|
Name |
Accession |
Description |
Interval |
E-value |
| FeuA |
cd01138 |
Periplasmic binding protein FeuA. These proteins have predicted to function as initial ... |
45-295 |
1.54e-72 |
|
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: 223.75 E-value: 1.54e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517499693 45 KEPRIASMSIHLTNNLLALGITPVGSVIGGDLKSFLPHvadrLKDTKPLGVVADPDMEALLALKPDVIYVDQQYAGNdLS 124
Cdd:cd01138 7 AKPKRIVALSGETEGLALLGIKPVGAASIGGKNPYYKK----KTLAKVVGIVDEPNLEKVLELKPDLIIVSSKQEEN-YE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517499693 125 KFKKITETHSFNLDDGTWRDALKKVGKLVDREQQAETFIKDYEAQAERVKQLVHNKIGDGTVMGIRVTGKELRVFSTR-R 203
Cdd:cd01138 82 KLSKIAPTVPVSYNSSDWEEQLKEIGKLLNKEDEAEKWLADYKQKAKEAKEKIKKKLGNDKSVAVLRGRKQIYVFGEDgR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517499693 204 PMGPLLYDDLGLKPANGVEKLNKKKAFEVISQEVLPDFDADAIFVIVNNRGGADKVFEQlqsNPIWKDLKAVKANHVYMI 283
Cdd:cd01138 162 GGGPILYADLGLKAPEKVKEIEDKPGYAAISLEVLPEFDADYIFLLFFTGPEAKADFES---LPIWKNLPAVKNNHVYIV 238
|
250
....*....|..
gi 517499693 284 peQPWLDYSALG 295
Cdd:cd01138 239 --DAWVFYFADG 248
|
|
| FecB |
COG4594 |
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and ... |
1-309 |
9.50e-46 |
|
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443650 [Multi-domain] Cd Length: 316 Bit Score: 157.00 E-value: 9.50e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517499693 1 MKEKLMIFMCILSIFVLSACGQSTSQSNHTESTKGQ--------TAEQPADKKepRIASMSIHLTNNLLALGITPVGSVI 72
Cdd:COG4594 1 MKKLLLLLILLLALLLLAACGSSSSDSSSSEAAAGArtvkhamgETTIPGTPK--RVVVLEWSFADALLALGVTPVGIAD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517499693 73 GGDLKSFLPHVADRLKDTKPLGVVADPDMEALLALKPDVIYVDQ-----QYagNDLSkfkKITETHSFNLDDGTWRDAL- 146
Cdd:COG4594 79 DNDYDRWVPYLRDLIKGVTSVGTRSQPNLEAIAALKPDLIIADKsrheaIY--DQLS---KIAPTVLFKSRNGDYQENLe 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517499693 147 --KKVGKLVDREQQAETFIKDYEAQAERVKQLVHNKIGDGTVMGIRVTGKELRVFSTRRPMGPLLyDDLGLKPANGVEKL 224
Cdd:COG4594 154 sfKTIAKALGKEEEAEAVLADHDQRIAEAKAKLAAADKGKKVAVGQFRADGLRLYTPNSFAGSVL-AALGFENPPKQSKD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517499693 225 NkKKAFEVISQEVLPDFDADAIFVIVNnrgGADKVFEQLQSNPIWKDLKAVKANHVYMIPEQPWLDY-SALGAKMALDNA 303
Cdd:COG4594 233 N-GYGYSEVSLEQLPALDPDVLFIATY---DDPSILKEWKNNPLWKNLKAVKNGRVYEVDGDLWTRGrGPLAAELMADDL 308
|
....*.
