|
Name |
Accession |
Description |
Interval |
E-value |
| FecB |
COG4594 |
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and ... |
3-327 |
4.21e-105 |
|
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443650 [Multi-domain] Cd Length: 316 Bit Score: 310.31 E-value: 4.21e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578584380 3 KVIKMLVVTLAFLLVLAGCSGNSNKQSSDNKDKETTSIKHAMGTTEIKGKPKRVVTLYQGATDVAVSLGVKPVGAVESWT 82
Cdd:COG4594 2 KKLLLLLILLLALLLLAACGSSSSDSSSSEAAAGARTVKHAMGETTIPGTPKRVVVLEWSFADALLALGVTPVGIADDND 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578584380 83 QKPKFEYIKNDLKDTKIVGQEPAPNLEEISKLKPDLIVASKVRNEKVYDQLSKIAPTVSTDTV-FKFKDT---TKLMGKA 158
Cdd:COG4594 82 YDRWVPYLRDLIKGVTSVGTRSQPNLEAIAALKPDLIIADKSRHEAIYDQLSKIAPTVLFKSRnGDYQENlesFKTIAKA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578584380 159 LGKEKEAEDLLKKYDDKVAafqkDAKAKYKDA-WPLKASVVNFRADHTRIY-AGGYAGEILNDLGFKRNkdlQKQVDNGK 236
Cdd:COG4594 162 LGKEEEAEAVLADHDQRIA----EAKAKLAAAdKGKKVAVGQFRADGLRLYtPNSFAGSVLAALGFENP---PKQSKDNG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578584380 237 DIIQLTSKESIPLMNADHIFVVKSDpnakDAALVKktesEWTSSKEWKNLDAVKNNQVsDDLDEITWNLAGGYKSSLKLI 316
Cdd:COG4594 235 YGYSEVSLEQLPALDPDVLFIATYD----DPSILK----EWKNNPLWKNLKAVKNGRV-YEVDGDLWTRGRGPLAAELMA 305
|
330
....*....|.
gi 578584380 317 DDLYEKLNIEK 327
Cdd:COG4594 306 DDLVEILLKKK 316
|
|
| FhuD |
cd01146 |
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial ... |
51-318 |
1.42e-82 |
|
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: 250.67 E-value: 1.42e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578584380 51 GKPKRVVTLYQGATDVAVSLGVKPVGAVESWTQKPKFEYIKNDLKDTKIVGQEPAPNLEEISKLKPDLIVASKVRNEKVY 130
Cdd:cd01146 1 AKPQRIVALDWGALETLLALGVKPVGVADTAGYKPWIPEPALPLEGVVDVGTRGQPNLEAIAALKPDLILGSASRHDEIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578584380 131 DQLSKIAPTV---STDTVFKFKDTTKLMGKALGKEKEAEDLLKKYDDKVAafqkDAKAKYKDAWPLKASVVNFR-ADHTR 206
Cdd:cd01146 81 DQLSQIAPTVlldSSPWLAEWKENLRLIAKALGKEEEAEKLLAEYDQRLA----ELRQKLPDKGPKPVSVVRFSdAGSIR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578584380 207 IY-AGGYAGEILNDLGFKRNKDLQKQVDNGkdiIQLTSKESIPLMNADHIFVVksdpnakdAALVKKTESEWTSSKEWKN 285
Cdd:cd01146 157 LYgPNSFAGSVLEDLGLQNPWAQETTNDSG---FATISLERLAKADADVLFVF--------TYEDEELAQALQANPLWQN 225
|
250 260 270
....*....|....*....|....*....|...
gi 578584380 286 LDAVKNNQVSdDLDEITWNLAGGYkSSLKLIDD 318
Cdd:cd01146 226 LPAVKNGRVY-VVDDVWWFFGGGL-SAARLLLD 256
|
|
| fecB |
PRK11411 |
iron-dicitrate transporter substrate-binding subunit; Provisional |
5-324 |
5.51e-26 |
|
iron-dicitrate transporter substrate-binding subunit; Provisional
Pssm-ID: 183123 [Multi-domain] Cd Length: 303 Bit Score: 105.14 E-value: 5.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578584380 5 IKMLVVTLAFLLVLAGCSGNSnkqssdnkdkeTTSIKHAMGTTEIKGKPKRVVTLYQGATDVAVSLGVKPVGAVESWTQK 84
Cdd:PRK11411 2 LAFIRLLFAGLLLLSGSSHAF-----------AVTVQDEQGTFTLEKTPQRIVVLELSFVDALAAVGVSPVGVADDNDAK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578584380 85 PKFEYIKNDLKDTKIVGQEPAPNLEEISKLKPDLIVASKVRNEKVYDQLSKIAPTVstdtVFKFK--------DTTKLMG 156
Cdd:PRK11411 71 RILPEVRAHLKPWQSVGTRSQPSLEAIAALKPDLIIADSSRHAGVYIALQKIAPTL----LLKSRnetyqenlQSAAIIG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578584380 157 KALGKEKEAEDLLKKYddkvaafqKDAKAKYKDAWPLKASVVnF---RADHTRIYA-GGYAGEILNDLGFKRNKdlqkqV 232
Cdd:PRK11411 147 EVLGKKREMQARIEQH--------KERMAQFASQLPKGTRVA-FgtsREQQFNLHSpESYTGSVLAALGLNVPK-----A 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578584380 233 DNGKDIIQLTSKESIPLMNADHIFVVK-SDPNakdaaLVKKteseWTSSKEWKNLDAVKNNQVSdDLDEITWNLAGGYKS 311
Cdd:PRK11411 213 PMNGAAMPSISLEQLLALNPDWLLVAHyRQES-----IVKR----WQQDPLWQMLTAAKKQQVA-SVDSNTWARMRGIFA 282
|
330
....*....|...
