|
Name |
Accession |
Description |
Interval |
E-value |
| FecB |
COG4594 |
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and ... |
1-326 |
7.04e-140 |
|
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443650 [Multi-domain] Cd Length: 316 Bit Score: 398.14 E-value: 7.04e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613366465 1 MRglKTFSILGLIVALFLVAACGNTDNSSKKESSTKDTISVKDENGTVKVPKDAKRIVVLEYSFADALAALDVKPVGIAD 80
Cdd:COG4594 1 MK--KLLLLLILLLALLLLAACGSSSSDSSSSEAAAGARTVKHAMGETTIPGTPKRVVVLEWSFADALLALGVTPVGIAD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613366465 81 DGKKKRIIKPVREKIGDYTSVGTRKQPNLEEISKLKPDLIIADSSRHKGINKELNKIAPTLSLKSFDGDYKQNIDAFKTI 160
Cdd:COG4594 79 DNDYDRWVPYLRDLIKGVTSVGTRSQPNLEAIAALKPDLIIADKSRHEAIYDQLSKIAPTVLFKSRNGDYQENLESFKTI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613366465 161 AKALDKEKEGEKRLAEHDKLINKYKDEI-KFDRNQKVLPAVVAKAGLLAHPNYSYVGQFLNELGFKNALSDDvtkglsKY 239
Cdd:COG4594 159 AKALGKEEEAEAVLADHDQRIAEAKAKLaAADKGKKVAVGQFRADGLRLYTPNSFAGSVLAALGFENPPKQS------KD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613366465 240 LKGPYLQLDTEHLADLNPERMIIMTDnakKDSAEFKKLQEDATWKKLNAVKNNRVDIVDRDVWARSRGLISSEEMAKELV 319
Cdd:COG4594 233 NGYGYSEVSLEQLPALDPDVLFIATY---DDPSILKEWKNNPLWKNLKAVKNGRVYEVDGDLWTRGRGPLAAELMADDLV 309
|
....*..
gi 613366465 320 ELSKKEQ 326
Cdd:COG4594 310 EILLKKK 316
|
|
| fecB |
PRK11411 |
iron-dicitrate transporter substrate-binding subunit; Provisional |
33-324 |
3.24e-94 |
|
iron-dicitrate transporter substrate-binding subunit; Provisional
Pssm-ID: 183123 [Multi-domain] Cd Length: 303 Bit Score: 281.95 E-value: 3.24e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613366465 33 SSTKDTISVKDENGTVKVPKDAKRIVVLEYSFADALAALDVKPVGIADDGKKKRIIKPVREKIGDYTSVGTRKQPNLEEI 112
Cdd:PRK11411 18 SSHAFAVTVQDEQGTFTLEKTPQRIVVLELSFVDALAAVGVSPVGVADDNDAKRILPEVRAHLKPWQSVGTRSQPSLEAI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613366465 113 SKLKPDLIIADSSRHKGINKELNKIAPTLSLKSFDGDYKQNIDAFKTIAKALDKEKEGEKRLAEHDKLINKYKDeiKFDR 192
Cdd:PRK11411 98 AALKPDLIIADSSRHAGVYIALQKIAPTLLLKSRNETYQENLQSAAIIGEVLGKKREMQARIEQHKERMAQFAS--QLPK 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613366465 193 NQKVLPAVVAKAGLLAHPNYSYVGQFLNELGFKNALSDDVTKglskylkgPYLQLDTEHLADLNPERMIImtdNAKKDSA 272
Cdd:PRK11411 176 GTRVAFGTSREQQFNLHSPESYTGSVLAALGLNVPKAPMNGA--------AMPSISLEQLLALNPDWLLV---AHYRQES 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 613366465 273 EFKKLQEDATWKKLNAVKNNRVDIVDRDVWARSRGLISSEEMAKELVELSKK 324
Cdd:PRK11411 245 IVKRWQQDPLWQMLTAAKKQQVASVDSNTWARMRGIFAAERIAKDTVKIFHH 296
|
|
| FhuD |
cd01146 |
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial ... |
52-316 |
2.46e-86 |
|
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: 259.91 E-value: 2.46e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613366465 52 KDAKRIVVLEYSFADALAALDVKPVGIADDGKKKRIIKPVREKIGDYTSVGTRKQPNLEEISKLKPDLIIADSSRHKGIN 131
Cdd:cd01146 1 AKPQRIVALDWGALETLLALGVKPVGVADTAGYKPWIPEPALPLEGVVDVGTRGQPNLEAIAALKPDLILGSASRHDEIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613366465 132 KELNKIAPTLSLKSFDgDYKQNIDAFKTIAKALDKEKEGEKRLAEHDKLINKYKDEIKFDRNQKVLPAVVAKAG-LLAHP 210
Cdd:cd01146 81 DQLSQIAPTVLLDSSP-WLAEWKENLRLIAKALGKEEEAEKLLAEYDQRLAELRQKLPDKGPKPVSVVRFSDAGsIRLYG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613366465 211 NYSYVGQFLNELGFKNALSDDVTKGlskylkGPYLQLDTEHLADLNPERMIIMTDNAKKDsaeFKKLQEDATWKKLNAVK 290
Cdd:cd01146 160 PNSFAGSVLEDLGLQNPWAQETTND------SGFATISLERLAKADADVLFVFTYEDEEL---AQALQANPLWQNLPAVK 230
|
250 260
....*....|....*....|....*.
