|
Name |
Accession |
Description |
Interval |
E-value |
| FhuD |
cd01146 |
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial ... |
60-320 |
1.72e-55 |
|
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: 181.72 E-value: 1.72e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086656 60 KKPKRVATIAWANHDVALALGVVPVGFSAANygikdnktGILPWTKEKLDELgaKSPNVYQDTDGLDYEAIADSKPDVIL 139
Cdd:cd01146 1 AKPQRIVALDWGALETLLALGVKPVGVADTA--------GYKPWIPEPALPL--EGVVDVGTRGQPNLEAIAALKPDLIL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086656 140 AAYSGITkEEYNKLSEIAPVVAYKDQPWVTSWRDQVKYDSMGMGMKKEGEQLVKDTEKLIADTAAKYPDIKGKKAAFgmF 219
Cdd:cd01146 71 GSASRHD-EIYDQLSQIAPTVLLDSSPWLAEWKENLRLIAKALGKEEEAEKLLAEYDQRLAELRQKLPDKGPKPVSV--V 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086656 220 NTTDLSKFYIYTPSDPRGEMLEEVGMEYPEglkKQVKDNKSFYLELSAENADvLNDTELLVV--YGNSTTLKTLQKDPIL 297
Cdd:cd01146 148 RFSDAGSIRLYGPNSFAGSVLEDLGLQNPW---AQETTNDSGFATISLERLA-KADADVLFVftYEDEELAQALQANPLW 223
|
250 260
....*....|....*....|....*...
gi 1752086656 298 GEVPAIKKGNVVVIEDNT-----PLAAA 320
Cdd:cd01146 224 QNLPAVKNGRVYVVDDVWwffggGLSAA 251
|
|
| FecB |
COG4594 |
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and ... |
1-319 |
6.44e-48 |
|
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443650 [Multi-domain] Cd Length: 316 Bit Score: 163.94 E-value: 6.44e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086656 1 MKKItkvMLFAFMSVLVLALAACSGDSSKDKTSSDKKTesagsgyPIKIQHAFGTTIIDKKPKRVATIAWANHDVALALG 80
Cdd:COG4594 1 MKKL---LLLLILLLALLLLAACGSSSSDSSSSEAAAG-------ARTVKHAMGETTIPGTPKRVVVLEWSFADALLALG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086656 81 VVPVGFSAANygikdNKTGILPWTKEKLDE---LGA-KSPNVyqdtdgldyEAIADSKPDVILAAYS---GItkeeYNKL 153
Cdd:COG4594 71 VTPVGIADDN-----DYDRWVPYLRDLIKGvtsVGTrSQPNL---------EAIAALKPDLIIADKSrheAI----YDQL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086656 154 SEIAPVVAYKDQPwvTSWRDQVKYDSM---GMGMKKEGEQLVKDTEKLIADTAAKYPDI-KGKKAAFGMFNTtdlSKFYI 229
Cdd:COG4594 133 SKIAPTVLFKSRN--GDYQENLESFKTiakALGKEEEAEAVLADHDQRIAEAKAKLAAAdKGKKVAVGQFRA---DGLRL 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086656 230 YTPSDPRGEMLEEVGMEYPEglkKQVKDNKSFYLELSAE-----NADVLndteLLVVYGNSTTLKTLQKDPILGEVPAIK 304
Cdd:COG4594 208 YTPNSFAGSVLAALGFENPP---KQSKDNGYGYSEVSLEqlpalDPDVL----FIATYDDPSILKEWKNNPLWKNLKAVK 280
|
330 340
....*....|....*....|.