gi 578584380 312 SLKLIDDLYEKLN 324
Cdd:PRK11411 283 AERIAKDTVKIFH 295
|
|
| Peripla_BP_2 |
pfam01497 |
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ... |
57-294 |
1.02e-24 |
|
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: 99.75 E-value: 1.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578584380 57 VTLYQGATDVAVSLGVkPVGAVESWTqKPKFEYIKNDLKDTKIVGQEPAPNLEEISKLKPDLIVASK-VRNEKVYDQLSK 135
Cdd:pfam01497 1 AALSPAYTEILYALGA-TDSIVGVDA-YTRDPLKADAVAAIVKVGAYGEINVERLAALKPDLVILSTgYLTDEAEELLSL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578584380 136 IAPTV---STDTVFKFKDTTKLMGKALGKEKEAEDLLKKYDDKVAAFQKDAkakykDAWPLKASVVNFRADHTRIYA--- 209
Cdd:pfam01497 79 IIPTVifeSSSTGESLKEQIKQLGELLGLEDEAEELVAEIDSALAAAKKAV-----PSLTRKPVLVFGGADGGGYVVags 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578584380 210 GGYAGEILNDLGFKrnKDLQKQVDNGKDIIqltSKESIPLMNADHIFVVKSDPNAKD-AALVKKTEsewtsskEWKNLDA 288
Cdd:pfam01497 154 NTYIGDLLRILGIE--NIAAELSGSEYAPI---SFEAILSSNPDVIIVSGRDSFTKTgPEFVAANP-------LWAGLPA 221
|
....*.
gi 578584380 289 VKNNQV 294
Cdd:pfam01497 222 VKNGRV 227
|
|
| IsdE |
TIGR03659 |
heme ABC transporter, heme-binding protein isdE; This family of ABC substrate-binding proteins ... |
3-320 |
3.08e-15 |
|
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: 74.62 E-value: 3.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578584380 3 KVIKMLVVTLAFLLVLAGCSGNSNKQSSDNKdkettsikhamgtteiKGKPKRVVtlyqgATDVAVS-----LGVKPVGA 77
Cdd:TIGR03659 1 KKILSLVLLAVLSLGLTGCSSSKEKSKVSNK----------------KSKEERIV-----ATSVAVTeildkLDLDLVGV 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578584380 78 VESWTQKPKfeyiknDLKDTKIVGQEPAPNLEEISKLKPDLIVAS---KVRNEKVYDQLSKIAPTVSTDTVFKFKDTTKL 154
Cdd:TIGR03659 60 PTSQKTLPK------RYKDVPEVGNPMSPDMEKIKSLKPTVVLSVttlEEDLGPKFKQLGVEATFLNLTSVDGMKKSITE 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578584380 155 MGKALGKEKEAEDLLKKYDDKVAAFQKDAKAKYKdawplkASV-VNFRADHTRIYA--GGYAGEILNDLGfkrnkdlqkq 231
Cdd:TIGR03659 134 LGEKYGREEQAEKLVKEINEKEAEVKKKVKGKKK------PKVlILMGVPGSYLVAteNSYIGDLVKLAG---------- 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578584380 232 vdnGKDIIQLTSKESIPLMNADhifVVKSDPN-------AKDAALVKKTESEWTSSKEWKNLDAVKNNQVSdDLDEITWN 304
Cdd:TIGR03659 198 ---GENVYKGNKQEYLSSNTEY---LLKANPDiilraahGMPDEVKKMFDEEFKTNDIWKHFEAVKNNRVY-DLDEELFG 270
|
330
....*....|....*....
gi 578584380 305 LAGG--YKSSLK-LIDDLY 320
Cdd:TIGR03659 271 MTANlkVAEALDeLKKILY 289
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| FecB |
COG4594 |
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and ... |
3-327 |
4.21e-105 |
|
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443650 [Multi-domain] Cd Length: 316 Bit Score: 310.31 E-value: 4.21e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578584380 3 KVIKMLVVTLAFLLVLAGCSGNSNKQSSDNKDKETTSIKHAMGTTEIKGKPKRVVTLYQGATDVAVSLGVKPVGAVESWT 82
Cdd:COG4594 2 KKLLLLLILLLALLLLAACGSSSSDSSSSEAAAGARTVKHAMGETTIPGTPKRVVVLEWSFADALLALGVTPVGIADDND 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578584380 83 QKPKFEYIKNDLKDTKIVGQEPAPNLEEISKLKPDLIVASKVRNEKVYDQLSKIAPTVSTDTV-FKFKDT---TKLMGKA 158
Cdd:COG4594 82 YDRWVPYLRDLIKGVTSVGTRSQPNLEAIAALKPDLIIADKSRHEAIYDQLSKIAPTVLFKSRnGDYQENlesFKTIAKA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578584380 159 LGKEKEAEDLLKKYDDKVAafqkDAKAKYKDA-WPLKASVVNFRADHTRIY-AGGYAGEILNDLGFKRNkdlQKQVDNGK 236
Cdd:COG4594 162 LGKEEEAEAVLADHDQRIA----EAKAKLAAAdKGKKVAVGQFRADGLRLYtPNSFAGSVLAALGFENP---PKQSKDNG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578584380 237 DIIQLTSKESIPLMNADHIFVVKSDpnakDAALVKktesEWTSSKEWKNLDAVKNNQVsDDLDEITWNLAGGYKSSLKLI 316
Cdd:COG4594 235 YGYSEVSLEQLPALDPDVLFIATYD----DPSILK----EWKNNPLWKNLKAVKNGRV-YEVDGDLWTRGRGPLAAELMA 305
|
330
....*....|.