gi 613366465 291 NNRVDIVDRDVWARSRGLISSEEMAK 316
Cdd:cd01146 231 NGRVYVVDDVWWFFGGGLSAARLLLD 256
|
|
| Peripla_BP_2 |
pfam01497 |
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ... |
58-294 |
5.65e-29 |
|
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: 111.31 E-value: 5.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613366465 58 VVLEYSFADALAALDVKPVGIADDGKKKRIIKPVREKigDYTSVGTRKQPNLEEISKLKPDLIIADSSRHKGIN-KELNK 136
Cdd:pfam01497 1 AALSPAYTEILYALGATDSIVGVDAYTRDPLKADAVA--AIVKVGAYGEINVERLAALKPDLVILSTGYLTDEAeELLSL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613366465 137 IAPTLSLkSFDGDYKQNIDAFKTIAKALDKEKEGEKRLAEHDKLINKYKDEIkfdRNQKVLPAVVAKAGLLAHP----NY 212
Cdd:pfam01497 79 IIPTVIF-ESSSTGESLKEQIKQLGELLGLEDEAEELVAEIDSALAAAKKAV---PSLTRKPVLVFGGADGGGYvvagSN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613366465 213 SYVGQFLNELGFKNALSDDVTKGlskylkgpYLQLDTEHLADLNPErMIIMTDNAKKDSAEFKKLQEDATWKKLNAVKNN 292
Cdd:pfam01497 155 TYIGDLLRILGIENIAAELSGSE--------YAPISFEAILSSNPD-VIIVSGRDSFTKTGPEFVAANPLWAGLPAVKNG 225
|
..
gi 613366465 293 RV 294
Cdd:pfam01497 226 RV 227
|
|
| IsdE |
TIGR03659 |
heme ABC transporter, heme-binding protein isdE; This family of ABC substrate-binding proteins ... |
5-294 |
4.60e-24 |
|
heme ABC transporter, heme-binding protein isdE; This family of ABC substrate-binding proteins is observed primarily in close proximity with proteins localized to the cell wall and bearing the NEAT (NEAr Transporter, pfam05031) heme-binding domain. IsdE has been shown to bind heme and is involved in the process of scavenging heme for the purpose of obtaining iron.
Pssm-ID: 274706 [Multi-domain] Cd Length: 289 Bit Score: 99.27 E-value: 4.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613366465 5 KTFSILGLIVALFLVAACGNTDNSSKKEsstkdtisVKDENGTvkvpkdakRIVVLEYSFADALAALDVKPVGIADDGKK 84
Cdd:TIGR03659 2 KILSLVLLAVLSLGLTGCSSSKEKSKVS--------NKKSKEE--------RIVATSVAVTEILDKLDLDLVGVPTSQKT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613366465 85 kriikpVREKIGDYTSVGTRKQPNLEEISKLKPDLIIADSSRHKGIN---KELNKIAPTLSLKSFDGDYKqnidAFKTIA 161
Cdd:TIGR03659 66 ------LPKRYKDVPEVGNPMSPDMEKIKSLKPTVVLSVTTLEEDLGpkfKQLGVEATFLNLTSVDGMKK----SITELG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613366465 162 KALDKEKEGEKRLAEhdklINKYKDEIKFDRNQKVLPAVVAKAG-----LLAHPNySYVGQFLNELGFKNALSDDvtkgl 236
Cdd:TIGR03659 136 EKYGREEQAEKLVKE----INEKEAEVKKKVKGKKKPKVLILMGvpgsyLVATEN-SYIGDLVKLAGGENVYKGN----- 205
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 613366465 237 skylKGPYLQLDTEHLADLNPErMII-----MTDNAKKD-SAEFKklqEDATWKKLNAVKNNRV 294
Cdd:TIGR03659 206 ----KQEYLSSNTEYLLKANPD-IILraahgMPDEVKKMfDEEFK---TNDIWKHFEAVKNNRV 261
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| FecB |
COG4594 |
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and ... |
1-326 |
7.04e-140 |
|
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443650 [Multi-domain] Cd Length: 316 Bit Score: 398.14 E-value: 7.04e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613366465 1 MRglKTFSILGLIVALFLVAACGNTDNSSKKESSTKDTISVKDENGTVKVPKDAKRIVVLEYSFADALAALDVKPVGIAD 80
Cdd:COG4594 1 MK--KLLLLLILLLALLLLAACGSSSSDSSSSEAAAGARTVKHAMGETTIPGTPKRVVVLEWSFADALLALGVTPVGIAD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613366465 81 DGKKKRIIKPVREKIGDYTSVGTRKQPNLEEISKLKPDLIIADSSRHKGINKELNKIAPTLSLKSFDGDYKQNIDAFKTI 160
Cdd:COG4594 79 DNDYDRWVPYLRDLIKGVTSVGTRSQPNLEAIAALKPDLIIADKSRHEAIYDQLSKIAPTVLFKSRNGDYQENLESFKTI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613366465 161 AKALDKEKEGEKRLAEHDKLINKYKDEI-KFDRNQKVLPAVVAKAGLLAHPNYSYVGQFLNELGFKNALSDDvtkglsKY 239
Cdd:COG4594 159 AKALGKEEEAEAVLADHDQRIAEAKAKLaAADKGKKVAVGQFRADGLRLYTPNSFAGSVLAALGFENPPKQS------KD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613366465 240 LKGPYLQLDTEHLADLNPERMIIMTDnakKDSAEFKKLQEDATWKKLNAVKNNRVDIVDRDVWARSRGLISSEEMAKELV 319
Cdd:COG4594 233 NGYGYSEVSLEQLPALDPDVLFIATY---DDPSILKEWKNNPLWKNLKAVKNGRVYEVDGDLWTRGRGPLAAELMADDLV 309
|
....*..