gi 517499693 304 EEIFSK 309
Cdd:COG4594 309 VEILLK 314
|
|
| Peripla_BP_2 |
pfam01497 |
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ... |
60-286 |
4.04e-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: 4.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517499693 60 LLALGITPvgSVIGGDLKSFLPHVADRLKDTKPLGVVADPDMEALLALKPDVIYVDQQY-AGNDLSKFKKITETHSFNLD 138
Cdd:pfam01497 11 LYALGATD--SIVGVDAYTRDPLKADAVAAIVKVGAYGEINVERLAALKPDLVILSTGYlTDEAEELLSLIIPTVIFESS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517499693 139 D--GTWRDALKKVGKLVDREQQAETFIKDYEAQAERVKQLVHNKIGDGTVMGIRVTGKELRVFSTRRPMGPLLyDDLGLK 216
Cdd:pfam01497 89 StgESLKEQIKQLGELLGLEDEAEELVAEIDSALAAAKKAVPSLTRKPVLVFGGADGGGYVVAGSNTYIGDLL-RILGIE 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517499693 217 PANGVEklnKKKAFEVISQEVLPDFDADAIFViVNNRGGADKVFEQLQSNPIWKDLKAVKANHVYMIPEQ 286
Cdd:pfam01497 168 NIAAEL---SGSEYAPISFEAILSSNPDVIIV-SGRDSFTKTGPEFVAANPLWAGLPAVKNGRVYTLPSD 233
|
|
| IsdE |
TIGR03659 |
heme ABC transporter, heme-binding protein isdE; This family of ABC substrate-binding proteins ... |
2-307 |
8.44e-19 |
|
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: 84.63 E-value: 8.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517499693 2 KEKLMIFMCILSIFVLSACGQSTSQSnhtestkgqtAEQPADKKEPRIASMSIHLTNNLLALGITPVGSvigGDLKSFLP 81
Cdd:TIGR03659 1 KKILSLVLLAVLSLGLTGCSSSKEKS----------KVSNKKSKEERIVATSVAVTEILDKLDLDLVGV---PTSQKTLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517499693 82 hvaDRLKDTKPLGVVADPDMEALLALKPDVIY-VDQqyAGNDL-SKFKKI-TETHSFNLDD-GTWRDALKKVGKLVDREQ 157
Cdd:TIGR03659 68 ---KRYKDVPEVGNPMSPDMEKIKSLKPTVVLsVTT--LEEDLgPKFKQLgVEATFLNLTSvDGMKKSITELGEKYGREE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517499693 158 QAETFIKDYEAQAERVKQLVHNKIGDGTVMGIRVTGKELrVFSTRRPMGPLLyDDLGlkpANGVEKlNKKKAFEVISQEV 237
Cdd:TIGR03659 143 QAEKLVKEINEKEAEVKKKVKGKKKPKVLILMGVPGSYL-VATENSYIGDLV-KLAG---GENVYK-GNKQEYLSSNTEY 216
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517499693 238 LPDFDADAIFVIVNnrGGADKVFEQLQ----SNPIWKDLKAVKANHVYMIPEQPWLDYSALGAKMALDNAEEIF 307
Cdd:TIGR03659 217 LLKANPDIILRAAH--GMPDEVKKMFDeefkTNDIWKHFEAVKNNRVYDLDEELFGMTANLKVAEALDELKKIL 288
|
|
| PRK10957 |
PRK10957 |
iron-enterobactin transporter periplasmic binding protein; Provisional |
5-307 |
8.77e-19 |
|
iron-enterobactin transporter periplasmic binding protein; Provisional
Pssm-ID: 236806 [Multi-domain] Cd Length: 317 Bit Score: 85.02 E-value: 8.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517499693 5 LMIFMCILSIFVLSACGQSTSQSN----HTESTKGQT--AEQPAdkkepRIASMSIHLTNNLLAL-------GITPVGSV 71
Cdd:PRK10957 2 LYRLALLLLGLLLSGIAAAQASAAgwprTVTDSRGSVtlESKPQ-----RIVSTSVTLTGTLLAIdapviasGATTPNTR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517499693 72 IGgDLKSFLPHVAD--RLKDTKPLgVVADPDMEALLALKPDVIYVDQqyAGND-----LSKFKKITETHSFNLDDGTWRD 144
Cdd:PRK10957 77 VA-DDQGFFRQWSDvaKERGVEVL-YIGEPDAEAVAAQMPDLIVISA--TGGDsalalYDQLSAIAPTLVIDYDDKSWQE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517499693 145 ALKKVGKLVDREQQAETFIKDYEAQAERVKQLVHNKIGDGTVMGIRVTGKELRVFSTRRPMGPLLyDDLGLKPANGVEKL 224
Cdd:PRK10957 153 LATQLGEATGLEKQAAAVIAQFDAQLAEVKAKITLPPQPVSALVYNGAGHSANLWTPESAQGQLL-EQLGFTLAELPAGL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517499693 225 N------KKKAFEVISQEVLPD-FDADAIFVIvnnrGGADKVFEQLQSNPIWKDLKAVKANHVY-MIPEQPWLD-YSALg 295
Cdd:PRK10957 232 QastsqgKRHDIIQLGGENLAAgLNGETLFLF----AGDDKDADAFLADPLLANLPAVQNKQVYaLGTDTFRLDyYSAT- 306
|
330
....*....|..