gi 578584380 317 DDLYEKLNIEK 327
Cdd:COG4594 306 DDLVEILLKKK 316
|
|
| FhuD |
cd01146 |
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial ... |
51-318 |
1.42e-82 |
|
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: 250.67 E-value: 1.42e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578584380 51 GKPKRVVTLYQGATDVAVSLGVKPVGAVESWTQKPKFEYIKNDLKDTKIVGQEPAPNLEEISKLKPDLIVASKVRNEKVY 130
Cdd:cd01146 1 AKPQRIVALDWGALETLLALGVKPVGVADTAGYKPWIPEPALPLEGVVDVGTRGQPNLEAIAALKPDLILGSASRHDEIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578584380 131 DQLSKIAPTV---STDTVFKFKDTTKLMGKALGKEKEAEDLLKKYDDKVAafqkDAKAKYKDAWPLKASVVNFR-ADHTR 206
Cdd:cd01146 81 DQLSQIAPTVlldSSPWLAEWKENLRLIAKALGKEEEAEKLLAEYDQRLA----ELRQKLPDKGPKPVSVVRFSdAGSIR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578584380 207 IY-AGGYAGEILNDLGFKRNKDLQKQVDNGkdiIQLTSKESIPLMNADHIFVVksdpnakdAALVKKTESEWTSSKEWKN 285
Cdd:cd01146 157 LYgPNSFAGSVLEDLGLQNPWAQETTNDSG---FATISLERLAKADADVLFVF--------TYEDEELAQALQANPLWQN 225
|
250 260 270
....*....|....*....|....*....|...
gi 578584380 286 LDAVKNNQVSdDLDEITWNLAGGYkSSLKLIDD 318
Cdd:cd01146 226 LPAVKNGRVY-VVDDVWWFFGGGL-SAARLLLD 256
|
|
| FepB |
COG0614 |
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ... |
55-294 |
3.14e-43 |
|
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 440379 [Multi-domain] Cd Length: 264 Bit Score: 149.76 E-value: 3.14e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578584380 55 RVVTLYQGATDVAVSLGVKP--VGavesWTQKPKFEYIKNDLKDTKIVGQEPAPNLEEISKLKPDLIVASKVRN-EKVYD 131
Cdd:COG0614 2 RIVSLSPSATELLLALGAGDrlVG----VSDWGYCDYPELELKDLPVVGGTGEPNLEAILALKPDLVLASSSGNdEEDYE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578584380 132 QLSKI-APTVSTD--TVFKFKDTTKLMGKALGKEKEAEDLLKKYDDKVAAFQKDAKakyKDAWPLKASVVNFRADHTRIY 208
Cdd:COG0614 78 QLEKIgIPVVVLDprSLEDLYESIRLLGELLGREERAEALIAEYEARLAAVRARLA---GAEERPTVLYEIWSGDPLYTA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578584380 209 AGG-YAGEILNDLGFKRnkdlqkQVDNGKDIIQLTSKESIPLMNADHIFVVksdPNAKDAALVKKTESEWTSSKEWKNLD 287
Cdd:COG0614 155 GGGsFIGELLELAGGRN------VAADLGGGYPEVSLEQVLALDPDVIILS---GGGYDAETAEEALEALLADPGWQSLP 225
|
....*..
gi 578584380 288 AVKNNQV 294
Cdd:COG0614 226 AVKNGRV 232
|
|
| CeuA |
COG4607 |
ABC-type enterochelin transport system, periplasmic component [Inorganic ion transport and ... |
1-319 |
1.23e-42 |
|
ABC-type enterochelin transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443657 [Multi-domain] Cd Length: 310 Bit Score: 149.56 E-value: 1.23e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578584380 1 MNKVIkMLVVTLAFLLVLAGCSGNSNKQSSDNKdKETTSIKHAMGTTEIKGKPKRVVTLYQGATDVAVSLGVKPVGAves 80
Cdd:COG4607 1 MKKTL-LAALALAAALALAACGSSSAAAASAAA-AETVTVEHALGTVEVPKNPKRVVVFDNGALDTLDALGVEVAGV--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578584380 81 wtqkPKF---EYIKnDLKDTKI--VGQEPAPNLEEISKLKPDLIVASKvRNEKVYDQLSKIAPTV-----STDTVFKFKD 150
Cdd:COG4607 76 ----PKGllpDYLS-KYADDKYanVGTLFEPDLEAIAALKPDLIIIGG-RSAKKYDELSKIAPTIdltvdGEDYLESLKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578584380 151 TTKLMGKALGKEKEAEDLLKKYDDKVAAfqkdAKAKYKDAWplKASVVNFRADHTRIYA-GGYAGEILNDLGFKRNKDLQ 229
Cdd:COG4607 150 NTETLGEIFGKEDEAEELVADLDAKIAA----LKAAAAGKG--TALIVLTNGGKISAYGpGSRFGPIHDVLGFKPADEDI 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578584380 230 KQVDNGKDIiqltSKESIPLMNADHIFVV-------KSDPNAK---DAALVKKTesewtsskewknlDAVKNNQVSdDLD 299
Cdd:COG4607 224 EASTHGQAI----SFEFIAEANPDWLFVIdrdaaigGEGPAAKqvlDNELVKQT-------------TAWKNGQIV-YLD 285
|
330 340
....*....|....*....|.