gi 613366465 320 ELSKKEQ 326
Cdd:COG4594 310 EILLKKK 316
|
|
| fecB |
PRK11411 |
iron-dicitrate transporter substrate-binding subunit; Provisional |
33-324 |
3.24e-94 |
|
iron-dicitrate transporter substrate-binding subunit; Provisional
Pssm-ID: 183123 [Multi-domain] Cd Length: 303 Bit Score: 281.95 E-value: 3.24e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613366465 33 SSTKDTISVKDENGTVKVPKDAKRIVVLEYSFADALAALDVKPVGIADDGKKKRIIKPVREKIGDYTSVGTRKQPNLEEI 112
Cdd:PRK11411 18 SSHAFAVTVQDEQGTFTLEKTPQRIVVLELSFVDALAAVGVSPVGVADDNDAKRILPEVRAHLKPWQSVGTRSQPSLEAI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613366465 113 SKLKPDLIIADSSRHKGINKELNKIAPTLSLKSFDGDYKQNIDAFKTIAKALDKEKEGEKRLAEHDKLINKYKDeiKFDR 192
Cdd:PRK11411 98 AALKPDLIIADSSRHAGVYIALQKIAPTLLLKSRNETYQENLQSAAIIGEVLGKKREMQARIEQHKERMAQFAS--QLPK 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613366465 193 NQKVLPAVVAKAGLLAHPNYSYVGQFLNELGFKNALSDDVTKglskylkgPYLQLDTEHLADLNPERMIImtdNAKKDSA 272
Cdd:PRK11411 176 GTRVAFGTSREQQFNLHSPESYTGSVLAALGLNVPKAPMNGA--------AMPSISLEQLLALNPDWLLV---AHYRQES 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 613366465 273 EFKKLQEDATWKKLNAVKNNRVDIVDRDVWARSRGLISSEEMAKELVELSKK 324
Cdd:PRK11411 245 IVKRWQQDPLWQMLTAAKKQQVASVDSNTWARMRGIFAAERIAKDTVKIFHH 296
|
|
| FhuD |
cd01146 |
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial ... |
52-316 |
2.46e-86 |
|
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: 259.91 E-value: 2.46e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613366465 52 KDAKRIVVLEYSFADALAALDVKPVGIADDGKKKRIIKPVREKIGDYTSVGTRKQPNLEEISKLKPDLIIADSSRHKGIN 131
Cdd:cd01146 1 AKPQRIVALDWGALETLLALGVKPVGVADTAGYKPWIPEPALPLEGVVDVGTRGQPNLEAIAALKPDLILGSASRHDEIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613366465 132 KELNKIAPTLSLKSFDgDYKQNIDAFKTIAKALDKEKEGEKRLAEHDKLINKYKDEIKFDRNQKVLPAVVAKAG-LLAHP 210
Cdd:cd01146 81 DQLSQIAPTVLLDSSP-WLAEWKENLRLIAKALGKEEEAEKLLAEYDQRLAELRQKLPDKGPKPVSVVRFSDAGsIRLYG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613366465 211 NYSYVGQFLNELGFKNALSDDVTKGlskylkGPYLQLDTEHLADLNPERMIIMTDNAKKDsaeFKKLQEDATWKKLNAVK 290
Cdd:cd01146 160 PNSFAGSVLEDLGLQNPWAQETTND------SGFATISLERLAKADADVLFVFTYEDEEL---AQALQANPLWQNLPAVK 230
|
250 260
....*....|....*....|....*.
gi 613366465 291 NNRVDIVDRDVWARSRGLISSEEMAK 316
Cdd:cd01146 231 NGRVYVVDDVWWFFGGGLSAARLLLD 256
|
|
| FepB |
COG0614 |
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ... |
56-318 |
3.17e-45 |
|
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 440379 [Multi-domain] Cd Length: 264 Bit Score: 154.77 E-value: 3.17e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613366465 56 RIVVLEYSFADALAALDVKP--VGIADDGkkkrIIKPVREKIGDYTSVGTRKQPNLEEISKLKPDLIIADSS-RHKGINK 132
Cdd:COG0614 2 RIVSLSPSATELLLALGAGDrlVGVSDWG----YCDYPELELKDLPVVGGTGEPNLEAILALKPDLVLASSSgNDEEDYE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613366465 133 ELNKI-APTLslkSFDGDYKQNI-DAFKTIAKALDKEKEGEKRLAEHDKLINKYKDEIK-FDRNQKVLPAVVAKAGLLAH 209
Cdd:COG0614 78 QLEKIgIPVV---VLDPRSLEDLyESIRLLGELLGREERAEALIAEYEARLAAVRARLAgAEERPTVLYEIWSGDPLYTA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613366465 210 PNYSYVGQFLNELGFKNALSDdvtkglskyLKGPYLQLDTEHLADLNPERMIIMTDNAKKDSAE--FKKLQEDATWKKLN 287
Cdd:COG0614 155 GGGSFIGELLELAGGRNVAAD---------LGGGYPEVSLEQVLALDPDVIILSGGGYDAETAEeaLEALLADPGWQSLP 225
|
250 260 270
....*....|....*....|....*....|...
