|
Name |
Accession |
Description |
Interval |
E-value |
| FecB |
COG4594 |
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and ... |
1-325 |
1.28e-131 |
|
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443650 [Multi-domain] Cd Length: 316 Bit Score: 377.34 E-value: 1.28e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239366356 1 MKKhISMLFVFLMTLVVLSACNSSESSSNSEESNSKTRTVKHAMGTSdNIPANPKRIVVLTNEGTEALLALGIKPVGAVK 80
Cdd:COG4594 1 MKK-LLLLLILLLALLLLAACGSSSSDSSSSEAAAGARTVKHAMGET-TIPGTPKRVVVLEWSFADALLALGVTPVGIAD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239366356 81 SWKGDPWYDYLKDDMKGVQNVGLETEPNVEAIAELKPDLIIGNKVRQEKIYDQLNAIAPTVFAESLAGNWKDNLT---LY 157
Cdd:COG4594 79 DNDYDRWVPYLRDLIKGVTSVGTRSQPNLEAIAALKPDLIIADKSRHEAIYDQLSKIAPTVLFKSRNGDYQENLEsfkTI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239366356 158 ANAVNKADKGKKAIADFDKRAADLKEKLGDQI-NKTVSVVRFLSGESRIYYTDSFSGIILDQLGFKRPEKQVElfkkqKD 236
Cdd:COG4594 159 AKALGKEEEAEAVLADHDQRIAEAKAKLAAADkGKKVAVGQFRADGLRLYTPNSFAGSVLAALGFENPPKQSK-----DN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239366356 237 QFTFSTDSKESIPDMDADVLFYFTYKadnakeNEKWANQWTSSSLWKNLKAVKSGNAHEVDDVVWTTAGGIKAANYLLDD 316
Cdd:COG4594 234 GYGYSEVSLEQLPALDPDVLFIATYD------DPSILKEWKNNPLWKNLKAVKNGRVYEVDGDLWTRGRGPLAAELMADD 307
|
....*....
gi 1239366356 317 IETYFLKTK 325
Cdd:COG4594 308 LVEILLKKK 316
|
|
| FhuD |
cd01146 |
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial ... |
52-315 |
1.47e-104 |
|
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: 306.52 E-value: 1.47e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239366356 52 ANPKRIVVLTNEGTEALLALGIKPVGAVKSWKGDPWYDYLKDDMKGVQNVGLETEPNVEAIAELKPDLIIGNKVRQEKIY 131
Cdd:cd01146 1 AKPQRIVALDWGALETLLALGVKPVGVADTAGYKPWIPEPALPLEGVVDVGTRGQPNLEAIAALKPDLILGSASRHDEIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239366356 132 DQLNAIAPTVFAESLA--GNWKDNLTLYANAVNKADKGKKAIADFDKRAADLKEKLGDQINKTVSVVRFL-SGESRIYYT 208
Cdd:cd01146 81 DQLSQIAPTVLLDSSPwlAEWKENLRLIAKALGKEEEAEKLLAEYDQRLAELRQKLPDKGPKPVSVVRFSdAGSIRLYGP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239366356 209 DSFSGIILDQLGFKRPEKQvelfkKQKDQFTFSTDSKESIPDMDADVLFYFTYkadnakENEKWANQWTSSSLWKNLKAV 288
Cdd:cd01146 161 NSFAGSVLEDLGLQNPWAQ-----ETTNDSGFATISLERLAKADADVLFVFTY------EDEELAQALQANPLWQNLPAV 229
|
250 260
....*....|....*....|....*..
gi 1239366356 289 KSGNAHEVDDVVWTTAGGIKAANYLLD 315
Cdd:cd01146 230 KNGRVYVVDDVWWFFGGGLSAARLLLD 256
|
|
| fecB |
PRK11411 |
iron-dicitrate transporter substrate-binding subunit; Provisional |
36-321 |
3.89e-33 |
|
iron-dicitrate transporter substrate-binding subunit; Provisional
Pssm-ID: 183123 [Multi-domain] Cd Length: 303 Bit Score: 124.02 E-value: 3.89e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239366356 36 KTRTVKHAMGTSdNIPANPKRIVVLTNEGTEALLALGIKPVGAVKSwkGDP--WYDYLKDDMKGVQNVGLETEPNVEAIA 113
Cdd:PRK11411 22 FAVTVQDEQGTF-TLEKTPQRIVVLELSFVDALAAVGVSPVGVADD--NDAkrILPEVRAHLKPWQSVGTRSQPSLEAIA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239366356 114 ELKPDLIIGNKVRQEKIYDQLNAIAPTVFAESLAGNWKDNL---TLYANAVNKADKGKKAIADFDKRAADLKEklgdQIN 190
Cdd:PRK11411 99 ALKPDLIIADSSRHAGVYIALQKIAPTLLLKSRNETYQENLqsaAIIGEVLGKKREMQARIEQHKERMAQFAS----QLP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239366356 191 KTVSVVrFlsGESR-----IYYTDSFSGIILDQLGFKRPekqvelfKKQKDQFTFSTDSKESIPDMDADVLFYFTYKadn 265
Cdd:PRK11411 175 KGTRVA-F--GTSReqqfnLHSPESYTGSVLAALGLNVP-------KAPMNGAAMPSISLEQLLALNPDWLLVAHYR--- 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1239366356 266 akeNEKWANQWTSSSLWKNLKAVKSGNAHEVDDVVWTTAGGIKAANYLLDDIETYF 321
Cdd:PRK11411 242 ---QESIVKRWQQDPLWQMLTAAKKQQVASVDSNTWARMRGIFAAERIAKDTVKIF 294
|
|
| Peripla_BP_2 |
pfam01497 |
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ... |
58-298 |
2.42e-31 |
|
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: 117.47 E-value: 2.42e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239366356 58 VVLTNEGTEALLALGI-KPVGAVKSWKGDPWYDYLKDDmkgVQNVGLETEPNVEAIAELKPDLIIG-NKVRQEKIYDQLN 135
Cdd:pfam01497 1 AALSPAYTEILYALGAtDSIVGVDAYTRDPLKADAVAA---IVKVGAYGEINVERLAALKPDLVILsTGYLTDEAEELLS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239366356 136 AIAPTVFAESL--AGNWKDNLTLYANAVNKADKGKKAIADFDKRAADLKEKLGDQINKTVSVvrFLSGESRIYY---TDS 210
Cdd:pfam01497 78 LIIPTVIFESSstGESLKEQIKQLGELLGLEDEAEELVAEIDSALAAAKKAVPSLTRKPVLV--FGGADGGGYVvagSNT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239366356 211 FSGIILDQLGFKRPekQVELFKKQKDQFtfstdSKESIPDMDADVLFYFTYKADNAKENEKWAnqwtSSSLWKNLKAVKS 290
Cdd:pfam01497 156 YIGDLLRILGIENI--AAELSGSEYAPI-----SFEAILSSNPDVIIVSGRDSFTKTGPEFVA----ANPLWAGLPAVKN 224
|
....*...