gi 578584380 300 EITWNLA-GGYKSSLKLIDDL 319
Cdd:COG4607 286 PDAWYLAgGGIQSLTEMLDEV 306
|
|
| FeuA |
cd01138 |
Periplasmic binding protein FeuA. These proteins have predicted to function as initial ... |
45-294 |
8.58e-38 |
|
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: 135.15 E-value: 8.58e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578584380 45 GTTEIKGKPKRVVTLYQGATDVAVsLGVKPVGAVESWTQKPKfeYIKNDLkdTKIVGQEPAPNLEEISKLKPDLIVASKv 124
Cdd:cd01138 1 GEVEIPAKPKRIVALSGETEGLAL-LGIKPVGAASIGGKNPY--YKKKTL--AKVVGIVDEPNLEKVLELKPDLIIVSS- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578584380 125 RNEKVYDQLSKIAPTVS-TDTVFKFKDTTKLMGKALGKEKEAEDLLKKYDDKVaafqKDAKAKYKDAWPLKASVVNFR-A 202
Cdd:cd01138 75 KQEENYEKLSKIAPTVPvSYNSSDWEEQLKEIGKLLNKEDEAEKWLADYKQKA----KEAKEKIKKKLGNDKSVAVLRgR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578584380 203 DHTRIY--AGGYAGEILN-DLGFKRNKdLQKQVDNGKDIIQLtSKESIPLMNADHIFVVKSDPNAKDAALvkktesewTS 279
Cdd:cd01138 151 KQIYVFgeDGRGGGPILYaDLGLKAPE-KVKEIEDKPGYAAI-SLEVLPEFDADYIFLLFFTGPEAKADF--------ES 220
|
250
....*....|....*
gi 578584380 280 SKEWKNLDAVKNNQV 294
Cdd:cd01138 221 LPIWKNLPAVKNNHV 235
|
|
| FatB |
cd01140 |
Siderophore binding protein FatB. These proteins have been shown to function as ABC-type ... |
42-321 |
2.98e-36 |
|
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: 131.61 E-value: 2.98e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578584380 42 HAMGTTEIKGKPKRVVTLYQGATDVAVSLGVKPVGAVESWTQkPKFeyiKNDLKDTKI--VGQEPAPNLEEISKLKPDLI 119
Cdd:cd01140 1 HALGETKVPKNPEKVVVFDVGALDTLDALGVKVVGVPKSSTL-PEY---LKKYKDDKYanVGTLFEPDLEAIAALKPDLI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578584380 120 VASKvRNEKVYDQLSKIAPTV-----STDTVFKFKDTTKLMGKALGKEKEAEDLLKKYDDKVAAFQKDAKAKYkdawplK 194
Cdd:cd01140 77 IIGG-RLAEKYDELKKIAPTIdlgadLKNYLESVKQNIETLGKIFGKEEEAKELVAEIDASIAEAKSAAKGKK------K 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578584380 195 ASVVNFRADHTRIYA-GGYAGEILNDLGFKRNKDLQKQVDNGKDIiqltSKESIPLMNADHIFVVksdpnAKDAAL--VK 271
Cdd:cd01140 150 ALVVLVNGGKLSAFGpGSRFGWLHDLLGFEPADENIKASSHGQPV----SFEYILEANPDWLFVI-----DRGAAIgaEG 220
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 578584380 272 KTESEWTSSKEWKNLDAVKNNQVSdDLDEITWNLAGGYKSSLK-LIDDLYE 321
Cdd:cd01140 221 SSAKEVLDNDLVKNTTAWKNGKVI-YLDPDLWYLSGGGLESLKqMIDDLKK 270
|
|
| fecB |
PRK11411 |
iron-dicitrate transporter substrate-binding subunit; Provisional |
5-324 |
5.51e-26 |
|
iron-dicitrate transporter substrate-binding subunit; Provisional
Pssm-ID: 183123 [Multi-domain] Cd Length: 303 Bit Score: 105.14 E-value: 5.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578584380 5 IKMLVVTLAFLLVLAGCSGNSnkqssdnkdkeTTSIKHAMGTTEIKGKPKRVVTLYQGATDVAVSLGVKPVGAVESWTQK 84
Cdd:PRK11411 2 LAFIRLLFAGLLLLSGSSHAF-----------AVTVQDEQGTFTLEKTPQRIVVLELSFVDALAAVGVSPVGVADDNDAK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578584380 85 PKFEYIKNDLKDTKIVGQEPAPNLEEISKLKPDLIVASKVRNEKVYDQLSKIAPTVstdtVFKFK--------DTTKLMG 156
Cdd:PRK11411 71 RILPEVRAHLKPWQSVGTRSQPSLEAIAALKPDLIIADSSRHAGVYIALQKIAPTL----LLKSRnetyqenlQSAAIIG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578584380 157 KALGKEKEAEDLLKKYddkvaafqKDAKAKYKDAWPLKASVVnF---RADHTRIYA-GGYAGEILNDLGFKRNKdlqkqV 232
Cdd:PRK11411 147 EVLGKKREMQARIEQH--------KERMAQFASQLPKGTRVA-FgtsREQQFNLHSpESYTGSVLAALGLNVPK-----A 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578584380 233 DNGKDIIQLTSKESIPLMNADHIFVVK-SDPNakdaaLVKKteseWTSSKEWKNLDAVKNNQVSdDLDEITWNLAGGYKS 311
Cdd:PRK11411 213 PMNGAAMPSISLEQLLALNPDWLLVAHyRQES-----IVKR----WQQDPLWQMLTAAKKQQVA-SVDSNTWARMRGIFA 282
|
330
....*....|...