gi 613366465 288 AVKNNRVDIVDRDVWARS--RGLISSEEMAKEL 318
Cdd:COG0614 226 AVKNGRVYVVPGDLLSRPgpRLLLALEDLAKAL 258
|
|
| CeuA |
COG4607 |
ABC-type enterochelin transport system, periplasmic component [Inorganic ion transport and ... |
1-318 |
6.79e-45 |
|
ABC-type enterochelin transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443657 [Multi-domain] Cd Length: 310 Bit Score: 155.34 E-value: 6.79e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613366465 1 MRglKTFSILGLIVALFLVAACGNTDnSSKKESSTKDTISVKDENGTVKVPKDAKRIVVLEYSFADALAALDVKPVGIAD 80
Cdd:COG4607 1 MK--KTLLAALALAAALALAACGSSS-AAAASAAAAETVTVEHALGTVEVPKNPKRVVVFDNGALDTLDALGVEVAGVPK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613366465 81 DGKKKRIiKPVREKigDYTSVGTRKQPNLEEISKLKPDLIIAdSSRHKGINKELNKIAPTLSL----KSFDGDYKQNIDa 156
Cdd:COG4607 78 GLLPDYL-SKYADD--KYANVGTLFEPDLEAIAALKPDLIII-GGRSAKKYDELSKIAPTIDLtvdgEDYLESLKRNTE- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613366465 157 fkTIAKALDKEKEGEKRLAEHDKLINKYKDeiKFDRNQKVLpAVVAKAG-LLAHPNYSYVGQFLNELGFKNALSDDVTkg 235
Cdd:COG4607 153 --TLGEIFGKEDEAEELVADLDAKIAALKA--AAAGKGTAL-IVLTNGGkISAYGPGSRFGPIHDVLGFKPADEDIEA-- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613366465 236 lskylkgpylqlDT-------EHLADLNPERMIIMTDNA----KKDSAefKKLQEDATWKKLNAVKNNRVDIVDRDVW-A 303
Cdd:COG4607 226 ------------SThgqaisfEFIAEANPDWLFVIDRDAaiggEGPAA--KQVLDNELVKQTTAWKNGQIVYLDPDAWyL 291
|
330
....*....|....*
gi 613366465 304 RSRGLISSEEMAKEL 318
Cdd:COG4607 292 AGGGIQSLTEMLDEV 306
|
|
| FatB |
cd01140 |
Siderophore binding protein FatB. These proteins have been shown to function as ABC-type ... |
45-318 |
1.05e-34 |
|
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: 127.37 E-value: 1.05e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613366465 45 NGTVKVPKDAKRIVVLEYSFADALAALDVKPVGIADDGKKKRIIKPVreKIGDYTSVGTRKQPNLEEISKLKPDLIIAdS 124
Cdd:cd01140 3 LGETKVPKNPEKVVVFDVGALDTLDALGVKVVGVPKSSTLPEYLKKY--KDDKYANVGTLFEPDLEAIAALKPDLIII-G 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613366465 125 SRHKGINKELNKIAPT----LSLKSFDGDYKQNIDafkTIAKALDKEKEGEKRLAEHDKLINKYKDEIKFDRNQKVLpaV 200
Cdd:cd01140 80 GRLAEKYDELKKIAPTidlgADLKNYLESVKQNIE---TLGKIFGKEEEAKELVAEIDASIAEAKSAAKGKKKALVV--L 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613366465 201 VAKAGLLAHPNYSYVGQFLNELGFKNALSDDVTkglskylKGPYLQLDTEHLADLNPErMIIMTDNAKKDSAEFKKLQED 280
Cdd:cd01140 155 VNGGKLSAFGPGSRFGWLHDLLGFEPADENIKA-------SSHGQPVSFEYILEANPD-WLFVIDRGAAIGAEGSSAKEV 226
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 613366465 281 AT---WKKLNAVKNNRVDIVDRDVWARSRGLISS-EEMAKEL 318
Cdd:cd01140 227 LDndlVKNTTAWKNGKVIYLDPDLWYLSGGGLESlKQMIDDL 268
|
|
| FeuA |
cd01138 |
Periplasmic binding protein FeuA. These proteins have predicted to function as initial ... |
46-301 |
1.72e-33 |
|
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: 123.60 E-value: 1.72e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613366465 46 GTVKVPKDAKRIVVLEYSFADaLAALDVKPVGIADDGKK----KRIIKPVREKIGDYtsvgtrkqPNLEEISKLKPDLII 121
Cdd:cd01138 1 GEVEIPAKPKRIVALSGETEG-LALLGIKPVGAASIGGKnpyyKKKTLAKVVGIVDE--------PNLEKVLELKPDLII 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613366465 122 AdSSRHKGINKELNKIAPTLSLKSFDGDYKQNidaFKTIAKALDKEKEGEKRLAEHDKLINKYKDEIKFDRNQKVLPAVV 201
Cdd:cd01138 72 V-SSKQEENYEKLSKIAPTVPVSYNSSDWEEQ---LKEIGKLLNKEDEAEKWLADYKQKAKEAKEKIKKKLGNDKSVAVL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613366465 202 AKAGLLAhpNYSYVGQFLN-----ELGFKnalsddVTKGLSKYLKGP-YLQLDTEHLADLNPERMIIMTDNAKKDSAEFK 275
Cdd:cd01138 148 RGRKQIY--VFGEDGRGGGpilyaDLGLK------APEKVKEIEDKPgYAAISLEVLPEFDADYIFLLFFTGPEAKADFE 219
|
250 260
....*....|....*....|....*.
gi 613366465 276 KLQedaTWKKLNAVKNNRVDIVDRDV 301
Cdd:cd01138 220 SLP---IWKNLPAVKNNHVYIVDAWV 242
|
|
| Peripla_BP_2 |
pfam01497 |
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ... |
58-294 |
5.65e-29 |
|
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: 111.31 E-value: 5.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613366465 58 VVLEYSFADALAALDVKPVGIADDGKKKRIIKPVREKigDYTSVGTRKQPNLEEISKLKPDLIIADSSRHKGIN-KELNK 136
Cdd:pfam01497 1 AALSPAYTEILYALGATDSIVGVDAYTRDPLKADAVA--AIVKVGAYGEINVERLAALKPDLVILSTGYLTDEAeELLSL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613366465 137 IAPTLSLkSFDGDYKQNIDAFKTIAKALDKEKEGEKRLAEHDKLINKYKDEIkfdRNQKVLPAVVAKAGLLAHP----NY 212
Cdd:pfam01497 79 IIPTVIF-ESSSTGESLKEQIKQLGELLGLEDEAEELVAEIDSALAAAKKAV---PSLTRKPVLVFGGADGGGYvvagSN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613366465 213 SYVGQFLNELGFKNALSDDVTKGlskylkgpYLQLDTEHLADLNPErMIIMTDNAKKDSAEFKKLQEDATWKKLNAVKNN 292
Cdd:pfam01497 155 TYIGDLLRILGIENIAAELSGSE--------YAPISFEAILSSNPD-VIIVSGRDSFTKTGPEFVAANPLWAGLPAVKNG 225
|
..