gi 1239366356 291 GNAHEVDD 298
Cdd:pfam01497 225 GRVYTLPS 232
|
|
| IsdE |
TIGR03659 |
heme ABC transporter, heme-binding protein isdE; This family of ABC substrate-binding proteins ... |
2-321 |
3.01e-09 |
|
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: 56.90 E-value: 3.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239366356 2 KKHISMLFVFLMtLVVLSACNSSESSSnseesnsktrtvkhamgTSDNIPANPKRIVVLTNEGTEALLALGIKPVGAVKS 81
Cdd:TIGR03659 1 KKILSLVLLAVL-SLGLTGCSSSKEKS-----------------KVSNKKSKEERIVATSVAVTEILDKLDLDLVGVPTS 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239366356 82 WKGDPwydylkDDMKGVQNVGLETEPNVEAIAELKPDLIIGNKVRQEKIYDQLNAIA-PTVFA--ESLAGnWKDNLTLYA 158
Cdd:TIGR03659 63 QKTLP------KRYKDVPEVGNPMSPDMEKIKSLKPTVVLSVTTLEEDLGPKFKQLGvEATFLnlTSVDG-MKKSITELG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239366356 159 NAVNKADKGKKAIADFDKRAADLKEKLGDQINKTVSVVRFLSGESRIYYTDSFSGIILDQLGfkrpekQVELFKKQKDQF 238
Cdd:TIGR03659 136 EKYGREEQAEKLVKEINEKEAEVKKKVKGKKKPKVLILMGVPGSYLVATENSYIGDLVKLAG------GENVYKGNKQEY 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239366356 239 -TFSTdskESIPDMDADVLFYfTYKA--DNAKE--NEKWAnqwtSSSLWKNLKAVKSGNAHEVDDVVWTTAGGIKAANyL 313
Cdd:TIGR03659 210 lSSNT---EYLLKANPDIILR-AAHGmpDEVKKmfDEEFK----TNDIWKHFEAVKNNRVYDLDEELFGMTANLKVAE-A 280
|
....*...
gi 1239366356 314 LDDIETYF 321
Cdd:TIGR03659 281 LDELKKIL 288
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| FecB |
COG4594 |
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and ... |
1-325 |
1.28e-131 |
|
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443650 [Multi-domain] Cd Length: 316 Bit Score: 377.34 E-value: 1.28e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239366356 1 MKKhISMLFVFLMTLVVLSACNSSESSSNSEESNSKTRTVKHAMGTSdNIPANPKRIVVLTNEGTEALLALGIKPVGAVK 80
Cdd:COG4594 1 MKK-LLLLLILLLALLLLAACGSSSSDSSSSEAAAGARTVKHAMGET-TIPGTPKRVVVLEWSFADALLALGVTPVGIAD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239366356 81 SWKGDPWYDYLKDDMKGVQNVGLETEPNVEAIAELKPDLIIGNKVRQEKIYDQLNAIAPTVFAESLAGNWKDNLT---LY 157
Cdd:COG4594 79 DNDYDRWVPYLRDLIKGVTSVGTRSQPNLEAIAALKPDLIIADKSRHEAIYDQLSKIAPTVLFKSRNGDYQENLEsfkTI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239366356 158 ANAVNKADKGKKAIADFDKRAADLKEKLGDQI-NKTVSVVRFLSGESRIYYTDSFSGIILDQLGFKRPEKQVElfkkqKD 236
Cdd:COG4594 159 AKALGKEEEAEAVLADHDQRIAEAKAKLAAADkGKKVAVGQFRADGLRLYTPNSFAGSVLAALGFENPPKQSK-----DN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239366356 237 QFTFSTDSKESIPDMDADVLFYFTYKadnakeNEKWANQWTSSSLWKNLKAVKSGNAHEVDDVVWTTAGGIKAANYLLDD 316
Cdd:COG4594 234 GYGYSEVSLEQLPALDPDVLFIATYD------DPSILKEWKNNPLWKNLKAVKNGRVYEVDGDLWTRGRGPLAAELMADD 307
|
....*....
