGLDM 304
Cdd:cd01142 235 LADP---RWQNLRAVKNGRVYVNPEGAFWWDRPSAEEALLGLWLAKTLYPERFTDDDM 289
|
|
| FepB |
COG0614 |
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ... |
39-299 |
4.44e-43 |
|
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 440379 [Multi-domain] Cd Length: 264 Bit Score: 149.38 E-value: 4.44e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901432 39 RIADSWFAHHSVLMTLGAGRQIVATVNHPQSQ-PWMfkinpSLNQALQIHGT-SFNSEALLALHTDVLFVAKGKGDAQSY 116
Cdd:COG0614 2 RIVSLSPSATELLLALGAGDRLVGVSDWGYCDyPEL-----ELKDLPVVGGTgEPNLEAILALKPDLVLASSSGNDEEDY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901432 117 NQ---AGIPTLEMAFTDYPSMEKSVTTTADVLGTdQARARAVAynQFLTRTIADVRAKTATLAEnqRPRVLH-IQSLNPL 192
Cdd:COG0614 77 EQlekIGIPVVVLDPRSLEDLYESIRLLGELLGR-EERAEALI--AEYEARLAAVRARLAGAEE--RPTVLYeIWSGDPL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901432 193 KVDGRNTLIDTWIALSGGRNVAGEVDGNMKEVSPERVLYWQPEVIILgAGCGDIASSPYAA--------LFKELNAVKQG 264
Cdd:COG0614 152 YTAGGGSFIGELLELAGGRNVAADLGGGYPEVSLEQVLALDPDVIIL-SGGGYDAETAEEAlealladpGWQSLPAVKNG 230
|
250 260 270
....*....|....*....|....*....|....*
gi 851901432 265 KVWRNPAGVfpWDRYGTESALQLQWAASKLHPALF 299
Cdd:COG0614 231 RVYVVPGDL--LSRPGPRLLLALEDLAKALHPELF 263
|
|
| TroA_f |
cd01139 |
Periplasmic binding protein TroA_f. These proteins are predicted to function as initial ... |
23-319 |
3.23e-24 |
|
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: 100.84 E-value: 3.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901432 23 VVDDAGHTVTVPTQVQRIAdswfahhsvlmtLGAGRQIVATVNHPQSQP------W---MFKINPSLNQALQ-------- 85
Cdd:cd01139 3 VTDVAGRKVTLDAPVERVL------------LGEGRQLYALALLEGENPfarivgWggdLKKGDPDTYAKYKekfpeiad 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901432 86 ------IHGTSFNSEALLALHTDVLFVA-------KGKGDAQSYNQAGIPTLemaFTDYP-SMEKSVTTTADVLGTD-QA 150
Cdd:cd01139 71 ipligsTYNGDFSVEKVLTLKPDLVILNiwakttaEESGILEKLEQAGIPVV---FVDFRqKPLKNTTPSMRLLGKAlGR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901432 151 RARAVAYNQFLTRTIADVRAKTATLAENqRPRVLHIQSLNPLKVDGRNTLIDTW---IALSGGRNVA-GEVDGNMKEVSP 226
Cdd:cd01139 148 EERAEEFIEFYQERIDRIRDRLAKINEP-KPKVFIELGAGGPEECCSTYGNGNWgelVDAAGGDNIAdGLIPGTSGELNA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901432 227 ERVLYWQPEVIILGAG----------------CGDIASSPYAAL-----FKELNAVKQGKVW-------RNPAGVFPwdr 278
Cdd:cd01139 227 EYVIAANPEIIIATGGnwakdpsgvslgpdgtTADAKESLLRALlkrpgWSSLQAVKNGRVYalwhqfyRSPYNFVA--- 303
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 851901432 279 ygtesalqLQWAASKLHPALFGGLDMVNVTRDFYRQF--FDYS 319
Cdd:cd01139 304 --------LEAFAKWLYPELFKDLDPEATLQEFHRQFlpVDYS 338
|
|
| HemV-2 |
cd01147 |
Metal binding protein HemV-2. These proteins are predicted to function as initial receptors ... |
33-279 |
1.15e-22 |
|
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: 95.09 E-value: 1.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901432 33 VPTQVQRIADSWFAHHSVLMTLGAGRQIVA-------------TVNHPQSQPWmfkinPSLNQalQIHGTSFNSEALLAL 99
Cdd:cd01147 1 VPKPVERVVAAGPGALRLLYALAAPDKIVGvddaeksdegrpyFLASPELKDL-----PVIGR--GGRGNTPNYEKIAAL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901432 100 HTDVLF----VAKGKGDAQSYNQAGIPTLEMAF-TDYPSMEKSVTTTADVLGTDqARARAVAynQFLTRTIADVRAKTAT 174
Cdd:cd01147 74 KPDVVIdvgsDDPTSIADDLQKKTGIPVVVLDGgDSLEDTPEQIRLLGKVLGKE-ERAEELI--SFIESILADVEERTKD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901432 175 LAENQRPRVlHIQSLNPLKVDGRNTLIDTW---IALSGGRNVAGEVDG-NMKEVSPERVLYWQPEVIIL---GAGCGDIA 247
Cdd:cd01147 151 IPDEEKPTV-YFGRIGTKGAAGLESGLAGSievFELAGGINVADGLGGgGLKEVSPEQILLWNPDVIFLdtgSFYLSLEG 229
|
250 260 270
....*....|....*....|....*....|..