gi 1752086656 305 KGNVVVIEDNT------PLAA 319
Cdd:COG4594 281 NGRVYEVDGDLwtrgrgPLAA 301
|
|
| Peripla_BP_2 |
pfam01497 |
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ... |
66-311 |
1.62e-21 |
|
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: 91.66 E-value: 1.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086656 66 ATIAWANHDVALALGVVP--VGFSAANYGikdnktgilPWTKEKLDELgaksPNVYQDTDgLDYEAIADSKPDVILAAYS 143
Cdd:pfam01497 1 AALSPAYTEILYALGATDsiVGVDAYTRD---------PLKADAVAAI----VKVGAYGE-INVERLAALKPDLVILSTG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086656 144 GITKEEYNKLSEIAPVVAYKDQPWVTSWRDQVKYDSMGMGMKKEGEQLVKDTEKLIADTAAKYPDIKGKKAAfgMFNTTD 223
Cdd:pfam01497 67 YLTDEAEELLSLIIPTVIFESSSTGESLKEQIKQLGELLGLEDEAEELVAEIDSALAAAKKAVPSLTRKPVL--VFGGAD 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086656 224 LSKFYIYTPSDPRGEMLEEVGMEYPeglkkQVKDNKSFYLELSAENadVLN-DTELLVVYGNSTTLKT----LQKDPILG 298
Cdd:pfam01497 145 GGGYVVAGSNTYIGDLLRILGIENI-----AAELSGSEYAPISFEA--ILSsNPDVIIVSGRDSFTKTgpefVAANPLWA 217
|
250
....*....|...
gi 1752086656 299 EVPAIKKGNVVVI 311
Cdd:pfam01497 218 GLPAVKNGRVYTL 230
|
|
| PRK10957 |
PRK10957 |
iron-enterobactin transporter periplasmic binding protein; Provisional |
9-308 |
4.52e-19 |
|
iron-enterobactin transporter periplasmic binding protein; Provisional
Pssm-ID: 236806 [Multi-domain] Cd Length: 317 Bit Score: 86.18 E-value: 4.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086656 9 LFAFMSVLVLALAACSGDSSkdktssdkktESAGSGYPIKIQHAFGTTIIDKKPKRVATIAWANHDVALALGVvPVGFSA 88
Cdd:PRK10957 1 PLYRLALLLLGLLLSGIAAA----------QASAAGWPRTVTDSRGSVTLESKPQRIVSTSVTLTGTLLAIDA-PVIASG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086656 89 A---NYGIKDNKTGILPWTKEKlDELGAKspNVYQDtdGLDYEAIADSKPDVILAAYSG--ITKEEYNKLSEIAP--VVA 161
Cdd:PRK10957 70 AttpNTRVADDQGFFRQWSDVA-KERGVE--VLYIG--EPDAEAVAAQMPDLIVISATGgdSALALYDQLSAIAPtlVID 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086656 162 YKDQpwvtSWRDQVKYDSMGMGMKKEGEQLVKDTEKLIADTAAKYPDIKGKKAAFGmFNTTDLSkFYIYTPSDPRGEMLE 241
Cdd:PRK10957 145 YDDK----SWQELATQLGEATGLEKQAAAVIAQFDAQLAEVKAKITLPPQPVSALV-YNGAGHS-ANLWTPESAQGQLLE 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1752086656 242 EVGMEY---PEGLKKQVKDNK-SFYLELSAEN-ADVLNDTELLVVYGNSTTLKTLQKDPILGEVPAIKKGNV 308
Cdd:PRK10957 219 QLGFTLaelPAGLQASTSQGKrHDIIQLGGENlAAGLNGETLFLFAGDDKDADAFLADPLLANLPAVQNKQV 290
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| FhuD |
cd01146 |
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial ... |
60-320 |
1.72e-55 |
|
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: 181.72 E-value: 1.72e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086656 60 KKPKRVATIAWANHDVALALGVVPVGFSAANygikdnktGILPWTKEKLDELgaKSPNVYQDTDGLDYEAIADSKPDVIL 139
Cdd:cd01146 1 AKPQRIVALDWGALETLLALGVKPVGVADTA--------GYKPWIPEPALPL--EGVVDVGTRGQPNLEAIAALKPDLIL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086656 140 AAYSGITkEEYNKLSEIAPVVAYKDQPWVTSWRDQVKYDSMGMGMKKEGEQLVKDTEKLIADTAAKYPDIKGKKAAFgmF 219
Cdd:cd01146 71 GSASRHD-EIYDQLSQIAPTVLLDSSPWLAEWKENLRLIAKALGKEEEAEKLLAEYDQRLAELRQKLPDKGPKPVSV--V 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086656 220 NTTDLSKFYIYTPSDPRGEMLEEVGMEYPEglkKQVKDNKSFYLELSAENADvLNDTELLVV--YGNSTTLKTLQKDPIL 297
Cdd:cd01146 148 RFSDAGSIRLYGPNSFAGSVLEDLGLQNPW---AQETTNDSGFATISLERLA-KADADVLFVftYEDEELAQALQANPLW 223
|
250 260
....*....|....*....|....*...