gi 1239366356 317 IETYFLKTK 325
Cdd:COG4594 308 LVEILLKKK 316
|
|
| FhuD |
cd01146 |
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial ... |
52-315 |
1.47e-104 |
|
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: 306.52 E-value: 1.47e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239366356 52 ANPKRIVVLTNEGTEALLALGIKPVGAVKSWKGDPWYDYLKDDMKGVQNVGLETEPNVEAIAELKPDLIIGNKVRQEKIY 131
Cdd:cd01146 1 AKPQRIVALDWGALETLLALGVKPVGVADTAGYKPWIPEPALPLEGVVDVGTRGQPNLEAIAALKPDLILGSASRHDEIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239366356 132 DQLNAIAPTVFAESLA--GNWKDNLTLYANAVNKADKGKKAIADFDKRAADLKEKLGDQINKTVSVVRFL-SGESRIYYT 208
Cdd:cd01146 81 DQLSQIAPTVLLDSSPwlAEWKENLRLIAKALGKEEEAEKLLAEYDQRLAELRQKLPDKGPKPVSVVRFSdAGSIRLYGP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239366356 209 DSFSGIILDQLGFKRPEKQvelfkKQKDQFTFSTDSKESIPDMDADVLFYFTYkadnakENEKWANQWTSSSLWKNLKAV 288
Cdd:cd01146 161 NSFAGSVLEDLGLQNPWAQ-----ETTNDSGFATISLERLAKADADVLFVFTY------EDEELAQALQANPLWQNLPAV 229
|
250 260
....*....|....*....|....*..
gi 1239366356 289 KSGNAHEVDDVVWTTAGGIKAANYLLD 315
Cdd:cd01146 230 KNGRVYVVDDVWWFFGGGLSAARLLLD 256
|
|
| FeuA |
cd01138 |
Periplasmic binding protein FeuA. These proteins have predicted to function as initial ... |
49-305 |
2.59e-56 |
|
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: 182.92 E-value: 2.59e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239366356 49 NIPANPKRIVVLTNEGTEALLaLGIKPVGAVKswKGDPWYDYLKDDMKGVqnVGLETEPNVEAIAELKPDLIIGNKvRQE 128
Cdd:cd01138 4 EIPAKPKRIVALSGETEGLAL-LGIKPVGAAS--IGGKNPYYKKKTLAKV--VGIVDEPNLEKVLELKPDLIIVSS-KQE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239366356 129 KIYDQLNAIAPTVFAESLAGNWKDNLTLYANAVNKADKGKKAIADFDKRAADLKEKLGDQINKTVSV-VRFLSGESRIYY 207
Cdd:cd01138 78 ENYEKLSKIAPTVPVSYNSSDWEEQLKEIGKLLNKEDEAEKWLADYKQKAKEAKEKIKKKLGNDKSVaVLRGRKQIYVFG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239366356 208 TDS-FSGIILDQ-LGFKRPEKQVELFKKQkdqfTFSTDSKESIPDMDADVLFYFTYKADNAKENEKwanqwtSSSLWKNL 285
Cdd:cd01138 158 EDGrGGGPILYAdLGLKAPEKVKEIEDKP----GYAAISLEVLPEFDADYIFLLFFTGPEAKADFE------SLPIWKNL 227
|
250 260
....*....|....*....|.
gi 1239366356 286 KAVKSGNAHEVD-DVVWTTAG 305
Cdd:cd01138 228 PAVKNNHVYIVDaWVFYFADG 248
|
|
| FepB |
COG0614 |
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ... |
56-305 |
7.63e-50 |
|
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 440379 [Multi-domain] Cd Length: 264 Bit Score: 166.71 E-value: 7.63e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239366356 56 RIVVLTNEGTEALLALGIKP--VGAVkswkGDPWYDYLKDDMKGVQNVGLETEPNVEAIAELKPDLIIGNKV-RQEKIYD 132
Cdd:COG0614 2 RIVSLSPSATELLLALGAGDrlVGVS----DWGYCDYPELELKDLPVVGGTGEPNLEAILALKPDLVLASSSgNDEEDYE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239366356 133 QLNAI-APTVF--AESLAgNWKDNLTLYANAVNKADKGKKAIADFDKRAADLKEKLGDQINKTVSVVRFLSGES-RIYYT 208
Cdd:COG0614 78 QLEKIgIPVVVldPRSLE-DLYESIRLLGELLGREERAEALIAEYEARLAAVRARLAGAEERPTVLYEIWSGDPlYTAGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239366356 209 DSFSGIILDQLGFKRpekqveLFKKQKDqfTFSTDSKESIPDMDADVLFYFTYKADNAKENEKwANQWTSSSLWKNLKAV 288
Cdd:COG0614 157 GSFIGELLELAGGRN------VAADLGG--GYPEVSLEQVLALDPDVIILSGGGYDAETAEEA-LEALLADPGWQSLPAV 227
|
250
....*....|....*..