gi 851901432 248 SSPYAALFKELNAVKQGKVWRNPAGVFPWDRY 279
Cdd:cd01147 230 YAKNRPFWQSLKAVKNGRVYLLPALPFNWYDT 261
|
|
| Peripla_BP_2 |
pfam01497 |
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ... |
48-271 |
6.70e-16 |
|
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: 75.87 E-value: 6.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901432 48 HSVLMTLGAGRQIVA---TVNHPQSQPWMFKInPSLNQALQIhgtsfNSEALLALHTDVLFVAKGKGDAQSYNQ--AGIP 122
Cdd:pfam01497 8 TEILYALGATDSIVGvdaYTRDPLKADAVAAI-VKVGAYGEI-----NVERLAALKPDLVILSTGYLTDEAEELlsLIIP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901432 123 TLEMAFTDYPSmekSVTTTADVLGTD-QARARAVAYNQFLTRTIADVRAKTATlaENQRPRVLHIQSLN-PLKVDGRNTL 200
Cdd:pfam01497 82 TVIFESSSTGE---SLKEQIKQLGELlGLEDEAEELVAEIDSALAAAKKAVPS--LTRKPVLVFGGADGgGYVVAGSNTY 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 851901432 201 IDTWIALSGGRNVAGEVDGNM-KEVSPERVLYWQPEVIILGAGCGD-------IASSPyaaLFKELNAVKQGKVWRNPA 271
Cdd:pfam01497 157 IGDLLRILGIENIAAELSGSEyAPISFEAILSSNPDVIIVSGRDSFtktgpefVAANP---LWAGLPAVKNGRVYTLPS 232
|
|
| ChuT |
COG4558 |
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism] ... |
1-268 |
1.48e-14 |
|
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443619 [Multi-domain] Cd Length: 285 Bit Score: 72.92 E-value: 1.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901432 1 MKTChtWLLCVWLAFPTLAtrqvvddAGHTVTVPTQvQRIADswfAHHSV---LMTLGAGRQIVA---TVNHPQsqpwmf 74
Cdd:COG4558 1 MKRL--ALALLLLALAALA-------AGASVAAAAA-ERIVS---LGGSVteiVYALGAGDRLVGvdtTSTYPA------ 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901432 75 kinpslnQALQI----HGTSFNSEALLALHTDVLFVAKGKGDAQSYNQ---AGIPTLEmaFTDYPSME---KSVTTTADV 144
Cdd:COG4558 62 -------AAKALpdvgYMRQLSAEGILSLKPTLVLASEGAGPPEVLDQlraAGVPVVV--VPAAPSLEgvlAKIRAVAAA 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901432 145 LGTdQARARAVAynQFLTRTIADVRAKTATLAEnqRPRVLHIQSL--NPLKVDGRNTLIDTWIALSGGRNVAGEVDGnMK 222
Cdd:COG4558 133 LGV-PEAGEALA--ARLEADLAALAARVAAIGK--PPRVLFLLSRggGRPMVAGRGTAADALIRLAGGVNAAAGFEG-YK 206
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 851901432 223 EVSPERVLYWQPEVIILGAGCGDIASSPyAALFK-----ELNAVKQGKVWR 268
Cdd:COG4558 207 PLSAEALIAAAPDVILVMTRGLESLGGV-DGLLAlpglaQTPAGKNKRIVA 256
|
|
| YvrC |
cd01143 |
Periplasmic binding protein YvrC. These proteins are predicted to function as initial ... |
50-239 |
2.74e-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: 70.38 E-value: 2.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901432 50 VLMTLGAGRQIVATV---NHPqsqpwmfkinPSLNQALQIHGTS-FNSEALLALHTDVLFVAKGKGDA--QSYNQAGIPT 123