gi 1752086656 298 GEVPAIKKGNVVVIEDNT-----PLAAA 320
Cdd:cd01146 224 QNLPAVKNGRVYVVDDVWwffggGLSAA 251
|
|
| FecB |
COG4594 |
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and ... |
1-319 |
6.44e-48 |
|
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443650 [Multi-domain] Cd Length: 316 Bit Score: 163.94 E-value: 6.44e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086656 1 MKKItkvMLFAFMSVLVLALAACSGDSSKDKTSSDKKTesagsgyPIKIQHAFGTTIIDKKPKRVATIAWANHDVALALG 80
Cdd:COG4594 1 MKKL---LLLLILLLALLLLAACGSSSSDSSSSEAAAG-------ARTVKHAMGETTIPGTPKRVVVLEWSFADALLALG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086656 81 VVPVGFSAANygikdNKTGILPWTKEKLDE---LGA-KSPNVyqdtdgldyEAIADSKPDVILAAYS---GItkeeYNKL 153
Cdd:COG4594 71 VTPVGIADDN-----DYDRWVPYLRDLIKGvtsVGTrSQPNL---------EAIAALKPDLIIADKSrheAI----YDQL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086656 154 SEIAPVVAYKDQPwvTSWRDQVKYDSM---GMGMKKEGEQLVKDTEKLIADTAAKYPDI-KGKKAAFGMFNTtdlSKFYI 229
Cdd:COG4594 133 SKIAPTVLFKSRN--GDYQENLESFKTiakALGKEEEAEAVLADHDQRIAEAKAKLAAAdKGKKVAVGQFRA---DGLRL 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086656 230 YTPSDPRGEMLEEVGMEYPEglkKQVKDNKSFYLELSAE-----NADVLndteLLVVYGNSTTLKTLQKDPILGEVPAIK 304
Cdd:COG4594 208 YTPNSFAGSVLAALGFENPP---KQSKDNGYGYSEVSLEqlpalDPDVL----FIATYDDPSILKEWKNNPLWKNLKAVK 280
|
330 340
....*....|....*....|.
gi 1752086656 305 KGNVVVIEDNT------PLAA 319
Cdd:COG4594 281 NGRVYEVDGDLwtrgrgPLAA 301
|
|
| FepB |
COG0614 |
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ... |
64-329 |
1.02e-36 |
|
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 440379 [Multi-domain] Cd Length: 264 Bit Score: 133.20 E-value: 1.02e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086656 64 RVATIAWANHDVALALGVVP--VGFSAANYGIkdnktgiLPWTK-EKLDELGakspnvyqDTDGLDYEAIADSKPDVILA 140
Cdd:COG0614 2 RIVSLSPSATELLLALGAGDrlVGVSDWGYCD-------YPELElKDLPVVG--------GTGEPNLEAILALKPDLVLA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086656 141 AYSGITKEEYNKLSEI-APVVAYkDQPWVTSWRDQVKYdsMG--MGMKKEGEQLVKDTEKLIADTAAKYPDIKGKKAAFG 217
Cdd:COG0614 67 SSSGNDEEDYEQLEKIgIPVVVL-DPRSLEDLYESIRL--LGelLGREERAEALIAEYEARLAAVRARLAGAEERPTVLY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086656 218 MFNTTDlsKFYIYTPSDPRGEMLEEVGMEYpeglkkQVKDNKSFYLELSAENADVLnDTELLVVYGNS-------TTLKT 290
Cdd:COG0614 144 EIWSGD--PLYTAGGGSFIGELLELAGGRN------VAADLGGGYPEVSLEQVLAL-DPDVIILSGGGydaetaeEALEA 214
|
250 260 270
....*....|....*....|....*....|....*....