gi 517499693 296 aKMaLDNAEEIF 307
Cdd:PRK10957 307 -QL-LDRLAALF 316
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| FeuA |
cd01138 |
Periplasmic binding protein FeuA. These proteins have predicted to function as initial ... |
45-295 |
1.54e-72 |
|
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: 223.75 E-value: 1.54e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517499693 45 KEPRIASMSIHLTNNLLALGITPVGSVIGGDLKSFLPHvadrLKDTKPLGVVADPDMEALLALKPDVIYVDQQYAGNdLS 124
Cdd:cd01138 7 AKPKRIVALSGETEGLALLGIKPVGAASIGGKNPYYKK----KTLAKVVGIVDEPNLEKVLELKPDLIIVSSKQEEN-YE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517499693 125 KFKKITETHSFNLDDGTWRDALKKVGKLVDREQQAETFIKDYEAQAERVKQLVHNKIGDGTVMGIRVTGKELRVFSTR-R 203
Cdd:cd01138 82 KLSKIAPTVPVSYNSSDWEEQLKEIGKLLNKEDEAEKWLADYKQKAKEAKEKIKKKLGNDKSVAVLRGRKQIYVFGEDgR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517499693 204 PMGPLLYDDLGLKPANGVEKLNKKKAFEVISQEVLPDFDADAIFVIVNNRGGADKVFEQlqsNPIWKDLKAVKANHVYMI 283
Cdd:cd01138 162 GGGPILYADLGLKAPEKVKEIEDKPGYAAISLEVLPEFDADYIFLLFFTGPEAKADFES---LPIWKNLPAVKNNHVYIV 238
|
250
....*....|..
gi 517499693 284 peQPWLDYSALG 295
Cdd:cd01138 239 --DAWVFYFADG 248
|
|
| FhuD |
cd01146 |
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial ... |
44-288 |
3.02e-49 |
|
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: 164.38 E-value: 3.02e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517499693 44 KKEPRIASMSIHLTNNLLALGITPVGSVIGGDLKSFLPHVADRLKDTKPLGVVADPDMEALLALKPDVIYVDQQYAGNDL 123
Cdd:cd01146 1 AKPQRIVALDWGALETLLALGVKPVGVADTAGYKPWIPEPALPLEGVVDVGTRGQPNLEAIAALKPDLILGSASRHDEIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517499693 124 SKFKKI--TETHSFNLDDGTWRDALKKVGKLVDREQQAETFIKDYEAQAERVKQlVHNKIGDGTVMGIRVTG-KELRVFS 200
Cdd:cd01146 81 DQLSQIapTVLLDSSPWLAEWKENLRLIAKALGKEEEAEKLLAEYDQRLAELRQ-KLPDKGPKPVSVVRFSDaGSIRLYG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517499693 201 TRRPMGPLLyDDLGLKPANGVEKLNkKKAFEVISQEVLPDFDADAIFVIVnnrGGADKVFEQLQSNPIWKDLKAVKANHV 280
Cdd:cd01146 160 PNSFAGSVL-EDLGLQNPWAQETTN-DSGFATISLERLAKADADVLFVFT---YEDEELAQALQANPLWQNLPAVKNGRV 234
|
....*...