Cdd:cd01143 16 ILFALGAGDKIVGVDtysNYP----------KEVRKKPKVGSYSnPNVEKIVALKPDLVIVSSSSLAEllEKLKDAGIPV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901432 124 LEM-AFTDYPSMEKSVTTTADVLGTDQARARAVayNQFLTRtIADVRAKTATLaenQRPRVLHIQSLNPLKVDGRNTLID 202
Cdd:cd01143 86 VVLpAASSLDEIYDQIELIGKITGAEEEAEKLV--KEMKQK-IDKVKDKGKTI---KKSKVYIEVSLGGPYTAGKNTFIN 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 851901432 203 TWIALSGGRNVAGEVDGnMKEVSPERVLYWQPEVIIL 239
Cdd:cd01143 160 ELIRLAGAKNIAADSGG-WPQVSPEEILKANPDVIIL 195
|
|
| BtuF |
cd01144 |
Cobalamin binding protein BtuF. These proteins have been shown to function as initial ... |
54-267 |
2.67e-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: 65.78 E-value: 2.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901432 54 LGAGRQIVATV---NHPqsqpwmfkinPSLNQALQIHGT-SFNSEALLALHTDvLFVAKGKGDAQSY----NQAGIPTLE 125
Cdd:cd01144 17 LGLGDQLVGVTdycDYP----------PEAKKLPRVGGFyQLDLERVLALKPD-LVIAWDDCNVCAVvdqlRAAGIPVLV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901432 126 MAFTDYPSMEKSVTTTADVLGTdqaRARAVAYNQFLTRTIADVRAKTATlaeNQRPRVLHIQSLNPLKVDGRNTLIDTwI 205
Cdd:cd01144 86 SEPQTLDDILADIRRLGTLAGR---PARAEELAEALRRRLAALRKQYAS---KPPPRVFYQEWIDPLMTAGGDWVPEL-I 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 851901432 206 ALSGGRNVAGEVDGNMKEVSPERVLYWQPEVIILgAGCGDIASSPYA---ALFKELNAVKQGKVW 267
Cdd:cd01144 159 ALAGGVNVFADAGERSPQVSWEDVLAANPDVIVL-SPCGFGFTPAILrkePAWQALPAVRNGRVY 222
|
|
| HutB |
cd01149 |
Hemin binding protein HutB. These proteins have been shown to function as initial receptors ... |
50-239 |
8.03e-12 |
|
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: 64.21 E-value: 8.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901432 50 VLMTLGAGRQIVA---TVNHPQsqpwmfkinpslnQALQI----HGTSFNSEALLALHTDVLFVAKGKGDAQSYNQ---A 119
Cdd:cd01149 14 IVYALGAGDRLVGvdsTSTYPE-------------AAAKLpdvgYMRQLSAEGVLSLKPTLVIASDEAGPPEALDQlraA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901432 120 GIPTLEMAFTDYP-SMEKSVTTTADVLG-TDQARARAVAYNQfltrTIADVRAKTAtlAENQRPRVLHIQSL--NPLKVD 195
Cdd:cd01149 81 GVPVVTVPSTPTLdGLLTKIRQVAQALGvPEKGEALAQEVRQ----RLAALRKTVA--AHKKPPRVLFLLSHggGAAMAA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 851901432 196 GRNTLIDTWIALSGGRNVAGEVDGnMKEVSPERVLYWQPEVIIL 239
Cdd:cd01149 155 GRNTAADAIIALAGAVNAAAGFRG-YKPLSAEALIAAQPDVILV 197
|
|
| TroA-like |
cd00636 |
Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function ... |
38-180 |
4.07e-09 |