gi 1752086656 291 LQKDPILGEVPAIKKGNVVVIEDNtplaAAGTPSPLSIK 329
Cdd:COG0614 215 LLADPGWQSLPAVKNGRVYVVPGD----LLSRPGPRLLL 249
|
|
| FepB |
COG4592 |
ABC-type Fe2+-enterobactin transport system, periplasmic component [Inorganic ion transport ... |
11-309 |
1.51e-30 |
|
ABC-type Fe2+-enterobactin transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443649 [Multi-domain] Cd Length: 330 Bit Score: 118.51 E-value: 1.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086656 11 AFMSVLVLALAACSGDSSKDKTSSDkkteSAGSGYPIKIQHAFGTTIIDKKPKRVA----TIAwanhDVALALG--VVPV 84
Cdd:COG4592 10 AALLAAALLLAGCSSADSTASGTST----AAAGGWPRTVTTEKGTVTLPAKPQRIVstsvTLT----GSLLAIDapVVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086656 85 GFSAANYGIKDNktGILPWTKEKLDELGAKSpnVYQDtDGLDYEAIADSKPDVILAAYSGI--TKEEYNKLSEIAP--VV 160
Cdd:COG4592 82 GATTPNNVTDDQ--GFFRQWADVAKERGVKR--LYIG-LEPNAEAIAAAAPDLIIGSATGGdsALDLYDQLSAIAPtlVV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086656 161 AYKDqpwvTSWRDQVKYDSMGMGMKKEGEQLVKDTEKLIADTAAKypdIK---GKKAAFGMFNTtdlSKFYIYTPSDPRG 237
Cdd:COG4592 157 NYDD----KSWQELATQLGEATGHEAQADAVIAAFDARVAEVKAA---ITlppQPVSALVYNED---GGANLWTPESAQG 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1752086656 238 EMLEEVGMEY---PEGLKKQVKDNKSF-YLELSAEN-ADVLNDTELLVVYGNSTTLKTLQKDPILGEVPAIKKGNVV 309
Cdd:COG4592 227 QLLQALGFTLaplPAELATSTSQGKRGdIVQLSGENlAAALTGPTLFLFAADDKDVDALKADPLLAHLPAVQAGRVY 303
|
|
| Peripla_BP_2 |
pfam01497 |
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ... |
66-311 |
1.62e-21 |
|
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: 91.66 E-value: 1.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086656 66 ATIAWANHDVALALGVVP--VGFSAANYGikdnktgilPWTKEKLDELgaksPNVYQDTDgLDYEAIADSKPDVILAAYS 143
Cdd:pfam01497 1 AALSPAYTEILYALGATDsiVGVDAYTRD---------PLKADAVAAI----VKVGAYGE-INVERLAALKPDLVILSTG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086656 144 GITKEEYNKLSEIAPVVAYKDQPWVTSWRDQVKYDSMGMGMKKEGEQLVKDTEKLIADTAAKYPDIKGKKAAfgMFNTTD 223
Cdd:pfam01497 67 YLTDEAEELLSLIIPTVIFESSSTGESLKEQIKQLGELLGLEDEAEELVAEIDSALAAAKKAVPSLTRKPVL--VFGGAD 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086656 224 LSKFYIYTPSDPRGEMLEEVGMEYPeglkkQVKDNKSFYLELSAENadVLN-DTELLVVYGNSTTLKT----LQKDPILG 298
Cdd:pfam01497 145 GGGYVVAGSNTYIGDLLRILGIENI-----AAELSGSEYAPISFEA--ILSsNPDVIIVSGRDSFTKTgpefVAANPLWA 217
|
250
....*....|...