gi 1239366356 289 KSGNAHEVDDVVWTTAG 305
Cdd:COG0614 228 KNGRVYVVPGDLLSRPG 244
|
|
| CeuA |
COG4607 |
ABC-type enterochelin transport system, periplasmic component [Inorganic ion transport and ... |
1-318 |
2.90e-40 |
|
ABC-type enterochelin transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443657 [Multi-domain] Cd Length: 310 Bit Score: 143.01 E-value: 2.90e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239366356 1 MKKHIsMLFVFLMTLVVLSACNSSESSSNSEESNsKTRTVKHAMGTSDnIPANPKRIVVLTNEGTEALLALGIKPVGAVK 80
Cdd:COG4607 1 MKKTL-LAALALAAALALAACGSSSAAAASAAAA-ETVTVEHALGTVE-VPKNPKRVVVFDNGALDTLDALGVEVAGVPK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239366356 81 swkgDPWYDYLKD-DMKGVQNVGLETEPNVEAIAELKPDLIIgNKVRQEKIYDQLNAIAPTVF----AESLAGNWKDNLT 155
Cdd:COG4607 78 ----GLLPDYLSKyADDKYANVGTLFEPDLEAIAALKPDLII-IGGRSAKKYDELSKIAPTIDltvdGEDYLESLKRNTE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239366356 156 LYANAVNKADKGKKAIADFDKRAADLKEKLGDqiNKTVSVVRFLSGESRIYYTDSFSGIILDQLGFKrpekqvELFKKQK 235
Cdd:COG4607 153 TLGEIFGKEDEAEELVADLDAKIAALKAAAAG--KGTALIVLTNGGKISAYGPGSRFGPIHDVLGFK------PADEDIE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239366356 236 -----DQFTFstdskESIPDMDADVLFYFtyKADNAKENEKWANQWTSSS-LWKNLKAVKSGNAHEVDDVVW-TTAGGIK 308
Cdd:COG4607 225 asthgQAISF-----EFIAEANPDWLFVI--DRDAAIGGEGPAAKQVLDNeLVKQTTAWKNGQIVYLDPDAWyLAGGGIQ 297
|
330
....*....|
gi 1239366356 309 AANYLLDDIE 318
Cdd:COG4607 298 SLTEMLDEVA 307
|
|
| fecB |
PRK11411 |
iron-dicitrate transporter substrate-binding subunit; Provisional |
36-321 |
3.89e-33 |
|
iron-dicitrate transporter substrate-binding subunit; Provisional
Pssm-ID: 183123 [Multi-domain] Cd Length: 303 Bit Score: 124.02 E-value: 3.89e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239366356 36 KTRTVKHAMGTSdNIPANPKRIVVLTNEGTEALLALGIKPVGAVKSwkGDP--WYDYLKDDMKGVQNVGLETEPNVEAIA 113
Cdd:PRK11411 22 FAVTVQDEQGTF-TLEKTPQRIVVLELSFVDALAAVGVSPVGVADD--NDAkrILPEVRAHLKPWQSVGTRSQPSLEAIA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239366356 114 ELKPDLIIGNKVRQEKIYDQLNAIAPTVFAESLAGNWKDNL---TLYANAVNKADKGKKAIADFDKRAADLKEklgdQIN 190
Cdd:PRK11411 99 ALKPDLIIADSSRHAGVYIALQKIAPTLLLKSRNETYQENLqsaAIIGEVLGKKREMQARIEQHKERMAQFAS----QLP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239366356 191 KTVSVVrFlsGESR-----IYYTDSFSGIILDQLGFKRPekqvelfKKQKDQFTFSTDSKESIPDMDADVLFYFTYKadn 265
Cdd:PRK11411 175 KGTRVA-F--GTSReqqfnLHSPESYTGSVLAALGLNVP-------KAPMNGAAMPSISLEQLLALNPDWLLVAHYR--- 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1239366356 266 akeNEKWANQWTSSSLWKNLKAVKSGNAHEVDDVVWTTAGGIKAANYLLDDIETYF 321
Cdd:PRK11411 242 ---QESIVKRWQQDPLWQMLTAAKKQQVASVDSNTWARMRGIFAAERIAKDTVKIF 294
|
|
| FatB |
cd01140 |
Siderophore binding protein FatB. These proteins have been shown to function as ABC-type ... |
42-308 |
9.52e-32 |
|
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: 119.67 E-value: 9.52e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239366356 42 HAMGTSdNIPANPKRIVVLTNEGTEALLALGIKPVGAVKSWKGDPWYDYLKDDmkGVQNVGLETEPNVEAIAELKPDLII 121
Cdd:cd01140 1 HALGET-KVPKNPEKVVVFDVGALDTLDALGVKVVGVPKSSTLPEYLKKYKDD--KYANVGTLFEPDLEAIAALKPDLII 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239366356 122 GNKvRQEKIYDQLNAIAPTVF-----AESLAGnWKDNLTLYANAVNKADKGKKAIADFDKRAADLKEKLgdQINKTVSVV 196
Cdd:cd01140 78 IGG-RLAEKYDELKKIAPTIDlgadlKNYLES-VKQNIETLGKIFGKEEEAKELVAEIDASIAEAKSAA--KGKKKALVV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239366356 197 RFLSGESRIYYTDSFSGIILDQLGFKrPEKQVELFKKQKDQFTFstdskESIPDMDADVLFyFTYKADNAKENEKWANQW 276
Cdd:cd01140 154 LVNGGKLSAFGPGSRFGWLHDLLGFE-PADENIKASSHGQPVSF-----EYILEANPDWLF-VIDRGAAIGAEGSSAKEV 226
|
250 260 270
....*....|....*....|....*....|..
gi 1239366356 277 TSSSLWKNLKAVKSGNAHEVDDVVWTTAGGIK 308
Cdd:cd01140 227 LDNDLVKNTTAWKNGKVIYLDPDLWYLSGGGL 258
|
|
| Peripla_BP_2 |
pfam01497 |
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ... |
58-298 |
2.42e-31 |
|
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: 117.47 E-value: 2.42e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239366356 58 VVLTNEGTEALLALGI-KPVGAVKSWKGDPWYDYLKDDmkgVQNVGLETEPNVEAIAELKPDLIIG-NKVRQEKIYDQLN 135
Cdd:pfam01497 1 AALSPAYTEILYALGAtDSIVGVDAYTRDPLKADAVAA---IVKVGAYGEINVERLAALKPDLVILsTGYLTDEAEELLS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239366356 136 AIAPTVFAESL--AGNWKDNLTLYANAVNKADKGKKAIADFDKRAADLKEKLGDQINKTVSVvrFLSGESRIYY---TDS 210
Cdd:pfam01497 78 LIIPTVIFESSstGESLKEQIKQLGELLGLEDEAEELVAEIDSALAAAKKAVPSLTRKPVLV--FGGADGGGYVvagSNT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239366356 211 FSGIILDQLGFKRPekQVELFKKQKDQFtfstdSKESIPDMDADVLFYFTYKADNAKENEKWAnqwtSSSLWKNLKAVKS 290
Cdd:pfam01497 156 YIGDLLRILGIENI--AAELSGSEYAPI-----SFEAILSSNPDVIIVSGRDSFTKTGPEFVA----ANPLWAGLPAVKN 224
|
....*...