|
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: 54.49 E-value: 4.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901432 38 QRIADSWFAHHSVLMTLGAGRQIVATVNHPQSQPWMFKINPSLNQALqiHGTSFNSEALLALHTDVLFVAK--GKGDAQS 115
Cdd:cd00636 1 KRVVALDPGATELLLALGGDDKPVGVADPSGYPPEAKALLEKVPDVG--HGYEPNLEKIAALKPDLIIANGsgLEAWLDK 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 851901432 116 YNQAGIPTLEMAFTDYPS---MEKSVTTTADVLGtdqARARAVAYNQFLTRTIADVRAKTATLAENQR 180
Cdd:cd00636 79 LSKIAIPVVVVDEASELSlenIKESIRLIGKALG---KEENAEELIAELDARLAELRAKLAKIPKKKV 143
|
|
| FhuD |
cd01146 |
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial ... |
57-287 |
5.26e-08 |
|
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: 53.06 E-value: 5.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901432 57 GRQIVATVNHPQSQPWMFKINPSLNQALQIHGTS-FNSEALLALHTDvLFVAKGKGDAQSYNQ-AGI-PTLEMAF-TDYP 132
Cdd:cd01146 21 GVKPVGVADTAGYKPWIPEPALPLEGVVDVGTRGqPNLEAIAALKPD-LILGSASRHDEIYDQlSQIaPTVLLDSsPWLA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901432 133 SMEKSVTTTADVLG-TDQARARAVAYNQFltrtIADVRAKtatLAENQRPRV--LHIQSLNPLKVDGRNTLIDTWIALSG 209
Cdd:cd01146 100 EWKENLRLIAKALGkEEEAEKLLAEYDQR----LAELRQK---LPDKGPKPVsvVRFSDAGSIRLYGPNSFAGSVLEDLG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901432 210 GRN---VAGEVDGNMKEVSPERVLYWQPEVIILGAGCGDIASSPYAA--LFKELNAVKQGKVWRNPAGVfpWDRYGTESA 284
Cdd:cd01146 173 LQNpwaQETTNDSGFATISLERLAKADADVLFVFTYEDEELAQALQAnpLWQNLPAVKNGRVYVVDDVW--WFFGGGLSA 250
|
...
gi 851901432 285 LQL 287
Cdd:cd01146 251 ARL 253
|
|
| TroA_a |
cd01148 |
Metal binding protein TroA_a. These proteins are predicted to function as initial receptors ... |
49-266 |
3.71e-07 |
|
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: 50.80 E-value: 3.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901432 49 SVLMTLGAGRQIVATvnhpqsQPWMFKINPSLNQALQ----IHGTSFNSEALLALHTDVLFVAK-------GKGDAQSYN 117
Cdd:cd01148 30 EMMLALGLQDRMVGT------AGIDNKDLPELKAKYDkvpeLAKKYPSKETVLAARPDLVFGGWsygfdkgGLGTPDSLA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901432 118 QAGIPTLEM-----AFTDYPSME---KSVTTTADVLGTdqaRARAVAYNQFLTRTIADVRAKTAtlAENQRPRVLHIQS- 188
Cdd:cd01148 104 ELGIKTYILpescgQRRGEATLDdvyNDIRNLGKIFDV---EDRADKLVADLKARLAEISAKVK--GDGKKVAVFVYDSg 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901432 189 -LNPLKVdGRNTLIDTWIALSGGRNVAGEVDGNMKEVSPERVLYWQPEVIILGaGCGDIASSPYAALF-------KELNA 260
Cdd:cd01148 179 eDKPFTS-GRGGIPNAIITAAGGRNVFADVDESWTTVSWETVIARNPDVIVII-DYGDQNAAEQKIKFlkenpalKNVPA 256
|
....*.