gi 1752086656 299 EVPAIKKGNVVVI 311
Cdd:pfam01497 218 GLPAVKNGRVYTL 230
|
|
| CeuA |
COG4607 |
ABC-type enterochelin transport system, periplasmic component [Inorganic ion transport and ... |
1-227 |
9.37e-21 |
|
ABC-type enterochelin transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443657 [Multi-domain] Cd Length: 310 Bit Score: 91.01 E-value: 9.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086656 1 MKKITkvmLFAFMSVLVLALAACSGDSSKDKTSSDKKTesagsgypIKIQHAFGTTIIDKKPKRVATIAWANHDVALALG 80
Cdd:COG4607 1 MKKTL---LAALALAAALALAACGSSSAAAASAAAAET--------VTVEHALGTVEVPKNPKRVVVFDNGALDTLDALG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086656 81 VVPVGFSAANYgikdnktgilpwtkekLDELGAKSPNVYQDTDGL---DYEAIADSKPDVILAaySGITKEEYNKLSEIA 157
Cdd:COG4607 70 VEVAGVPKGLL----------------PDYLSKYADDKYANVGTLfepDLEAIAALKPDLIII--GGRSAKKYDELSKIA 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1752086656 158 PVV--AYKDQPWVTSWRDQVkyDSMG--MGMKKEGEQLVKDTEKLIADTAAKYPDikGKKAAFGMFNTTDLSKF 227
Cdd:COG4607 132 PTIdlTVDGEDYLESLKRNT--ETLGeiFGKEDEAEELVADLDAKIAALKAAAAG--KGTALIVLTNGGKISAY 201
|
|
| PRK10957 |
PRK10957 |
iron-enterobactin transporter periplasmic binding protein; Provisional |
9-308 |
4.52e-19 |
|
iron-enterobactin transporter periplasmic binding protein; Provisional
Pssm-ID: 236806 [Multi-domain] Cd Length: 317 Bit Score: 86.18 E-value: 4.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086656 9 LFAFMSVLVLALAACSGDSSkdktssdkktESAGSGYPIKIQHAFGTTIIDKKPKRVATIAWANHDVALALGVvPVGFSA 88
Cdd:PRK10957 1 PLYRLALLLLGLLLSGIAAA----------QASAAGWPRTVTDSRGSVTLESKPQRIVSTSVTLTGTLLAIDA-PVIASG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086656 89 A---NYGIKDNKTGILPWTKEKlDELGAKspNVYQDtdGLDYEAIADSKPDVILAAYSG--ITKEEYNKLSEIAP--VVA 161
Cdd:PRK10957 70 AttpNTRVADDQGFFRQWSDVA-KERGVE--VLYIG--EPDAEAVAAQMPDLIVISATGgdSALALYDQLSAIAPtlVID 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086656 162 YKDQpwvtSWRDQVKYDSMGMGMKKEGEQLVKDTEKLIADTAAKYPDIKGKKAAFGmFNTTDLSkFYIYTPSDPRGEMLE 241
Cdd:PRK10957 145 YDDK----SWQELATQLGEATGLEKQAAAVIAQFDAQLAEVKAKITLPPQPVSALV-YNGAGHS-ANLWTPESAQGQLLE 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1752086656 242 EVGMEY---PEGLKKQVKDNK-SFYLELSAEN-ADVLNDTELLVVYGNSTTLKTLQKDPILGEVPAIKKGNV 308
Cdd:PRK10957 219 QLGFTLaelPAGLQASTSQGKrHDIIQLGGENlAAGLNGETLFLFAGDDKDADAFLADPLLANLPAVQNKQV 290
|
|
| FeuA |
cd01138 |
Periplasmic binding protein FeuA. These proteins have predicted to function as initial ... |
54-315 |
1.19e-17 |
|
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: 81.23 E-value: 1.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086656 54 GTTIIDKKPKRVATIAWANHDVALaLGVVPVGfsAANYGIKdnktgiLPWTKEKLDelgaksPNVYQDTDGLDYEAIADS 133
Cdd:cd01138 1 GEVEIPAKPKRIVALSGETEGLAL-LGIKPVG--AASIGGK------NPYYKKKTL------AKVVGIVDEPNLEKVLEL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086656 134 KPDVILAaySGITKEEYNKLSEIAPVVAYKDQPwvTSWRDQVKYDSMGMGMKKEGEQLVKDTEKLIADTAAKypdIKGKK 213
Cdd:cd01138 66 KPDLIIV--SSKQEENYEKLSKIAPTVPVSYNS--SDWEEQLKEIGKLLNKEDEAEKWLADYKQKAKEAKEK---IKKKL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086656 214 AAFGMFNTTDLSK-FYIYTPSDPRGEML--EEVGMEYPEGLKKQvkDNKSFYLELSAEN-ADVLNDTELLVVYGNSTTLK 289
Cdd:cd01138 139 GNDKSVAVLRGRKqIYVFGEDGRGGGPIlyADLGLKAPEKVKEI--EDKPGYAAISLEVlPEFDADYIFLLFFTGPEAKA 216
|
250 260
....*....|....*....|....*.