gi 613366465 293 RV 294
Cdd:pfam01497 226 RV 227
|
|
| TroA_e |
cd01142 |
Periplasmic binding protein TroA_e. These proteins are predicted to function as initial ... |
32-324 |
2.35e-25 |
|
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: 102.82 E-value: 2.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613366465 32 ESSTKDTISVKDENG-TVKVPKDAKRIVVLEYSFADALAALDVKPVGIADDGKKKRIIKPVR--EKIGDYTSVGTRKQPN 108
Cdd:cd01142 1 PAATAATRTITDMAGrKVTIPDEVKRIAALWGAGNAVVAALGGGKLIVATTSTVQQEPWLYRlaPSLENVATGGTGNDVN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613366465 109 LEEISKLKPDLIIADSSRHKGINKELNKIAPTLSLKsfDGDYKQNIDAFKTIAKALDKEKEGEKRLAEHDKLINKYKDEI 188
Cdd:cd01142 81 IEELLALKPDVVIVWSTDGKEAGKAVLRLLNALSLR--DAELEEVKLTIALLGELLGRQEKAEALVAYFDDNLAYVAART 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613366465 189 K-FDRNQKVLPAVVAKAGLLAHPNYSYVGQFLNELGFKNALSDDVTKGLSKYlkgpylqlDTEHLADLNPERMIIMTDNA 267
Cdd:cd01142 159 KkLPDSERPRVYYAGPDPLTTDGTGSITNSWIDLAGGINVASEATKKGSGEV--------SLEQLLKWNPDVIIVGNADT 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 613366465 268 KKDsaefkkLQEDATWKKLNAVKNNRVDIVDRDVWARSRGlisSEEMAKELVELSKK 324
Cdd:cd01142 231 KAA------ILADPRWQNLRAVKNGRVYVNPEGAFWWDRP---SAEEALLGLWLAKT 278
|
|
| TroA-like |
cd00636 |
Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function ... |
55-200 |
4.54e-24 |
|
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: 95.70 E-value: 4.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613366465 55 KRIVVLEYSFADALAAL--DVKPVGIADDGKKKriiKPVREKIGDYTSVGTRKQPNLEEISKLKPDLIIADSSRHKGINK 132
Cdd:cd00636 1 KRVVALDPGATELLLALggDDKPVGVADPSGYP---PEAKALLEKVPDVGHGYEPNLEKIAALKPDLIIANGSGLEAWLD 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613366465 133 ELNKIA-PTLSL-KSFDGDYKQNIDAFKTIAKALDKEKEGEKRLAEHDKLINKYKDEIKFDRNQKVLPAV 200
Cdd:cd00636 78 KLSKIAiPVVVVdEASELSLENIKESIRLIGKALGKEENAEELIAELDARLAELRAKLAKIPKKKVSLVV 147
|
|
| IsdE |
TIGR03659 |
heme ABC transporter, heme-binding protein isdE; This family of ABC substrate-binding proteins ... |
5-294 |
4.60e-24 |
|
heme ABC transporter, heme-binding protein isdE; This family of ABC substrate-binding proteins is observed primarily in close proximity with proteins localized to the cell wall and bearing the NEAT (NEAr Transporter, pfam05031) heme-binding domain. IsdE has been shown to bind heme and is involved in the process of scavenging heme for the purpose of obtaining iron.