gi 1239366356 291 GNAHEVDD 298
Cdd:pfam01497 225 GRVYTLPS 232
|
|
| FepB |
COG4592 |
ABC-type Fe2+-enterobactin transport system, periplasmic component [Inorganic ion transport ... |
8-321 |
3.30e-31 |
|
ABC-type Fe2+-enterobactin transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443649 [Multi-domain] Cd Length: 330 Bit Score: 119.67 E-value: 3.30e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239366356 8 LFVFLMTLVVLSACNSSESSSNSEESNSK---TRTVKHAMGTSDnIPANPKRIVVLTNEGTEALLALGIKPVGAVKSWKG 84
Cdd:COG4592 9 AAALLAAALLLAGCSSADSTASGTSTAAAggwPRTVTTEKGTVT-LPAKPQRIVSTSVTLTGSLLAIDAPVVASGATTPN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239366356 85 DP-----WYDYLKDDMK--GVQNVGLETEPNVEAIAELKPDLIIGNKV---RQEKIYDQLNAIAPTVFAESLAGNWKDNL 154
Cdd:COG4592 88 NVtddqgFFRQWADVAKerGVKRLYIGLEPNAEAIAAAAPDLIIGSATggdSALDLYDQLSAIAPTLVVNYDDKSWQELA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239366356 155 TLYANAVNKADKGKKAIADFDKRAADLKEKLGDQINKTVSVVRFLSGESRIYYTDSFSGIILDQLGFKRPEKQVEL---- 230
Cdd:COG4592 168 TQLGEATGHEAQADAVIAAFDARVAEVKAAITLPPQPVSALVYNEDGGANLWTPESAQGQLLQALGFTLAPLPAELatst 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239366356 231 -FKKQKDQFTFstdSKESIPD-MDADVLFYF---TYKADNAKENekwanqwtssSLWKNLKAVKSGNAHEVDDvvWTTAG 305
Cdd:COG4592 248 sQGKRGDIVQL---SGENLAAaLTGPTLFLFaadDKDVDALKAD----------PLLAHLPAVQAGRVYALGP--DSFRL 312
|
330
....*....|....*.
gi 1239366356 306 GIKAANYLLDDIETYF 321
Cdd:COG4592 313 DYYSASNLLDRLEKLF 328
|
|
| TroA-like |
cd00636 |
Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function ... |
55-198 |
7.24e-30 |
|
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: 111.11 E-value: 7.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239366356 55 KRIVVLTNEGTEALLALG--IKPVGAVKSWKGDPWYDYLKDDmkgVQNVGLETEPNVEAIAELKPDLIIGNKVRQEKIYD 132
Cdd:cd00636 1 KRVVALDPGATELLLALGgdDKPVGVADPSGYPPEAKALLEK---VPDVGHGYEPNLEKIAALKPDLIIANGSGLEAWLD 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1239366356 133 QLNAIAPTVFAESLAG-----NWKDNLTLYANAVNKADKGKKAIADFDKRAADLKEKLGDQINKTVSVVRF 198
Cdd:cd00636 78 KLSKIAIPVVVVDEASelsleNIKESIRLIGKALGKEENAEELIAELDARLAELRAKLAKIPKKKVSLVVG 148
|
|
| PRK10957 |
PRK10957 |
iron-enterobactin transporter periplasmic binding protein; Provisional |
38-222 |
3.86e-17 |
|
iron-enterobactin transporter periplasmic binding protein; Provisional
Pssm-ID: 236806 [Multi-domain] Cd Length: 317 Bit Score: 80.40 E-value: 3.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239366356 38 RTVKHAMGTSdNIPANPKRIV--VLTNEGTeaLLALGIKPVGAVKSWKGDP----------WYDYLKDdmKGVQnVGLET 105
Cdd:PRK10957 29 RTVTDSRGSV-TLESKPQRIVstSVTLTGT--LLAIDAPVIASGATTPNTRvaddqgffrqWSDVAKE--RGVE-VLYIG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239366356 106 EPNVEAIAELKPDLII-----GNKVRQEkiYDQLNAIAPTVFAESLAGNWKDNLTLYANAVNKADKGKKAIADFDKRAAD 180
Cdd:PRK10957 103 EPDAEAVAAQMPDLIVisatgGDSALAL--YDQLSAIAPTLVIDYDDKSWQELATQLGEATGLEKQAAAVIAQFDAQLAE 180
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1239366356 181 LKEKLGDQINKTVSVVRFLSGES-RIYYTDSFSGIILDQLGFK 222
Cdd:PRK10957 181 VKAKITLPPQPVSALVYNGAGHSaNLWTPESAQGQLLEQLGFT 223
|
|
| YvrC |
cd01143 |
Periplasmic binding protein YvrC. These proteins are predicted to function as initial ... |
53-258 |
2.05e-16 |
|
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: 76.16 E-value: 2.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239366356 53 NPKRIVVLTNEGTEALLALGI-KPVGAVkswkgDPWYDYLKDDMKGVQnVGLETEPNVEAIAELKPDLIIGNKVRQEKIY 131
Cdd:cd01143 2 EPERIVSLSPSITEILFALGAgDKIVGV-----DTYSNYPKEVRKKPK-VGSYSNPNVEKIVALKPDLVIVSSSSLAELL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239366356 132 DQLNAIAPTVF----AESLAGNwKDNLTLYANAVNKADKGKKAIADFDKRAADLKEKLgdqINKTVSVVRFLSGESRIYY 207