gi 1752086656 290 TLQKDPILGEVPAIKKGNVVVIEDNT 315
Cdd:cd01138 217 DFESLPIWKNLPAVKNNHVYIVDAWV 242
|
|
| fecB |
PRK11411 |
iron-dicitrate transporter substrate-binding subunit; Provisional |
40-315 |
1.61e-17 |
|
iron-dicitrate transporter substrate-binding subunit; Provisional
Pssm-ID: 183123 [Multi-domain] Cd Length: 303 Bit Score: 81.64 E-value: 1.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086656 40 SAGSGYPIKIQHAFGTTIIDKKPKRVATIAWANHDVALALGVVPVGFSAANygikdNKTGILPWTKEKLDE---LGAKS- 115
Cdd:PRK11411 17 GSSHAFAVTVQDEQGTFTLEKTPQRIVVLELSFVDALAAVGVSPVGVADDN-----DAKRILPEVRAHLKPwqsVGTRSq 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086656 116 PNVyqdtdgldyEAIADSKPDVILA---AYSGItkeeYNKLSEIAPVVAYKDqpwvtswRDQVKYDSMGMGMKKeGEQLV 192
Cdd:PRK11411 92 PSL---------EAIAALKPDLIIAdssRHAGV----YIALQKIAPTLLLKS-------RNETYQENLQSAAII-GEVLG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086656 193 KDTE---------KLIADTAAKYPdiKGKKAAFGmfnTTDLSKFYIYTPSDPRGEMLEEVGMEYPEglkkqVKDNKSFYL 263
Cdd:PRK11411 151 KKREmqarieqhkERMAQFASQLP--KGTRVAFG---TSREQQFNLHSPESYTGSVLAALGLNVPK-----APMNGAAMP 220
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1752086656 264 ELSAENADVLNDTELLVV-YGNSTTLKTLQKDPILGEVPAIKKGNVVVIEDNT 315
Cdd:PRK11411 221 SISLEQLLALNPDWLLVAhYRQESIVKRWQQDPLWQMLTAAKKQQVASVDSNT 273
|
|
| TroA-like |
cd00636 |
Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function ... |
63-216 |
2.65e-11 |
|
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: 61.04 E-value: 2.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086656 63 KRVATIAWANHDVALALG--VVPVGFSAANYGIKDNKtgilpwtkeKLDELGAKSPNVYQdtdgLDYEAIADSKPDVILA 140
Cdd:cd00636 1 KRVVALDPGATELLLALGgdDKPVGVADPSGYPPEAK---------ALLEKVPDVGHGYE----PNLEKIAALKPDLIIA 67
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1752086656 141 AYSGItKEEYNKLSEIA---PVVAYKDQPWVTSWRDQVKYDSMGMGMKKEGEQLVKDTEKLIADTAAKYPDIKGKKAAF 216
Cdd:cd00636 68 NGSGL-EAWLDKLSKIAipvVVVDEASELSLENIKESIRLIGKALGKEENAEELIAELDARLAELRAKLAKIPKKKVSL 145
|
|
| FatB |
cd01140 |
Siderophore binding protein FatB. These proteins have been shown to function as ABC-type ... |
51-321 |
4.20e-11 |
|
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: 62.66 E-value: 4.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086656 51 HAFGTTIIDKKPKRVATIAWANHDVALALGVVPVGFSaanygikdnKTGILPWTKEKLdelgakSPNVYQDTDGL---DY 127
Cdd:cd01140 1 HALGETKVPKNPEKVVVFDVGALDTLDALGVKVVGVP---------KSSTLPEYLKKY------KDDKYANVGTLfepDL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086656 128 EAIADSKPDVILAaySGITKEEYNKLSEIAPVVAY---KDQPWvTSWRDQVkyDSMG--MGMKKEGEQLVKDTEKLIADT 202