Pssm-ID: 274706 [Multi-domain] Cd Length: 289 Bit Score: 99.27 E-value: 4.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613366465 5 KTFSILGLIVALFLVAACGNTDNSSKKEsstkdtisVKDENGTvkvpkdakRIVVLEYSFADALAALDVKPVGIADDGKK 84
Cdd:TIGR03659 2 KILSLVLLAVLSLGLTGCSSSKEKSKVS--------NKKSKEE--------RIVATSVAVTEILDKLDLDLVGVPTSQKT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613366465 85 kriikpVREKIGDYTSVGTRKQPNLEEISKLKPDLIIADSSRHKGIN---KELNKIAPTLSLKSFDGDYKqnidAFKTIA 161
Cdd:TIGR03659 66 ------LPKRYKDVPEVGNPMSPDMEKIKSLKPTVVLSVTTLEEDLGpkfKQLGVEATFLNLTSVDGMKK----SITELG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613366465 162 KALDKEKEGEKRLAEhdklINKYKDEIKFDRNQKVLPAVVAKAG-----LLAHPNySYVGQFLNELGFKNALSDDvtkgl 236
Cdd:TIGR03659 136 EKYGREEQAEKLVKE----INEKEAEVKKKVKGKKKPKVLILMGvpgsyLVATEN-SYIGDLVKLAGGENVYKGN----- 205
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 613366465 237 skylKGPYLQLDTEHLADLNPErMII-----MTDNAKKD-SAEFKklqEDATWKKLNAVKNNRV 294
Cdd:TIGR03659 206 ----KQEYLSSNTEYLLKANPD-IILraahgMPDEVKKMfDEEFK---TNDIWKHFEAVKNNRV 261
|
|
| FepB |
COG4592 |
ABC-type Fe2+-enterobactin transport system, periplasmic component [Inorganic ion transport ... |
1-294 |
3.56e-22 |
|
ABC-type Fe2+-enterobactin transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443649 [Multi-domain] Cd Length: 330 Bit Score: 95.01 E-value: 3.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613366465 1 MRGLKTFSILGLIVALFLVAACGNTDNSSKKESSTKD---TISVKDENGTVKVPKDAKRIVVLEYSFADALAALDVKPVG 77
Cdd:COG4592 1 MARRRLAAAAALLAAALLLAGCSSADSTASGTSTAAAggwPRTVTTEKGTVTLPAKPQRIVSTSVTLTGSLLAIDAPVVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613366465 78 --------IADDG---------KKKRIIKPVreKIGDytsvgtrkQPNLEEISKLKPDLIIADSSRHKGINK---ELNKI 137
Cdd:COG4592 81 sgattpnnVTDDQgffrqwadvAKERGVKRL--YIGL--------EPNAEAIAAAAPDLIIGSATGGDSALDlydQLSAI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613366465 138 APTLSLksfDGDYKQNIDAFKTIAKALDKEKEGEKRLAEHDKLINKYKDEIKfdrnqkvLPA--VVA-------KAGLLA 208
Cdd:COG4592 151 APTLVV---NYDDKSWQELATQLGEATGHEAQADAVIAAFDARVAEVKAAIT-------LPPqpVSAlvynedgGANLWT 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613366465 209 HPnySYVGQFLNELGFKNA-LSDDVTKGLSKYLKGPYLQLDTEHLAD-LNPERMIIMtDNAKKDSAEFKklqEDATWKKL 286
Cdd:COG4592 221 PE--SAQGQLLQALGFTLApLPAELATSTSQGKRGDIVQLSGENLAAaLTGPTLFLF-AADDKDVDALK---ADPLLAHL 294
|
....*...
gi 613366465 287 NAVKNNRV 294
Cdd:COG4592 295 PAVQAGRV 302
|
|
| HemV-2 |
cd01147 |
Metal binding protein HemV-2. These proteins are predicted to function as initial receptors ... |
50-294 |
1.18e-14 |
|
Metal binding protein HemV-2. These proteins are predicted to function as initial receptors in ABC transport of metal ions. They belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind the metal ion in the cleft between these domains. In addition, these proteins sometimes have a low complexity region containing a metal-binding histidine-rich motif (repetitive HDH sequence).
Pssm-ID: 238567 [Multi-domain] Cd Length: 262 Bit Score: 72.75 E-value: 1.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613366465 50 VPKDAKRIVVLEYSFADALAALDV--KPVGIADDGKKK--RIIKPVREKIGDYTSVGT---RKQPNLEEISKLKPDLIIA 122
Cdd:cd01147 1 VPKPVERVVAAGPGALRLLYALAApdKIVGVDDAEKSDegRPYFLASPELKDLPVIGRggrGNTPNYEKIAALKPDVVID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613366465 123 -DSSRHKGINKELNKIA--PTLSLkSFDGDYKQNIDAFKTIAKALDKEKEGEKrLAEhdkLINKYKDEIKfDRNQKV--- 196
Cdd:cd01147 81 vGSDDPTSIADDLQKKTgiPVVVL-DGGDSLEDTPEQIRLLGKVLGKEERAEE-LIS---FIESILADVE-ERTKDIpde 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613366465 197 --------LPAVVAKAGLLAHPNySYVGQFLnELGFKNALSDDVTKGLskylkgpyLQLDTEHLADLNPErmIIMTDNAK 268
Cdd:cd01147 155 ekptvyfgRIGTKGAAGLESGLA-GSIEVFE-LAGGINVADGLGGGGL--------KEVSPEQILLWNPD--VIFLDTGS 222
|
250 260
....*....|....*....|....*.
gi 613366465 269 KDSAEFKKLQEDATWKKLNAVKNNRV 294
Cdd:cd01147 223 FYLSLEGYAKNRPFWQSLKAVKNGRV 248
|
|
| PRK10576 |
PRK10576 |
Fe(3+)-hydroxamate ABC transporter substrate-binding protein FhuD; |
51-227 |
8.47e-13 |
|
Fe(3+)-hydroxamate ABC transporter substrate-binding protein FhuD;
Pssm-ID: 236719 Cd Length: 292 Bit Score: 67.73 E-value: 8.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613366465 51 PKDAKRIVVLEYSFADALAALDVKPVGIADdgkkkriiKP-----VREKI--GDYTSVGTRKQPNLEEISKLKPDLIIAd 123
Cdd:PRK10576 29 AIDPNRIVALEWLPVELLLALGVTPYGVAD--------THnyrlwVSEPAlpDSVIDVGLRTEPNLELLTQMKPSLILW- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613366465 124 sSRHKGINKE-LNKIAPTLSLKSFDGdyKQNI----DAFKTIAKALDKEKEGEKRLAEHDKLINKYKDEIKFDRNQKVLP 198
Cdd:PRK10576 100 -SAGYGPSPEkLARIAPGRGFAFSDG--KKPLavarKSLVELAQRLNLEAAAETHLAQFDDFIASAKPRLAGRGQRPLLL 176
|
170 180 190
....*....|....*....|....*....|.