gi 517499693 281 YMIPEQPW 288
Cdd:cd01146 235 YVVDDVWW 242
|
|
| FecB |
COG4594 |
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and ... |
1-309 |
9.50e-46 |
|
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443650 [Multi-domain] Cd Length: 316 Bit Score: 157.00 E-value: 9.50e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517499693 1 MKEKLMIFMCILSIFVLSACGQSTSQSNHTESTKGQ--------TAEQPADKKepRIASMSIHLTNNLLALGITPVGSVI 72
Cdd:COG4594 1 MKKLLLLLILLLALLLLAACGSSSSDSSSSEAAAGArtvkhamgETTIPGTPK--RVVVLEWSFADALLALGVTPVGIAD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517499693 73 GGDLKSFLPHVADRLKDTKPLGVVADPDMEALLALKPDVIYVDQ-----QYagNDLSkfkKITETHSFNLDDGTWRDAL- 146
Cdd:COG4594 79 DNDYDRWVPYLRDLIKGVTSVGTRSQPNLEAIAALKPDLIIADKsrheaIY--DQLS---KIAPTVLFKSRNGDYQENLe 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517499693 147 --KKVGKLVDREQQAETFIKDYEAQAERVKQLVHNKIGDGTVMGIRVTGKELRVFSTRRPMGPLLyDDLGLKPANGVEKL 224
Cdd:COG4594 154 sfKTIAKALGKEEEAEAVLADHDQRIAEAKAKLAAADKGKKVAVGQFRADGLRLYTPNSFAGSVL-AALGFENPPKQSKD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517499693 225 NkKKAFEVISQEVLPDFDADAIFVIVNnrgGADKVFEQLQSNPIWKDLKAVKANHVYMIPEQPWLDY-SALGAKMALDNA 303
Cdd:COG4594 233 N-GYGYSEVSLEQLPALDPDVLFIATY---DDPSILKEWKNNPLWKNLKAVKNGRVYEVDGDLWTRGrGPLAAELMADDL 308
|
....*.
gi 517499693 304 EEIFSK 309
Cdd:COG4594 309 VEILLK 314
|
|
| FepB |
COG0614 |
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ... |
48-301 |
4.09e-43 |
|
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 440379 [Multi-domain] Cd Length: 264 Bit Score: 148.61 E-value: 4.09e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517499693 48 RIASMSIHLTNNLLALGITPvgSVIGGDLKSFLPHVADRLKDTKPLGVVADPDMEALLALKPDVIYVDQ-QYAGNDLSKF 126
Cdd:COG0614 2 RIVSLSPSATELLLALGAGD--RLVGVSDWGYCDYPELELKDLPVVGGTGEPNLEAILALKPDLVLASSsGNDEEDYEQL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517499693 127 KKIT-ETHSFNLDD-GTWRDALKKVGKLVDREQQAETFIKDYEAQAERVKQLVHNKIGDGTVMGIRVTGKELRVFSTRRP 204
Cdd:COG0614 80 EKIGiPVVVLDPRSlEDLYESIRLLGELLGREERAEALIAEYEARLAAVRARLAGAEERPTVLYEIWSGDPLYTAGGGSF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517499693 205 MGPLLyDDLGLKPANGveklNKKKAFEVISQEVLPDFDADAIFVIVNNRG--GADKVFEQLQSNPIWKDLKAVKANHVYM 282
Cdd:COG0614 160 IGELL-ELAGGRNVAA----DLGGGYPEVSLEQVLALDPDVIILSGGGYDaeTAEEALEALLADPGWQSLPAVKNGRVYV 234
|
250
....*....|....*....