Cdd:cd01140 66 EAIAALKPDLIII--GGRLAEKYDELKKIAPTIDLgadLKNYL-ESVKQNI--ETLGkiFGKEEEAKELVAEIDASIAEA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086656 203 AAKYpdiKGKKAAfgMFNTTDLSKFYIYTPSDPRGEMLEEVGMEyPEGlkkQVKDNKSFYLELSAENADVLNDTELLVVY 282
Cdd:cd01140 141 KSAA---KGKKKA--LVVLVNGGKLSAFGPGSRFGWLHDLLGFE-PAD---ENIKASSHGQPVSFEYILEANPDWLFVID 211
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1752086656 283 ------GNSTTLKTLQKDPILGEVPAIKKGNVVVIEDNTPLAAAG 321
Cdd:cd01140 212 rgaaigAEGSSAKEVLDNDLVKNTTAWKNGKVIYLDPDLWYLSGG 256
|
|
| TroA_a |
cd01148 |
Metal binding protein TroA_a. These proteins are predicted to function as initial receptors ... |
45-328 |
4.09e-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: 4.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086656 45 YPIKIQHAFGTTIIDKKPKRVATIAWANHDVALALGVVP--VGFSaanyGIKDNKTGILPWTKEKLDELGAKSPNVyqdt 122
Cdd:cd01148 1 YPLTVENCGRSVTFDKAPQRVVSNDQNTTEMMLALGLQDrmVGTA----GIDNKDLPELKAKYDKVPELAKKYPSK---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086656 123 dgldyEAIADSKPDVILAAYS-GITKEEYNKLSEIAP--VVAY----------KDQPWVTSWRDQVKYDSMgMGMKKEGE 189
Cdd:cd01148 73 -----ETVLAARPDLVFGGWSyGFDKGGLGTPDSLAElgIKTYilpescgqrrGEATLDDVYNDIRNLGKI-FDVEDRAD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086656 190 QLVKDTEKLIADTAAKYPDIKGKKAAFGmFNTTDLSKFYIYTPSDPrGEMLEEVGMEypeglkKQVKDNKSFYLELSAEN 269
Cdd:cd01148 147 KLVADLKARLAEISAKVKGDGKKVAVFV-YDSGEDKPFTSGRGGIP-NAIITAAGGR------NVFADVDESWTTVSWET 218
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1752086656 270 ADVLNDTELLVV-YGNSTT----LKTLQKDPILGEVPAIKKGNVVVIedntPLAAAgTPSPLSI 328
Cdd:cd01148 219 VIARNPDVIVIIdYGDQNAaeqkIKFLKENPALKNVPAVKNNRFIVL----PLAEA-TPGIRNV 277
|
|
| TroA_d |
cd01141 |
Periplasmic binding protein TroA_d. These proteins are predicted to function as initial ... |
57-247 |
3.41e-06 |
|
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: 47.03 E-value: 3.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086656 57 IIDKKPKRVATIAWANHDVALALGVVP--VGFSAANYGIKDNKtgilpwtkekldeLGAKSPNVYQDTDGLDYEAIADSK 134
Cdd:cd01141 3 TIKVPPKRIVVLSPTHVDLLLALDKADkiVGVSASAYDLNTPA-------------VKERIDIQVGPTGSLNVELIVALK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086656 135 PDVILAAYSGITKEEYNKLSEIAPVVAYKdQPWVTSWR--DQVKYDSMGMGMKKEgeqlvKDTEKLIADTAAKYPDIKGK 212
Cdd:cd01141 70 PDLVILYGGFQAQTILDKLEQLGIPVLYV-NEYPSPLGraEWIKFAAAFYGVGKE-----DKADEAFAQIAGRYRDLAKK 143
|
170 180 190
....*....|....*....|....*....|....*....