gi 578584380 312 SLKLIDDLYEKLN 324
Cdd:PRK11411 283 AERIAKDTVKIFH 295
|
|
| FepB |
COG4592 |
ABC-type Fe2+-enterobactin transport system, periplasmic component [Inorganic ion transport ... |
8-294 |
4.86e-25 |
|
ABC-type Fe2+-enterobactin transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443649 [Multi-domain] Cd Length: 330 Bit Score: 103.10 E-value: 4.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578584380 8 LVVTLAFLLVLAGCSGNSNKQSSDNKDKETTS---IKHAMGTTEIKGKPKRVVTLYQGATDVAVSLGVkPVgaVESWTQK 84
Cdd:COG4592 9 AAALLAAALLLAGCSSADSTASGTSTAAAGGWprtVTTEKGTVTLPAKPQRIVSTSVTLTGSLLAIDA-PV--VASGATT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578584380 85 PK--------FEYIKNDLK--DTKIVGQEPAPNLEEISKLKPDLIVASKVRNE---KVYDQLSKIAPTVSTDTVFK-FKD 150
Cdd:COG4592 86 PNnvtddqgfFRQWADVAKerGVKRLYIGLEPNAEAIAAAAPDLIIGSATGGDsalDLYDQLSAIAPTLVVNYDDKsWQE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578584380 151 TTKLMGKALGKEKEAEDLLKKYDDKVAafqkDAKAKYKdAWPLKASVVNFRADhtriyaGGYA--------GEILNDLGF 222
Cdd:COG4592 166 LATQLGEATGHEAQADAVIAAFDARVA----EVKAAIT-LPPQPVSALVYNED------GGANlwtpesaqGQLLQALGF 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578584380 223 K-----RNKDLQKQVDNGKDIIQLtSKESIP-LMNADHIFVVKSDpnAKDAALVKktesewtSSKEWKNLDAVKNNQV 294
Cdd:COG4592 235 TlaplpAELATSTSQGKRGDIVQL-SGENLAaALTGPTLFLFAAD--DKDVDALK-------ADPLLAHLPAVQAGRV 302
|
|
| Peripla_BP_2 |
pfam01497 |
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ... |
57-294 |
1.02e-24 |
|
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: 99.75 E-value: 1.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578584380 57 VTLYQGATDVAVSLGVkPVGAVESWTqKPKFEYIKNDLKDTKIVGQEPAPNLEEISKLKPDLIVASK-VRNEKVYDQLSK 135
Cdd:pfam01497 1 AALSPAYTEILYALGA-TDSIVGVDA-YTRDPLKADAVAAIVKVGAYGEINVERLAALKPDLVILSTgYLTDEAEELLSL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578584380 136 IAPTV---STDTVFKFKDTTKLMGKALGKEKEAEDLLKKYDDKVAAFQKDAkakykDAWPLKASVVNFRADHTRIYA--- 209
Cdd:pfam01497 79 IIPTVifeSSSTGESLKEQIKQLGELLGLEDEAEELVAEIDSALAAAKKAV-----PSLTRKPVLVFGGADGGGYVVags 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578584380 210 GGYAGEILNDLGFKrnKDLQKQVDNGKDIIqltSKESIPLMNADHIFVVKSDPNAKD-AALVKKTEsewtsskEWKNLDA 288
Cdd:pfam01497 154 NTYIGDLLRILGIE--NIAAELSGSEYAPI---SFEAILSSNPDVIIVSGRDSFTKTgPEFVAANP-------LWAGLPA 221
|
....*.
gi 578584380 289 VKNNQV 294
Cdd:pfam01497 222 VKNGRV 227
|
|
| TroA-like |
cd00636 |
Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function ... |
54-200 |
8.70e-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: 94.93 E-value: 8.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578584380 54 KRVVTLYQGATDVAVSLG--VKPVGAVESWTQKPKFEYIKNDLKDtkiVGQEPAPNLEEISKLKPDLIVASKVRNEKVYD 131
Cdd:cd00636 1 KRVVALDPGATELLLALGgdDKPVGVADPSGYPPEAKALLEKVPD---VGHGYEPNLEKIAALKPDLIIANGSGLEAWLD 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578584380 132 QLSKIA-PTVSTDTVFKF-----KDTTKLMGKALGKEKEAEDLLKKYDDKVAafqkDAKAKYKDAWPLKASVVNF 200
Cdd:cd00636 78 KLSKIAiPVVVVDEASELsleniKESIRLIGKALGKEENAEELIAELDARLA----ELRAKLAKIPKKKVSLVVG 148
|
|
| PRK10957 |
PRK10957 |
iron-enterobactin transporter periplasmic binding protein; Provisional |
11-294 |
3.75e-18 |
|
iron-enterobactin transporter periplasmic binding protein; Provisional
Pssm-ID: 236806 [Multi-domain] Cd Length: 317 Bit Score: 83.48 E-value: 3.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578584380 11 TLAFLLVLAGCSGNSNKQSSDNKdkettSIKHAMGTTEIKGKPKRVVTlyqgaTDVAVS---LGVK-PVgaVESWTQKPK 86
Cdd:PRK10957 7 LLLLGLLLSGIAAAQASAAGWPR-----TVTDSRGSVTLESKPQRIVS-----TSVTLTgtlLAIDaPV--IASGATTPN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578584380 87 feyikNDLKDTKIV-----------GQEPA----PNLEEISKLKPDLIVASKVRNE---KVYDQLSKIAPTVSTDTVFK- 147
Cdd:PRK10957 75 -----TRVADDQGFfrqwsdvakerGVEVLyigePDAEAVAAQMPDLIVISATGGDsalALYDQLSAIAPTLVIDYDDKs 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578584380 148 FKDTTKLMGKALGKEKEAEDLLKKYDDKVAAfqkdAKAKYK-DAWPLKASVVNFRADHTRIY-AGGYAGEILNDLGFK-- 223
Cdd:PRK10957 150 WQELATQLGEATGLEKQAAAVIAQFDAQLAE----VKAKITlPPQPVSALVYNGAGHSANLWtPESAQGQLLEQLGFTla 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578584380 224 -RNKDLQKQVDNGK--DIIQLTSKESIPLMNADHIFVVKSDPNAKDAALVKKTesewtsskeWKNLDAVKNNQV 294
Cdd:PRK10957 226 eLPAGLQASTSQGKrhDIIQLGGENLAAGLNGETLFLFAGDDKDADAFLADPL---------LANLPAVQNKQV 290
|
|
| TroA_e |
cd01142 |
Periplasmic binding protein TroA_e. These proteins are predicted to function as initial ... |
46-294 |
7.81e-18 |
|
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: 82.02 E-value: 7.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578584380 46 TTEIKGKPKRVVTLYQGATDVAVSLGVKP--VGAVESWTQKPKFEYIKNDLKDTKIVGQEPAPNLEEISKLKPDLIVASK 123
Cdd:cd01142 17 KVTIPDEVKRIAALWGAGNAVVAALGGGKliVATTSTVQQEPWLYRLAPSLENVATGGTGNDVNIEELLALKPDVVIVWS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578584380 124 VRNEKVYDQLSKIAPTVS-TDTVFK-FKDTTKLMGKALGKEKEAEDLLKKYDDKVAAFQ------KDAKAK---YKDAWP 192
Cdd:cd01142 97 TDGKEAGKAVLRLLNALSlRDAELEeVKLTIALLGELLGRQEKAEALVAYFDDNLAYVAartkklPDSERPrvyYAGPDP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578584380 193 LKA----SVVNFRADHtriyAGGYageilNDLGFKRNKDLqKQVdngkdiiqltSKESIPLMNADHIFVvkSDPNAKDAA 268
Cdd:cd01142 177 LTTdgtgSITNSWIDL----AGGI-----NVASEATKKGS-GEV----------SLEQLLKWNPDVIIV--GNADTKAAI 234
|
250 260
....*....|....*....|....*.