gi 613366465 199 AVV--AKAGLLAHPNySYVGQFLNELGFKNA 227
Cdd:PRK10576 177 TSLidPRHALVFGPN-SLFQEVLDELGIENA 206
|
|
| BtuF |
cd01144 |
Cobalamin binding protein BtuF. These proteins have been shown to function as initial ... |
55-305 |
3.64e-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: 65.01 E-value: 3.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613366465 55 KRIVVLEYSFADALAAL--DVKPVGIAD-----DGKKKRiikpvrekigdyTSVGTRKQPNLEEISKLKPDLIIADSSRH 127
Cdd:cd01144 1 MRIVSLAPSATELLYALglGDQLVGVTDycdypPEAKKL------------PRVGGFYQLDLERVLALKPDLVIAWDDCN 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613366465 128 KGIN-KELNKIAPTLSlkSFDG-DYKQNIDAFKTIAKALDKEKEGEKRLAEHDKLINKYKDEIKFDRNQKVL-------P 198
Cdd:cd01144 69 VCAVvDQLRAAGIPVL--VSEPqTLDDILADIRRLGTLAGRPARAEELAEALRRRLAALRKQYASKPPPRVFyqewidpL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613366465 199 AVVAKAgllahpnysYVGQFLNELGFKNALSDdvtkglskyLKGPYLQLDTEHLADLNPERMIIMTDNAkkdSAEFKKLQ 278
Cdd:cd01144 147 MTAGGD---------WVPELIALAGGVNVFAD---------AGERSPQVSWEDVLAANPDVIVLSPCGF---GFTPAILR 205
|
250 260
....*....|....*....|....*..
gi 613366465 279 EDATWKKLNAVKNNRVDIVDRDVWARS 305
Cdd:cd01144 206 KEPAWQALPAVRNGRVYAVDGNWYFRP 232
|
|
| YvrC |
cd01143 |
Periplasmic binding protein YvrC. These proteins are predicted to function as initial ... |
52-264 |
3.37e-10 |
|
Periplasmic binding protein YvrC. These proteins are predicted to function as initial receptors in ABC transport of metal ions in eubacteria and archaea. They belong to the TroA superfamily of periplasmic metal binding proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind the metal ion in the cleft between these domains.
Pssm-ID: 238563 [Multi-domain] Cd Length: 195 Bit Score: 58.44 E-value: 3.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613366465 52 KDAKRIVVLEYSFADALAALDV--KPVGIAD-DGKKKRIIKPVreKIGDYTSvgtrkqPNLEEISKLKPDLIIADSSRHK 128
Cdd:cd01143 1 KEPERIVSLSPSITEILFALGAgdKIVGVDTySNYPKEVRKKP--KVGSYSN------PNVEKIVALKPDLVIVSSSSLA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613366465 129 GINKELNKIA-PTLSLK---SFDGDYKQnidaFKTIAKALDKEKEGEKRLAEHDKLINKYKDEIKFDRNQKVLpAVVAKA 204
Cdd:cd01143 73 ELLEKLKDAGiPVVVLPaasSLDEIYDQ----IELIGKITGAEEEAEKLVKEMKQKIDKVKDKGKTIKKSKVY-IEVSLG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 613366465 205 GLLAHPNYSYVGQFLNELGFKNALSDDVTkglskylkgpYLQLDTEHLADLNPErmIIMT 264
Cdd:cd01143 148 GPYTAGKNTFINELIRLAGAKNIAADSGG----------WPQVSPEEILKANPD--VIIL 195
|
|
| PRK10957 |
PRK10957 |
iron-enterobactin transporter periplasmic binding protein; Provisional |
7-294 |
1.08e-09 |
|
iron-enterobactin transporter periplasmic binding protein; Provisional
Pssm-ID: 236806 [Multi-domain] Cd Length: 317 Bit Score: 58.45 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613366465 7 FSILGLIVALFLVAACGNTDNSSKKESSTkdtisVKDENGTVKVPKDAKRIVVLEYSFADALAALDVkPV---------- 76
Cdd:PRK10957 2 LYRLALLLLGLLLSGIAAAQASAAGWPRT-----VTDSRGSVTLESKPQRIVSTSVTLTGTLLAIDA-PViasgattpnt 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613366465 77 GIADDGK---------KKRIIKPVrekigdYTSvgtrkQPNLEEISKLKPDLII-----ADSSRHkgINKELNKIAPTLS 142
Cdd:PRK10957 76 RVADDQGffrqwsdvaKERGVEVL------YIG-----EPDAEAVAAQMPDLIVisatgGDSALA--LYDQLSAIAPTLV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613366465 143 LksfdgDYK----QNIDAfkTIAKALDKEKEGEKRLAEHDKLINKYKDEIKfdrnqkvLP-----AVV----AKAGLLAH 209
Cdd:PRK10957 143 I-----DYDdkswQELAT--QLGEATGLEKQAAAVIAQFDAQLAEVKAKIT-------LPpqpvsALVyngaGHSANLWT 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613366465 210 PNySYVGQFLNELGFKNA-LSDDVTKGLSKYLKGPYLQLDTEHLAD-LNPERMIIMTdnakKDSAEFKKLQEDATWKKLN 287
Cdd:PRK10957 209 PE-SAQGQLLEQLGFTLAeLPAGLQASTSQGKRHDIIQLGGENLAAgLNGETLFLFA----GDDKDADAFLADPLLANLP 283
|
....*..