Cdd:cd01143 76 EKLKDAGIPVVvlpaASSLDEI-YDQIELIGKITGAEEEAEKLVKEMKQKIDKVKDKG---KTIKKSKVYIEVSLGGPYT 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1239366356 208 T--DSFSGIILDQLGFKRPEKQVELFKKQkdqftfstdSKESIPDMDADVLFY 258
Cdd:cd01143 152 AgkNTFINELIRLAGAKNIAADSGGWPQV---------SPEEILKANPDVIIL 195
|
|
| PRK10576 |
PRK10576 |
Fe(3+)-hydroxamate ABC transporter substrate-binding protein FhuD; |
43-185 |
5.54e-14 |
|
Fe(3+)-hydroxamate ABC transporter substrate-binding protein FhuD;
Pssm-ID: 236719 Cd Length: 292 Bit Score: 71.20 E-value: 5.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239366356 43 AMGTSDNIPANPKRIVVLTNEGTEALLALGIKPVGAV-----KSWKGDPwydYLKDdmkGVQNVGLETEPNVEAIAELKP 117
Cdd:PRK10576 21 QMNTAAAAAIDPNRIVALEWLPVELLLALGVTPYGVAdthnyRLWVSEP---ALPD---SVIDVGLRTEPNLELLTQMKP 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1239366356 118 DLII---GNKVRQEKiydqLNAIAPTV-FAESLAGN----WKDNLTLYANAVNKADKGKKAIADFDKRAADLKEKL 185
Cdd:PRK10576 95 SLILwsaGYGPSPEK----LARIAPGRgFAFSDGKKplavARKSLVELAQRLNLEAAAETHLAQFDDFIASAKPRL 166
|
|
| BtuF |
cd01144 |
Cobalamin binding protein BtuF. These proteins have been shown to function as initial ... |
55-182 |
3.10e-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: 65.40 E-value: 3.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239366356 55 KRIVVLTNEGTEALLALGI--KPVGAVKswkgdpWYDYlKDDMKGVQNVGLETEPNVEAIAELKPDLIIGNKVRQEKIY- 131
Cdd:cd01144 1 MRIVSLAPSATELLYALGLgdQLVGVTD------YCDY-PPEAKKLPRVGGFYQLDLERVLALKPDLVIAWDDCNVCAVv 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1239366356 132 DQLNAIAPTVF---AESLAGNWkDNLTLYANAVNKADKGKKAIADFDKRAADLK 182
Cdd:cd01144 74 DQLRAAGIPVLvsePQTLDDIL-ADIRRLGTLAGRPARAEELAEALRRRLAALR 126
|
|
| TroA_a |
cd01148 |
Metal binding protein TroA_a. These proteins are predicted to function as initial receptors ... |
54-289 |
1.25e-11 |
|
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: 64.28 E-value: 1.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239366356 54 PKRIVVLTNEGTEALLALGIKP--VGAVKSWKGD-PwydYLKDDMKGVQNVGlETEPNVEAIAELKPDLIIG-----NKV 125
Cdd:cd01148 18 PQRVVSNDQNTTEMMLALGLQDrmVGTAGIDNKDlP---ELKAKYDKVPELA-KKYPSKETVLAARPDLVFGgwsygFDK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239366356 126 RQEKIYDQLNAIAPTVFAES-----------LAGNWKDnLTLYANAVNKADKGKKAIADFDKRAADLKEKLGDqINKTVS 194
Cdd:cd01148 94 GGLGTPDSLAELGIKTYILPescgqrrgeatLDDVYND-IRNLGKIFDVEDRADKLVADLKARLAEISAKVKG-DGKKVA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239366356 195 VVRFLSGESRIYY--TDSFSGIILDQLGFKrpekqvELFKKQKDQFTfsTDSKESIPDMDADVLFYFTYkaDNAKENEKW 272
Cdd:cd01148 172 VFVYDSGEDKPFTsgRGGIPNAIITAAGGR------NVFADVDESWT--TVSWETVIARNPDVIVIIDY--GDQNAAEQK 241
|
250
....*....|....*..
gi 1239366356 273 ANQWTSSSLWKNLKAVK 289
Cdd:cd01148 242 IKFLKENPALKNVPAVK 258
|
|
| TroA_e |
cd01142 |
Periplasmic binding protein TroA_e. These proteins are predicted to function as initial ... |
37-296 |
5.71e-11 |
|
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: 62.37 E-value: 5.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239366356 37 TRTVKHAMGTSDNIPANPKRIVVLTNEGTEALLALGIKP--VGAVKSWKGDPWYDYLKDDMKGVQNVGLETEPNVEAIAE 114
Cdd:cd01142 7 TRTITDMAGRKVTIPDEVKRIAALWGAGNAVVAALGGGKliVATTSTVQQEPWLYRLAPSLENVATGGTGNDVNIEELLA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239366356 115 LKPDLIIGNKVRQEKIYDQLNAIAPTVFAESLAgnwKDNLTLYANAVNKadkgkkaIADFDKRAADLKEKLGDQINKTVS 194
Cdd:cd01142 87 LKPDVVIVWSTDGKEAGKAVLRLLNALSLRDAE---LEEVKLTIALLGE-------LLGRQEKAEALVAYFDDNLAYVAA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239366356 195 VVRFLSGESR--IYY----------TDSFSGIILDQLGFKRpekqvelFKKQKDQFTFSTDSKESIPDMDADVlfYFTYK 262
Cdd:cd01142 157 RTKKLPDSERprVYYagpdplttdgTGSITNSWIDLAGGIN-------VASEATKKGSGEVSLEQLLKWNPDV--IIVGN 227
|
250 260 270
....*....|....*....|....*....|....