gi 578584380 269 LvkktesewtSSKEWKNLDAVKNNQV 294
Cdd:cd01142 235 L---------ADPRWQNLRAVKNGRV 251
|
|
| YvrC |
cd01143 |
Periplasmic binding protein YvrC. These proteins are predicted to function as initial ... |
51-257 |
3.00e-17 |
|
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: 78.47 E-value: 3.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578584380 51 GKPKRVVTLYQGATDVAVSLGV-KPVGAVESWTQKPKfeyiknDLKDTKIVGQEPAPNLEEISKLKPDLIVASKVRNEKV 129
Cdd:cd01143 1 KEPERIVSLSPSITEILFALGAgDKIVGVDTYSNYPK------EVRKKPKVGSYSNPNVEKIVALKPDLVIVSSSSLAEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578584380 130 YDQLSKIA-PTVSTDTVFKFKDTTKLM---GKALGKEKEAEDLLKKYDDKVAAFQKDAKAKYKdawplkaSVVNFRADHT 205
Cdd:cd01143 75 LEKLKDAGiPVVVLPAASSLDEIYDQIeliGKITGAEEEAEKLVKEMKQKIDKVKDKGKTIKK-------SKVYIEVSLG 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 578584380 206 RIYAGG---YAGEILNDLGfkrnkdLQKQVDNGKDIIQLtSKESIPLMNADHIFV 257
Cdd:cd01143 148 GPYTAGkntFINELIRLAG------AKNIAADSGGWPQV-SPEEILKANPDVIIL 195
|
|
| IsdE |
TIGR03659 |
heme ABC transporter, heme-binding protein isdE; This family of ABC substrate-binding proteins ... |
3-320 |
3.08e-15 |
|
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: 74.62 E-value: 3.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578584380 3 KVIKMLVVTLAFLLVLAGCSGNSNKQSSDNKdkettsikhamgtteiKGKPKRVVtlyqgATDVAVS-----LGVKPVGA 77
Cdd:TIGR03659 1 KKILSLVLLAVLSLGLTGCSSSKEKSKVSNK----------------KSKEERIV-----ATSVAVTeildkLDLDLVGV 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578584380 78 VESWTQKPKfeyiknDLKDTKIVGQEPAPNLEEISKLKPDLIVAS---KVRNEKVYDQLSKIAPTVSTDTVFKFKDTTKL 154
Cdd:TIGR03659 60 PTSQKTLPK------RYKDVPEVGNPMSPDMEKIKSLKPTVVLSVttlEEDLGPKFKQLGVEATFLNLTSVDGMKKSITE 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578584380 155 MGKALGKEKEAEDLLKKYDDKVAAFQKDAKAKYKdawplkASV-VNFRADHTRIYA--GGYAGEILNDLGfkrnkdlqkq 231
Cdd:TIGR03659 134 LGEKYGREEQAEKLVKEINEKEAEVKKKVKGKKK------PKVlILMGVPGSYLVAteNSYIGDLVKLAG---------- 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578584380 232 vdnGKDIIQLTSKESIPLMNADhifVVKSDPN-------AKDAALVKKTESEWTSSKEWKNLDAVKNNQVSdDLDEITWN 304
Cdd:TIGR03659 198 ---GENVYKGNKQEYLSSNTEY---LLKANPDiilraahGMPDEVKKMFDEEFKTNDIWKHFEAVKNNRVY-DLDEELFG 270
|
330
....*....|....*....
gi 578584380 305 LAGG--YKSSLK-LIDDLY 320
Cdd:TIGR03659 271 MTANlkVAEALDeLKKILY 289
|
|
| HemV-2 |
cd01147 |
Metal binding protein HemV-2. These proteins are predicted to function as initial receptors ... |
59-294 |
4.96e-15 |
|
Metal binding protein HemV-2. These proteins are predicted to function as initial receptors in ABC transport of metal ions. They belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind the metal ion in the cleft between these domains. In addition, these proteins sometimes have a low complexity region containing a metal-binding histidine-rich motif (repetitive HDH sequence).
Pssm-ID: 238567 [Multi-domain] Cd Length: 262 Bit Score: 73.91 E-value: 4.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578584380 59 LYQGATDVAVSlgvkpVGAVESWTQKPKFEYIKNDLKDTKIVGQE---PAPNLEEISKLKPDLIVASK-VRNEKVYDQLS 134
Cdd:cd01147 20 YALAAPDKIVG-----VDDAEKSDEGRPYFLASPELKDLPVIGRGgrgNTPNYEKIAALKPDVVIDVGsDDPTSIADDLQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578584380 135 KIA--PTVSTDTVFKFKDTT---KLMGKALGKEKEAEDLLKKYDDKvaafQKDAKAKYKDawpLKASvvnfraDHTRIYA 209
Cdd:cd01147 95 KKTgiPVVVLDGGDSLEDTPeqiRLLGKVLGKEERAEELISFIESI----LADVEERTKD---IPDE------EKPTVYF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578584380 210 GG---------YAGEILNDLGFKRN--KDLQKqVDNGKDIIQLtSKESIPLMNADHIFVVksdpnakDAALVKKTESEWT 278
Cdd:cd01147 162 GRigtkgaaglESGLAGSIEVFELAggINVAD-GLGGGGLKEV-SPEQILLWNPDVIFLD-------TGSFYLSLEGYAK 232
|
250
....*....|....*.