gi 851901432 261 VKQGKV 266
Cdd:cd01148 257 VKNNRF 262
|
|
| btuF |
PRK09534 |
corrinoid ABC transporter substrate-binding protein; Reviewed |
14-253 |
3.22e-06 |
|
corrinoid ABC transporter substrate-binding protein; Reviewed
Pssm-ID: 236552 [Multi-domain] Cd Length: 359 Bit Score: 48.37 E-value: 3.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901432 14 AFPTLATrqvvDDAGHTVTVPTQVQRIADSWFAHHSVLMTLGAGRQIVATVnhpQSQPWMFKINPSLNqALQIHGTSFNS 93
Cdd:PRK09534 41 SFPVTET----DATGTEITLDERPERVVTLNPSAAQTMWELGARDRVVGVT---QYASYLDGAEERTN-VSGGQPFGVNV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901432 94 EALLALHTD-VLFVAKGKGDA-QSYNQAGIPTLEMAF-TDYPSMEKSVTTTADVLGTDQArarAVAYNQFLTRTIADVRA 170
Cdd:PRK09534 113 EAVVGLDPDlVLAPNAVAGDTvTRLREAGITVFHFPAaTSIEDVAEKTATIGRLTGNCEA---AAETNAEMRDRVDAVED 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901432 171 KTATLaeNQRPRVLHiqSLNPLKVDGRNTLIDTWIALSGGRNVAGEVDGN-MKEVSPERVLYWQPEVIILGAGCGDIA-S 248
Cdd:PRK09534 190 RTADV--DDRPRVLY--PLGDGYTAGGNTFIGALIEAAGGHNVAADATTDgYPQLSEEVIVQQDPDVIVVATASALVAeT 265
|
....*
gi 851901432 249 SPYAA 253
Cdd:PRK09534 266 EPYAS 270
|
|
| FeuA |
cd01138 |
Periplasmic binding protein FeuA. These proteins have predicted to function as initial ... |
30-275 |
1.57e-03 |
|
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: 39.62 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901432 30 TVTVPTQVQRIADSWFAHHSVLMTlgaGRQIVATVNHPQSQPWMFKinPSLNQALQIhGTSFNSEALLALHTDVLFV-AK 108
Cdd:cd01138 2 EVEIPAKPKRIVALSGETEGLALL---GIKPVGAASIGGKNPYYKK--KTLAKVVGI-VDEPNLEKVLELKPDLIIVsSK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901432 109 GKGDAQSYNQAGiPTLEMAFTDYpSMEKSVTTTADVLGT-DQARARAVAYNQFLTR---TIADVRAKTATLAenQRPRVL 184
Cdd:cd01138 76 QEENYEKLSKIA-PTVPVSYNSS-DWEEQLKEIGKLLNKeDEAEKWLADYKQKAKEakeKIKKKLGNDKSVA--VLRGRK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901432 185 HIQSLNPLKVdGRNTLIDTWIALSGGRNVAGEVDG-NMKEVSPERVLYWQPEVIILGAGCGDIASSPYAAL--FKELNAV 261
Cdd:cd01138 152 QIYVFGEDGR-GGGPILYADLGLKAPEKVKEIEDKpGYAAISLEVLPEFDADYIFLLFFTGPEAKADFESLpiWKNLPAV 230
|
250
....*....|....
gi 851901432 262 KQGKVWRNPAGVFP 275
Cdd:cd01138 231 KNNHVYIVDAWVFY 244
|
|
| PRK03379 |
PRK03379 |
vitamin B12-transporter protein BtuF; Provisional |
92-248 |
1.94e-03 |
|
vitamin B12-transporter protein BtuF; Provisional
Pssm-ID: 179575 [Multi-domain] Cd Length: 260 Bit Score: 39.28 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901432 92 NSEALLALHTDVLFVAKGkGDAQ-SYNQA---GIPTLemaFTDYPSMEKsVTTTADVLGT-----DQARARAvaynQFLT 162
Cdd:PRK03379 64 NLERIVALKPDLVLAWRG-GNAErQVDQLaslGIKVM---WVDATSIEQ-IANALRQLAPwspqpEKAEQAA----QSLL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851901432 163 RTIADVRAKTATLAenqrPRVLHIQ-SLNPLKVDGRNTLIDTWIALSGGRNVAGEVDGNMKEVSPERVLYWQPEVIILGA 241
Cdd:PRK03379 135 QQYAALKAQYADKP----KKRVFLQfGTNPLFTSGKHSIQSQVLSLCGGENIFADSRVPWPQVSREQVLARKPQAIVITG 210
|
....*..
gi 851901432 242 GCGDIAS 248
Cdd:PRK03379 211 GPDQIPK 217
|
|
| |