gi 613366465 288 AVKNNRV 294
Cdd:PRK10957 284 AVQNKQV 290
|
|
| TroA_f |
cd01139 |
Periplasmic binding protein TroA_f. These proteins are predicted to function as initial ... |
39-294 |
3.25e-08 |
|
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: 54.24 E-value: 3.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613366465 39 ISVKDENG-TVKVPKDAKRIVVLEYSFADALAALD-----VKPVGIADDGKKKR-----IIKPVREKIGDYTSVGTRKQP 107
Cdd:cd01139 1 ITVTDVAGrKVTLDAPVERVLLGEGRQLYALALLEgenpfARIVGWGGDLKKGDpdtyaKYKEKFPEIADIPLIGSTYNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613366465 108 --NLEEISKLKPDLIIADSSRHK-----GINKELNKIAPTLSLKSFDGDYKQN-IDAFKTIAKALDKEKEGEKRLAEHDK 179
Cdd:cd01139 81 dfSVEKVLTLKPDLVILNIWAKTtaeesGILEKLEQAGIPVVFVDFRQKPLKNtTPSMRLLGKALGREERAEEFIEFYQE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613366465 180 LINKYKDEIKFDRNQKvlPAVVAKAGLLAHPNY------SYVGQFLNELGFKNaLSDDVTKGLSKylkgpylQLDTEHLA 253
Cdd:cd01139 161 RIDRIRDRLAKINEPK--PKVFIELGAGGPEECcstygnGNWGELVDAAGGDN-IADGLIPGTSG-------ELNAEYVI 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 613366465 254 DLNPErMIIMTD---NAKKDS---------AEFKKLQEDAT-----WKKLNAVKNNRV 294
Cdd:cd01139 231 AANPE-IIIATGgnwAKDPSGvslgpdgttADAKESLLRALlkrpgWSSLQAVKNGRV 287
|
|
| TroA_d |
cd01141 |
Periplasmic binding protein TroA_d. These proteins are predicted to function as initial ... |
47-186 |
4.79e-08 |
|
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: 52.42 E-value: 4.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613366465 47 TVKVPkdAKRIVVLEYSFADALAALDV--KPVGIadDGKKKRIIKPVREKIGDYtSVGTRKQPNLEEISKLKPDLII--A 122
Cdd:cd01141 3 TIKVP--PKRIVVLSPTHVDLLLALDKadKIVGV--SASAYDLNTPAVKERIDI-QVGPTGSLNVELIVALKPDLVIlyG 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 613366465 123 DSSRHKGINK--ELNKIAPTLslkSFDGDYKQNIDAFKTIAKALDKEKEgEKRLAEHDKLINKYKD 186
Cdd:cd01141 78 GFQAQTILDKleQLGIPVLYV---NEYPSPLGRAEWIKFAAAFYGVGKE-DKADEAFAQIAGRYRD 139
|
|
| TroA_a |
cd01148 |
Metal binding protein TroA_a. These proteins are predicted to function as initial receptors ... |
37-294 |
1.35e-05 |
|
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: 45.79 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613366465 37 DTISVKDENGTVKVPKDAKRIVVLEYSFADALAALDVKP--VGIADDGKKkriIKPVREKIGDYTSVGTRKQPNLEEISK 114
Cdd:cd01148 1 YPLTVENCGRSVTFDKAPQRVVSNDQNTTEMMLALGLQDrmVGTAGIDNK---DLPELKAKYDKVPELAKKYPSKETVLA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613366465 115 LKPDLIIADSS---RHKGIN--KELNKI-APTLSLKSFDG--DYKQNIDA----FKTIAKALDKEKEGEKRLAEHDKLIN 182
Cdd:cd01148 78 ARPDLVFGGWSygfDKGGLGtpDSLAELgIKTYILPESCGqrRGEATLDDvyndIRNLGKIFDVEDRADKLVADLKARLA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613366465 183 KYKDEIKfdRNQKVLPAVVAKAGLLAHPNYSYVG---QFLNELGFKNALSDdvtkglskyLKGPYLQLDTEHLADLNPER 259
Cdd:cd01148 158 EISAKVK--GDGKKVAVFVYDSGEDKPFTSGRGGipnAIITAAGGRNVFAD---------VDESWTTVSWETVIARNPDV 226
|
250 260 270
....*....|....*....|....*....|....*.
gi 613366465 260 -MIIMTDNAKKDSAEFKKLQEDATWKKLNAVKNNRV 294
Cdd:cd01148 227 iVIIDYGDQNAAEQKIKFLKENPALKNVPAVKNNRF 262
|
|
| ChuT |
COG4558 |
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism] ... |
53-298 |
1.86e-05 |
|
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443619 [Multi-domain] Cd Length: 285 Bit Score: 45.57 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613366465 53 DAKRIVVLEYSFADALAALdvkpvgiaddGKKKRII-------KPvrEKIGDYTSVGTRKQPNLEEISKLKPDLIIADSS 125
Cdd:COG4558 26 AAERIVSLGGSVTEIVYAL----------GAGDRLVgvdttstYP--AAAKALPDVGYMRQLSAEGILSLKPTLVLASEG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613366465 126 ----------RHKGInkELNKIAPTLSLKSFdgdyKQNIDAfktIAKALDKEKEGEKRLAEHDKLINKYKDEI-KFDRNQ 194
Cdd:COG4558 94 agppevldqlRAAGV--PVVVVPAAPSLEGV----LAKIRA---VAAALGVPEAGEALAARLEADLAALAARVaAIGKPP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613366465 195 KVL--------PAVVAKAGLLAHpnysyvgQFLNELGFKNALSDdvtkglskyLKGpYLQLDTEHLADLNPERMIIMTDN 266
Cdd:COG4558 165 RVLfllsrgggRPMVAGRGTAAD-------ALIRLAGGVNAAAG---------FEG-YKPLSAEALIAAAPDVILVMTRG 227
|
250 260 270
....*....|....*....|....*....|....*..
gi 613366465 267 AKKDSAefkklqEDATWK-----KLNAVKNNRVDIVD 298
Cdd:COG4558 228 LESLGG------VDGLLAlpglaQTPAGKNKRIVAMD 258
|
|
| |