gi 1239366356 263 ADNAKEnekwanqWTSSSLWKNLKAVKSGNAHEV 296
Cdd:cd01142 228 ADTKAA-------ILADPRWQNLRAVKNGRVYVN 254
|
|
| IsdE |
TIGR03659 |
heme ABC transporter, heme-binding protein isdE; This family of ABC substrate-binding proteins ... |
2-321 |
3.01e-09 |
|
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: 56.90 E-value: 3.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239366356 2 KKHISMLFVFLMtLVVLSACNSSESSSnseesnsktrtvkhamgTSDNIPANPKRIVVLTNEGTEALLALGIKPVGAVKS 81
Cdd:TIGR03659 1 KKILSLVLLAVL-SLGLTGCSSSKEKS-----------------KVSNKKSKEERIVATSVAVTEILDKLDLDLVGVPTS 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239366356 82 WKGDPwydylkDDMKGVQNVGLETEPNVEAIAELKPDLIIGNKVRQEKIYDQLNAIA-PTVFA--ESLAGnWKDNLTLYA 158
Cdd:TIGR03659 63 QKTLP------KRYKDVPEVGNPMSPDMEKIKSLKPTVVLSVTTLEEDLGPKFKQLGvEATFLnlTSVDG-MKKSITELG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239366356 159 NAVNKADKGKKAIADFDKRAADLKEKLGDQINKTVSVVRFLSGESRIYYTDSFSGIILDQLGfkrpekQVELFKKQKDQF 238
Cdd:TIGR03659 136 EKYGREEQAEKLVKEINEKEAEVKKKVKGKKKPKVLILMGVPGSYLVATENSYIGDLVKLAG------GENVYKGNKQEY 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239366356 239 -TFSTdskESIPDMDADVLFYfTYKA--DNAKE--NEKWAnqwtSSSLWKNLKAVKSGNAHEVDDVVWTTAGGIKAANyL 313
Cdd:TIGR03659 210 lSSNT---EYLLKANPDIILR-AAHGmpDEVKKmfDEEFK----TNDIWKHFEAVKNNRVYDLDEELFGMTANLKVAE-A 280
|
....*...
gi 1239366356 314 LDDIETYF 321
Cdd:TIGR03659 281 LDELKKIL 288
|
|
| TroA_d |
cd01141 |
Periplasmic binding protein TroA_d. These proteins are predicted to function as initial ... |
50-220 |
1.65e-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: 53.58 E-value: 1.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239366356 50 IPANPKRIVVLTNEGTEALLALGikpvgAVKSWKGDPWYDYLKDD----MKGVQNVGLETEPNVEAIAELKPDLIIGNKV 125
Cdd:cd01141 4 IKVPPKRIVVLSPTHVDLLLALD-----KADKIVGVSASAYDLNTpavkERIDIQVGPTGSLNVELIVALKPDLVILYGG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239366356 126 RQ-EKIYDQLNAIAPTVFAESLAGNWKDNL-----TLYANAVNKADKGKKAIADFDKRAADLKEKLGDQINKTVSVVRFL 199
Cdd:cd01141 79 FQaQTILDKLEQLGIPVLYVNEYPSPLGRAewikfAAAFYGVGKEDKADEAFAQIAGRYRDLAKKVSNLNKPTVAIGKPV 158
|
170 180
....*....|....*....|.
gi 1239366356 200 SGESRIYYTDSFSGIILDQLG 220
Cdd:cd01141 159 KGLWYMPGGNSYVAKMLRDAG 179
|
|
| HemV-2 |
cd01147 |
Metal binding protein HemV-2. These proteins are predicted to function as initial receptors ... |
50-296 |
1.45e-06 |
|
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: 48.87 E-value: 1.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239366356 50 IPANPKRIVVLTNEGTEALLALGI--KPVG---------AVKSWKGDPWYDYLKDDMKGVQNvgleTEPNVEAIAELKPD 118
Cdd:cd01147 1 VPKPVERVVAAGPGALRLLYALAApdKIVGvddaeksdeGRPYFLASPELKDLPVIGRGGRG----NTPNYEKIAALKPD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239366356 119 LII--GNkVRQEKIYDQLNAIA--PTV---FAESLAgNWKDNLTLYANAVNKADKGKKAIADFDKRAADLKE---KLGDQ 188
Cdd:cd01147 77 VVIdvGS-DDPTSIADDLQKKTgiPVVvldGGDSLE-DTPEQIRLLGKVLGKEERAEELISFIESILADVEErtkDIPDE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239366356 189 INKTVSVVRF-LSGESRIYYTDSFSGIILDQLGfkrpekqVELFKKQKDQFTFSTDSKESIPDMDADVLFYFTYKADNAK 267
Cdd:cd01147 155 EKPTVYFGRIgTKGAAGLESGLAGSIEVFELAG-------GINVADGLGGGGLKEVSPEQILLWNPDVIFLDTGSFYLSL 227
|
250 260
....*....|....*....|....*....