gi 517499693 283 IPEQPWLDYSALGAKMALD 301
Cdd:COG0614 235 VPGDLLSRPGPRLLLALED 253
|
|
| FatB |
cd01140 |
Siderophore binding protein FatB. These proteins have been shown to function as ABC-type ... |
44-309 |
7.89e-33 |
|
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: 121.98 E-value: 7.89e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517499693 44 KKEPRIASMSIHLTNNLLALGITPVGSVIggdlKSFLPHVADRLKDTK--PLGVVADPDMEALLALKPDVIYVDQQyAGN 121
Cdd:cd01140 10 KNPEKVVVFDVGALDTLDALGVKVVGVPK----SSTLPEYLKKYKDDKyaNVGTLFEPDLEAIAALKPDLIIIGGR-LAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517499693 122 DLSKFKKITETHSFNLD-DGTWRDALKKV---GKLVDREQQAETFIKDYEAQAERVKQLVhnkIGDGTVMGIRVTGKELR 197
Cdd:cd01140 85 KYDELKKIAPTIDLGADlKNYLESVKQNIetlGKIFGKEEEAKELVAEIDASIAEAKSAA---KGKKKALVVLVNGGKLS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517499693 198 VFSTRRPMGPLlYDDLGLKPAngVEKLNKKKAFEVISQEVLPDFDADAIFVIvnNR----GGADKVFEQLQSNPIWKDLK 273
Cdd:cd01140 162 AFGPGSRFGWL-HDLLGFEPA--DENIKASSHGQPVSFEYILEANPDWLFVI--DRgaaiGAEGSSAKEVLDNDLVKNTT 236
|
250 260 270
....*....|....*....|....*....|....*.
gi 517499693 274 AVKANHVYMIPEQPWldYSALGAKMALDNAEEIFSK 309
Cdd:cd01140 237 AWKNGKVIYLDPDLW--YLSGGGLESLKQMIDDLKK 270
|
|
| CeuA |
COG4607 |
ABC-type enterochelin transport system, periplasmic component [Inorganic ion transport and ... |
1-288 |
1.94e-32 |
|
ABC-type enterochelin transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443657 [Multi-domain] Cd Length: 310 Bit Score: 121.83 E-value: 1.94e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517499693 1 MKEKLMIFMCILSIFVLSACGQSTSQSNHTESTKGQT-------AEQPADKKepRIASMSIHLTNNLLALGITPVGSVig 73
Cdd:COG4607 1 MKKTLLAALALAAALALAACGSSSAAAASAAAAETVTvehalgtVEVPKNPK--RVVVFDNGALDTLDALGVEVAGVP-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517499693 74 gdlKSFLPHVADRLKDTK--PLGVVADPDMEALLALKPDVIYVDQQYAGNdLSKFKKITETHSFNLDDGTWRDALKK--- 148
Cdd:COG4607 77 ---KGLLPDYLSKYADDKyaNVGTLFEPDLEAIAALKPDLIIIGGRSAKK-YDELSKIAPTIDLTVDGEDYLESLKRnte 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517499693 149 -VGKLVDREQQAETFIKDYEAQAERVKQLVHnkiGDGTVMGIRVTGKELRVFSTRRPMGPlLYDDLGLKPAngVEKLNKK 227
Cdd:COG4607 153 tLGEIFGKEDEAEELVADLDAKIAALKAAAA---GKGTALIVLTNGGKISAYGPGSRFGP-IHDVLGFKPA--DEDIEAS 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517499693 228 KAFEVISQEVLPDFDADAIFVI-----VNNRGGADKVFEqlqSNPIWKDLKAVKANHVYMIPEQPW 288
Cdd:COG4607 227 THGQAISFEFIAEANPDWLFVIdrdaaIGGEGPAAKQVL---DNELVKQTTAWKNGQIVYLDPDAW 289
|
|
| Peripla_BP_2 |
pfam01497 |
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ... |
60-286 |
4.04e-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: 4.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517499693 60 LLALGITPvgSVIGGDLKSFLPHVADRLKDTKPLGVVADPDMEALLALKPDVIYVDQQY-AGNDLSKFKKITETHSFNLD 138
Cdd:pfam01497 11 LYALGATD--SIVGVDAYTRDPLKADAVAAIVKVGAYGEINVERLAALKPDLVILSTGYlTDEAEELLSLIIPTVIFESS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517499693 139 D--GTWRDALKKVGKLVDREQQAETFIKDYEAQAERVKQLVHNKIGDGTVMGIRVTGKELRVFSTRRPMGPLLyDDLGLK 216