gi 1752086656 213 KAAFG----MFNTTDLSKFYIYTPSDPRGEMLEEVGMEY 247
Cdd:cd01141 144 VSNLNkptvAIGKPVKGLWYMPGGNSYVAKMLRDAGGRY 182
|
|
| TroA_e |
cd01142 |
Periplasmic binding protein TroA_e. These proteins are predicted to function as initial ... |
54-313 |
1.05e-05 |
|
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: 46.58 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086656 54 GTTI-IDKKPKRVATIAWANHDVALALGVVP--VGFSAANYGIKDNKTgILPWTKEKLDELGAKSPNVyqdtdgldyEAI 130
Cdd:cd01142 15 GRKVtIPDEVKRIAALWGAGNAVVAALGGGKliVATTSTVQQEPWLYR-LAPSLENVATGGTGNDVNI---------EEL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086656 131 ADSKPDVILAaYSGITKEEYNKLSEIAPVVAYKdqpWVTSWRDQVKYDSMG--MGMKKEGEQLVK---DTEKLIADTAAK 205
Cdd:cd01142 85 LALKPDVVIV-WSTDGKEAGKAVLRLLNALSLR---DAELEEVKLTIALLGelLGRQEKAEALVAyfdDNLAYVAARTKK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086656 206 YPDIKGKKAAFGMFN--TTDLSKFYiytpsdpRGEMLEEVGMEYPEGlKKQVKDNKSFYLE-LSAENADVlndtellVVY 282
Cdd:cd01142 161 LPDSERPRVYYAGPDplTTDGTGSI-------TNSWIDLAGGINVAS-EATKKGSGEVSLEqLLKWNPDV-------IIV 225
|
250 260 270
....*....|....*....|....*....|.
gi 1752086656 283 GNSTTLKTLQKDPILGEVPAIKKGNVVVIED 313
Cdd:cd01142 226 GNADTKAAILADPRWQNLRAVKNGRVYVNPE 256
|
|
| YvrC |
cd01143 |
Periplasmic binding protein YvrC. These proteins are predicted to function as initial ... |
113-216 |
2.37e-04 |
|
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: 41.49 E-value: 2.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086656 113 AKSPNVYQDTDGLDYEAIADSKPDVILAAYSGItKEEYNKLSEIAPVVAYKDQPwvtSWRDQVkYDSMGM-----GMKKE 187
Cdd:cd01143 39 VRKKPKVGSYSNPNVEKIVALKPDLVIVSSSSL-AELLEKLKDAGIPVVVLPAA---SSLDEI-YDQIELigkitGAEEE 113
|
90 100
....*....|....*....|....*....
gi 1752086656 188 GEQLVKDTEKLIADTAAKYPDIKGKKAAF 216
Cdd:cd01143 114 AEKLVKEMKQKIDKVKDKGKTIKKSKVYI 142
|
|
| HemV-2 |
cd01147 |
Metal binding protein HemV-2. These proteins are predicted to function as initial receptors ... |
84-308 |
6.31e-04 |
|
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: 40.78 E-value: 6.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086656 84 VGFSAANYGIKDNK-TGILPWTKEkLDELGAKSPnvyqdTDGLDYEAIADSKPDVILAAYSGITKEEYNKLSEIA--PVV 160
Cdd:cd01147 29 VGVDDAEKSDEGRPyFLASPELKD-LPVIGRGGR-----GNTPNYEKIAALKPDVVIDVGSDDPTSIADDLQKKTgiPVV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752086656 161 AYKDQPWVTSWRDQVKYdsMG--MGMKKEGEQLV---KDTEKLIADTAAKYPDIKGKKAAFGMFNTTdlSKFYIYTPSDP 235
Cdd:cd01147 103 VLDGGDSLEDTPEQIRL--LGkvLGKEERAEELIsfiESILADVEERTKDIPDEEKPTVYFGRIGTK--GAAGLESGLAG 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1752086656 236 RGEMLEEVgmeypeGLKKQVKD-NKSFYLELSAENADVLNDTELLVVYGNS--TTLKTLQKDPILGEVPAIKKGNV 308
Cdd:cd01147 179 SIEVFELA------GGINVADGlGGGGLKEVSPEQILLWNPDVIFLDTGSFylSLEGYAKNRPFWQSLKAVKNGRV 248
|
|
| |