gi 1239366356 268 ENEKWANqwtssSLWKNLKAVKSGNAHEV 296
Cdd:cd01147 228 EGYAKNR-----PFWQSLKAVKNGRVYLL 251
|
|
| TroA_f |
cd01139 |
Periplasmic binding protein TroA_f. These proteins are predicted to function as initial ... |
39-296 |
1.92e-06 |
|
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: 48.84 E-value: 1.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239366356 39 TVKHAMGTSDNIPANPKRIVVLTNEGTEALLAL-GIKPVGAVKSWKGD-------PWYDYLKD--DMKGVQNVGLETEP- 107
Cdd:cd01139 2 TVTDVAGRKVTLDAPVERVLLGEGRQLYALALLeGENPFARIVGWGGDlkkgdpdTYAKYKEKfpEIADIPLIGSTYNGd 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239366356 108 -NVEAIAELKPDLIIGNKVRQEKIYD-----QLNAIA-PTV---FAESLAGNWKDNLTLYANAVNKADKGKKAIADFDKR 177
Cdd:cd01139 82 fSVEKVLTLKPDLVILNIWAKTTAEEsgileKLEQAGiPVVfvdFRQKPLKNTTPSMRLLGKALGREERAEEFIEFYQER 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239366356 178 AADLKEKLGdQINKT---VSVVRFLSGESRiyYTDSFS----GIILDQLG--------FKRPEKQV--ELFKKQKDQFTF 240
Cdd:cd01139 162 IDRIRDRLA-KINEPkpkVFIELGAGGPEE--CCSTYGngnwGELVDAAGgdniadglIPGTSGELnaEYVIAANPEIII 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1239366356 241 STDSKeSIPDMDADVLFYFTYKADNAKENEKwanQWTSSSLWKNLKAVKSGNAHEV 296
Cdd:cd01139 239 ATGGN-WAKDPSGVSLGPDGTTADAKESLLR---ALLKRPGWSSLQAVKNGRVYAL 290
|
|
| PRK03379 |
PRK03379 |
vitamin B12-transporter protein BtuF; Provisional |
56-193 |
1.15e-05 |
|
vitamin B12-transporter protein BtuF; Provisional
Pssm-ID: 179575 [Multi-domain] Cd Length: 260 Bit Score: 46.22 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239366356 56 RIVVLTNEGTEALLALGIKPVgAVKSWKgdpwyDYlKDDMKGVQNVGLETEPNVEAIAELKPDLII----GNKVRQekiY 131
Cdd:PRK03379 19 RVITLSPANTELAFAAGITPV-GVSSYS-----DY-PPQAKKIEQVATWQGMNLERIVALKPDLVLawrgGNAERQ---V 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1239366356 132 DQLNAIAPTVFaeslagnWKDNLTL--YANAVNK-------ADKGKKAIADFDKRAADLKEKLGDQINKTV 193
Cdd:PRK03379 89 DQLASLGIKVM-------WVDATSIeqIANALRQlapwspqPEKAEQAAQSLLQQYAALKAQYADKPKKRV 152
|
|
| ChuT |
COG4558 |
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism] ... |
43-199 |
1.79e-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: 1.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239366356 43 AMGTSDNIPAnPKRIVVLTNEGTEALLALGikpvgavkswkgdpwydyLKDDMKGV-------------QNVGLETEPNV 109
Cdd:COG4558 17 AAGASVAAAA-AERIVSLGGSVTEIVYALG------------------AGDRLVGVdttstypaaakalPDVGYMRQLSA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239366356 110 EAIAELKPDLIIG-NKVRQEKIYDQLNAIA-PTVF---AESLAGNwKDNLTLYANAVNKADKGKKAIADFDKRAADLKEK 184
Cdd:COG4558 78 EGILSLKPTLVLAsEGAGPPEVLDQLRAAGvPVVVvpaAPSLEGV-LAKIRAVAAALGVPEAGEALAARLEADLAALAAR 156
|
170
....*....|....*
gi 1239366356 185 LgDQINKTVSVVrFL 199
Cdd:COG4558 157 V-AAIGKPPRVL-FL 169
|
|
| Oxidored_nitro |
pfam00148 |
Nitrogenase component 1 type Oxidoreductase; |
55-123 |
7.39e-04 |
|
Nitrogenase component 1 type Oxidoreductase;
Pssm-ID: 395096 [Multi-domain] Cd Length: 398 Bit Score: 41.08 E-value: 7.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239366356 55 KRIVVLTNEG-----TEALLALGIKPVGAVKSWKGDPWYDYLKDDMKgvqnvglETEPNV----------EAIAELKPDL 119
Cdd:pfam00148 272 KRVAIYGDPDlvlglARFLLELGMEPVAVGTGTGHPDDYERLKAELE-------EGDPEVidgadleeleELIKELKPDL 344
|
....
gi 1239366356 120 IIGN 123
Cdd:pfam00148 345 LLGN 348
|
|
| HutB |
cd01149 |
Hemin binding protein HutB. These proteins have been shown to function as initial receptors ... |
54-204 |
3.24e-03 |
|
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: 38.40 E-value: 3.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239366356 54 PKRIVVLTNEGTEALLALGI-KPVGAVKSWKGDPwydylkDDMKGVQNVGLETEPNVEAIAELKPDLIIGNKVRQEKI-Y 131
Cdd:cd01149 1 PERIVSLGGSVTEIVYALGAgDRLVGVDSTSTYP------EAAAKLPDVGYMRQLSAEGVLSLKPTLVIASDEAGPPEaL 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1239366356 132 DQLNAIAPTVF----AESLAGnWKDNLTLYANAVNKADKGKKAIADFDKRAADLKeKLGDQINKTVSVVRFLSGESR 204
Cdd:cd01149 75 DQLRAAGVPVVtvpsTPTLDG-LLTKIRQVAQALGVPEKGEALAQEVRQRLAALR-KTVAAHKKPPRVLFLLSHGGG 149
|
|
| |