Cdd:pfam01497 89 StgESLKEQIKQLGELLGLEDEAEELVAEIDSALAAAKKAVPSLTRKPVLVFGGADGGGYVVAGSNTYIGDLL-RILGIE 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517499693 217 PANGVEklnKKKAFEVISQEVLPDFDADAIFViVNNRGGADKVFEQLQSNPIWKDLKAVKANHVYMIPEQ 286
Cdd:pfam01497 168 NIAAEL---SGSEYAPISFEAILSSNPDVIIV-SGRDSFTKTGPEFVAANPLWAGLPAVKNGRVYTLPSD 233
|
|
| IsdE |
TIGR03659 |
heme ABC transporter, heme-binding protein isdE; This family of ABC substrate-binding proteins ... |
2-307 |
8.44e-19 |
|
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: 84.63 E-value: 8.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517499693 2 KEKLMIFMCILSIFVLSACGQSTSQSnhtestkgqtAEQPADKKEPRIASMSIHLTNNLLALGITPVGSvigGDLKSFLP 81
Cdd:TIGR03659 1 KKILSLVLLAVLSLGLTGCSSSKEKS----------KVSNKKSKEERIVATSVAVTEILDKLDLDLVGV---PTSQKTLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517499693 82 hvaDRLKDTKPLGVVADPDMEALLALKPDVIY-VDQqyAGNDL-SKFKKI-TETHSFNLDD-GTWRDALKKVGKLVDREQ 157
Cdd:TIGR03659 68 ---KRYKDVPEVGNPMSPDMEKIKSLKPTVVLsVTT--LEEDLgPKFKQLgVEATFLNLTSvDGMKKSITELGEKYGREE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517499693 158 QAETFIKDYEAQAERVKQLVHNKIGDGTVMGIRVTGKELrVFSTRRPMGPLLyDDLGlkpANGVEKlNKKKAFEVISQEV 237
Cdd:TIGR03659 143 QAEKLVKEINEKEAEVKKKVKGKKKPKVLILMGVPGSYL-VATENSYIGDLV-KLAG---GENVYK-GNKQEYLSSNTEY 216
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517499693 238 LPDFDADAIFVIVNnrGGADKVFEQLQ----SNPIWKDLKAVKANHVYMIPEQPWLDYSALGAKMALDNAEEIF 307
Cdd:TIGR03659 217 LLKANPDIILRAAH--GMPDEVKKMFDeefkTNDIWKHFEAVKNNRVYDLDEELFGMTANLKVAEALDELKKIL 288
|
|
| PRK10957 |
PRK10957 |
iron-enterobactin transporter periplasmic binding protein; Provisional |
5-307 |
8.77e-19 |
|
iron-enterobactin transporter periplasmic binding protein; Provisional
Pssm-ID: 236806 [Multi-domain] Cd Length: 317 Bit Score: 85.02 E-value: 8.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517499693 5 LMIFMCILSIFVLSACGQSTSQSN----HTESTKGQT--AEQPAdkkepRIASMSIHLTNNLLAL-------GITPVGSV 71
Cdd:PRK10957 2 LYRLALLLLGLLLSGIAAAQASAAgwprTVTDSRGSVtlESKPQ-----RIVSTSVTLTGTLLAIdapviasGATTPNTR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517499693 72 IGgDLKSFLPHVAD--RLKDTKPLgVVADPDMEALLALKPDVIYVDQqyAGND-----LSKFKKITETHSFNLDDGTWRD 144
Cdd:PRK10957 77 VA-DDQGFFRQWSDvaKERGVEVL-YIGEPDAEAVAAQMPDLIVISA--TGGDsalalYDQLSAIAPTLVIDYDDKSWQE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517499693 145 ALKKVGKLVDREQQAETFIKDYEAQAERVKQLVHNKIGDGTVMGIRVTGKELRVFSTRRPMGPLLyDDLGLKPANGVEKL 224
Cdd:PRK10957 153 LATQLGEATGLEKQAAAVIAQFDAQLAEVKAKITLPPQPVSALVYNGAGHSANLWTPESAQGQLL-EQLGFTLAELPAGL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517499693 225 N------KKKAFEVISQEVLPD-FDADAIFVIvnnrGGADKVFEQLQSNPIWKDLKAVKANHVY-MIPEQPWLD-YSALg 295
Cdd:PRK10957 232 QastsqgKRHDIIQLGGENLAAgLNGETLFLF----AGDDKDADAFLADPLLANLPAVQNKQVYaLGTDTFRLDyYSAT- 306
|
330
....*....|..