gi 578584380 279 SSKEWKNLDAVKNNQV 294
Cdd:cd01147 233 NRPFWQSLKAVKNGRV 248
|
|
| PRK10576 |
PRK10576 |
Fe(3+)-hydroxamate ABC transporter substrate-binding protein FhuD; |
53-223 |
7.64e-10 |
|
Fe(3+)-hydroxamate ABC transporter substrate-binding protein FhuD;
Pssm-ID: 236719 Cd Length: 292 Bit Score: 58.87 E-value: 7.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578584380 53 PKRVVTLYQGATDVAVSLGVKPVGAVES-----WTQKPKfeyikndLKDTKI-VGQEPAPNLEEISKLKPDLIVASKVRN 126
Cdd:PRK10576 32 PNRIVALEWLPVELLLALGVTPYGVADThnyrlWVSEPA-------LPDSVIdVGLRTEPNLELLTQMKPSLILWSAGYG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578584380 127 EKVyDQLSKIAPTVStdtvFKFKDTTK----------LMGKALGKEKEAEDLLKKYDDKVAAfQKDAKAKYKDAWPLKAS 196
Cdd:PRK10576 105 PSP-EKLARIAPGRG----FAFSDGKKplavarkslvELAQRLNLEAAAETHLAQFDDFIAS-AKPRLAGRGQRPLLLTS 178
|
170 180
....*....|....*....|....*...
gi 578584380 197 VVNFRadHTRIY-AGGYAGEILNDLGFK 223
Cdd:PRK10576 179 LIDPR--HALVFgPNSLFQEVLDELGIE 204
|
|
| TroA_a |
cd01148 |
Metal binding protein TroA_a. These proteins are predicted to function as initial receptors ... |
50-294 |
3.63e-08 |
|
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: 53.88 E-value: 3.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578584380 50 KGKPKRVVTLYQGATDVAVSLGVKP--VG-AVESWTQKPKFeyiKNDLKDTKIVGQEpAPNLEEISKLKPDLIVAS---- 122
Cdd:cd01148 15 DKAPQRVVSNDQNTTEMMLALGLQDrmVGtAGIDNKDLPEL---KAKYDKVPELAKK-YPSKETVLAARPDLVFGGwsyg 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578584380 123 ------------KVRNEKVYDQLSKIAPTVSTDTVFKFKDTTKLMGKALGKEKEAEDLLKKYDDKVAAFQKDAKAKYKda 190
Cdd:cd01148 91 fdkgglgtpdslAELGIKTYILPESCGQRRGEATLDDVYNDIRNLGKIFDVEDRADKLVADLKARLAEISAKVKGDGK-- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578584380 191 wplKASVVNF-RADHTRIYAGGYA--GEILNDLGfKRN--KDLQKQVDNgkdiiqlTSKESIPLMNADHIFVVKSDPNAK 265
Cdd:cd01148 169 ---KVAVFVYdSGEDKPFTSGRGGipNAIITAAG-GRNvfADVDESWTT-------VSWETVIARNPDVIVIIDYGDQNA 237
|
250 260
....*....|....*....|....*....
gi 578584380 266 DAALVKktesEWTSSKEWKNLDAVKNNQV 294
Cdd:cd01148 238 AEQKIK----FLKENPALKNVPAVKNNRF 262
|
|
| BtuF |
cd01144 |
Cobalamin binding protein BtuF. These proteins have been shown to function as initial ... |
54-294 |
7.88e-08 |
|
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: 52.30 E-value: 7.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578584380 54 KRVVTLYQGATDVAVSLGV--KPVGAVeSWTQKPKfeyiknDLKDTKIVGQEPAPNLEEISKLKPDLIVASKVRN-EKVY 130
Cdd:cd01144 1 MRIVSLAPSATELLYALGLgdQLVGVT-DYCDYPP------EAKKLPRVGGFYQLDLERVLALKPDLVIAWDDCNvCAVV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578584380 131 DQLSKIAPTVSTDTVFKFKD---TTKLMGKALGKEKEAEDLLKKYDDKVAAFQKDAKAK-----YKDAW--PLKASvvnf 200
Cdd:cd01144 74 DQLRAAGIPVLVSEPQTLDDilaDIRRLGTLAGRPARAEELAEALRRRLAALRKQYASKppprvFYQEWidPLMTA---- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578584380 201 radhtriyAGGYAGEILNDLGfkrnkdlqkqvdnGKDIIQL-------TSKESIPLMNADHIfVVKSDPNAKDAALVKKt 273
Cdd:cd01144 150 --------GGDWVPELIALAG-------------GVNVFADagerspqVSWEDVLAANPDVI-VLSPCGFGFTPAILRK- 206
|
250 260
....*....|....*....|.
gi 578584380 274 eseWtssKEWKNLDAVKNNQV 294
Cdd:cd01144 207 ---E---PAWQALPAVRNGRV 221
|
|
| ChuT |
COG4558 |
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism] ... |
43-257 |
1.00e-07 |
|
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443619 [Multi-domain] Cd Length: 285 Bit Score: 52.50 E-value: 1.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578584380 43 AMGTTEIKGKPKRVVTLYQGATDVAVSLGVKP-VGAVESWTQKPKfeyiknDLKDTKIVGQEPAPNLEEISKLKPDLIVA 121
Cdd:COG4558 17 AAGASVAAAAAERIVSLGGSVTEIVYALGAGDrLVGVDTTSTYPA------AAKALPDVGYMRQLSAEGILSLKPTLVLA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578584380 122 S-KVRNEKVYDQL--SKIaPTV---STDTVFKFKDTTKLMGKALGKEKEAEDLLKKYDDKVAAFQKDAKAKYKdawPLKA 195
Cdd:COG4558 91 SeGAGPPEVLDQLraAGV-PVVvvpAAPSLEGVLAKIRAVAAALGVPEAGEALAARLEADLAALAARVAAIGK---PPRV 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578584380 196 SVVnFRADHTRIYAGG---YAGEILNDLG-------FKRNKDLqkqvdngkdiiqltSKESIPLMNADHIFV 257
Cdd:COG4558 167 LFL-LSRGGGRPMVAGrgtAADALIRLAGgvnaaagFEGYKPL--------------SAEALIAAAPDVILV 223
|
|
| HutB |
cd01149 |
Hemin binding protein HutB. These proteins have been shown to function as initial receptors ... |
53-188 |
3.54e-06 |
|
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: 47.26 E-value: 3.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578584380 53 PKRVVTLYQGATDVAVSLGV-KPVGAVESWTQKPKfeyiknDLKDTKIVGQEPAPNLEEISKLKPDLIVASKVRNEK-VY 130
Cdd:cd01149 1 PERIVSLGGSVTEIVYALGAgDRLVGVDSTSTYPE------AAAKLPDVGYMRQLSAEGVLSLKPTLVIASDEAGPPeAL 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578584380 131 DQLSKIAPTV----STDTVFKFKDTTKLMGKALGKEKEAEDLLKKYDDKVAAFQKDAKAKYK 188
Cdd:cd01149 75 DQLRAAGVPVvtvpSTPTLDGLLTKIRQVAQALGVPEKGEALAQEVRQRLAALRKTVAAHKK 136
|
|
| TroA_f |
cd01139 |
Periplasmic binding protein TroA_f. These proteins are predicted to function as initial ... |
46-294 |
5.41e-05 |
|
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: 44.22 E-value: 5.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578584380 46 TTEIKGKPKRVVtLYQGATDVAVSL--GVKPVGAVESWTQK---------PKFEYIKNDLKDTKIVGQEPAP--NLEEIS 112
Cdd:cd01139 10 KVTLDAPVERVL-LGEGRQLYALALleGENPFARIVGWGGDlkkgdpdtyAKYKEKFPEIADIPLIGSTYNGdfSVEKVL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578584380 113 KLKPDLIV----ASKVRNEKVYDQLSKIA--PTVSTDtvFKFK------DTTKLMGKALGKEKEAEDLLKKYDDKVAAF- 179
Cdd:cd01139 89 TLKPDLVIlniwAKTTAEESGILEKLEQAgiPVVFVD--FRQKplknttPSMRLLGKALGREERAEEFIEFYQERIDRIr 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578584380 180 QKDAKAKykdawPLKASVVNFRA-----DHTRIYAGGYAGEILNDLGfkrnkdlqkqVDN-GKDIIQLTSKESIP--LMN 251
Cdd:cd01139 167 DRLAKIN-----EPKPKVFIELGaggpeECCSTYGNGNWGELVDAAG----------GDNiADGLIPGTSGELNAeyVIA 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 578584380 252 ADHIFVVKSDPN-AKDA------ALVKKTESEWTSSKE------WKNLDAVKNNQV 294
Cdd:cd01139 232 ANPEIIIATGGNwAKDPsgvslgPDGTTADAKESLLRAllkrpgWSSLQAVKNGRV 287
|
|
| PRK14048 |
PRK14048 |
ferrichrome/ferrioxamine B periplasmic transporter; Provisional |
39-192 |
5.52e-05 |
|
ferrichrome/ferrioxamine B periplasmic transporter; Provisional
Pssm-ID: 172540 [Multi-domain] Cd Length: 374 Bit Score: 44.50 E-value: 5.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578584380 39 SIKHAMGTTEIKGKPKRVVTLYQGATDVAVSL-GVKPVGAVESWTQKPK------FEYIKN---DLKDTKIV--GQEPAP 106
Cdd:PRK14048 33 TVTDAVGREVTIPAPPKAVLLGSGFNLIALSLiHPDPVSLLAGWSGDMKgdnpeiYESFLRkfpELADVPLIddGSGPGL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578584380 107 NLEEISKLKPDLIVAS--KVRNE---KVYDQLSKIA-PTVSTD----TVFKFKDTTKLMGKALGKEKEAEDLLKKYDDKV 176
Cdd:PRK14048 113 SFETILTLKADLAILAnwQADTEagqRAIEYLESIGvPVIVVDfnneALKNTPDNMRLLGKVFEREEQAEDFARFYEERL 192
|
170
....*....|....*.
gi 578584380 177 AAFqKDAKAKYKDAWP 192
Cdd:PRK14048 193 ARI-RDRVAKHSEPGP 207
|
|
| PRK03379 |
PRK03379 |
vitamin B12-transporter protein BtuF; Provisional |
55-134 |
4.16e-04 |
|
vitamin B12-transporter protein BtuF; Provisional
Pssm-ID: 179575 [Multi-domain] Cd Length: 260 Bit Score: 41.21 E-value: 4.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578584380 55 RVVTLYQGATDVAVSLGVKPVgAVESWTQKPKfeyiknDLKDTKIVGQEPAPNLEEISKLKPDLIVASKVRN-EKVYDQL 133
Cdd:PRK03379 19 RVITLSPANTELAFAAGITPV-GVSSYSDYPP------QAKKIEQVATWQGMNLERIVALKPDLVLAWRGGNaERQVDQL 91
|
.
gi 578584380 134 S 134
Cdd:PRK03379 92 A 92
|
|
| TroA_d |
cd01141 |
Periplasmic binding protein TroA_d. These proteins are predicted to function as initial ... |
49-140 |
4.57e-04 |
|
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: 40.48 E-value: 4.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578584380 49 IKGKPKRVVTLYQGATDVAVSLGV--KPVGAveswtqkPKFEYIKNDLKDTKI----VGQEPAPNLEEISKLKPDLIVAS 122
Cdd:cd01141 4 IKVPPKRIVVLSPTHVDLLLALDKadKIVGV-------SASAYDLNTPAVKERidiqVGPTGSLNVELIVALKPDLVILY 76
|
90
....*....|....*....
gi 578584380 123 KVRN-EKVYDQLSKIAPTV 140
Cdd:cd01141 77 GGFQaQTILDKLEQLGIPV 95
|
|
| |