gi 517499693 296 aKMaLDNAEEIF 307
Cdd:PRK10957 307 -QL-LDRLAALF 316
|
|
| HemV-2 |
cd01147 |
Metal binding protein HemV-2. These proteins are predicted to function as initial receptors ... |
99-291 |
1.26e-17 |
|
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: 80.84 E-value: 1.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517499693 99 PDMEALLALKPDVIY----VDQQYAGNDLSKFKKITET---HSFNLDDgtWRDALKKVGKLVDREQQAE---TFIKDYEA 168
Cdd:cd01147 65 PNYEKIAALKPDVVIdvgsDDPTSIADDLQKKTGIPVVvldGGDSLED--TPEQIRLLGKVLGKEERAEeliSFIESILA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517499693 169 QA-ERVKQLVHNKIGDGTVMGIRVTGKelRVFSTRRPMGPLLYDDLGLKpaNGVEKLNKKKAFEViSQEVLPDFDADAIF 247
Cdd:cd01147 143 DVeERTKDIPDEEKPTVYFGRIGTKGA--AGLESGLAGSIEVFELAGGI--NVADGLGGGGLKEV-SPEQILLWNPDVIF 217
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 517499693 248 VIvnNRGGADKVFEQLQSNPIWKDLKAVKANHVYMIPEQP--WLDY 291
Cdd:cd01147 218 LD--TGSFYLSLEGYAKNRPFWQSLKAVKNGRVYLLPALPfnWYDT 261
|
|
| TroA-like |
cd00636 |
Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function ... |
47-177 |
5.13e-16 |
|
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: 73.75 E-value: 5.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517499693 47 PRIASMSIHLTNNLLALG--ITPVGSVIGGDLKSFLPHVADRLKDtkpLGVVADPDMEALLALKPDVIYVDQQYAGNDLS 124
Cdd:cd00636 1 KRVVALDPGATELLLALGgdDKPVGVADPSGYPPEAKALLEKVPD---VGHGYEPNLEKIAALKPDLIIANGSGLEAWLD 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 517499693 125 KFKKITE-----THSFNLDDGTWRDALKKVGKLVDREQQAETFIKDYEAQAERVKQLV 177
Cdd:cd00636 78 KLSKIAIpvvvvDEASELSLENIKESIRLIGKALGKEENAEELIAELDARLAELRAKL 135
|
|
| fecB |
PRK11411 |
iron-dicitrate transporter substrate-binding subunit; Provisional |
8-309 |
1.03e-13 |
|
iron-dicitrate transporter substrate-binding subunit; Provisional
Pssm-ID: 183123 [Multi-domain] Cd Length: 303 Bit Score: 70.09 E-value: 1.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517499693 8 FMCILSIFVLSACGQSTSQSNHTESTKGQTAEqpadkkepRIASMSIHLTNNLLALGITPVGSVIGGDLKSFLPHVADRL 87
Cdd:PRK11411 9 FAGLLLLSGSSHAFAVTVQDEQGTFTLEKTPQ--------RIVVLELSFVDALAAVGVSPVGVADDNDAKRILPEVRAHL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517499693 88 KDTKPLGVVADPDMEALLALKPDVIYVD-QQYAG--NDLSK------FKKITETHSFNLddgtwrDALKKVGKLVDREQQ 158
Cdd:PRK11411 81 KPWQSVGTRSQPSLEAIAALKPDLIIADsSRHAGvyIALQKiaptllLKSRNETYQENL------QSAAIIGEVLGKKRE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517499693 159 AETFIKDYEAQAERVKQlvhnKIGDGTVMgirvtgkelrVFSTRRPMGPLLYDD----------LGLK----PANGvekl 224
Cdd:PRK11411 155 MQARIEQHKERMAQFAS----QLPKGTRV----------AFGTSREQQFNLHSPesytgsvlaaLGLNvpkaPMNG---- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517499693 225 nkkKAFEVISQEVLPDFDADAIFVIVNNRggaDKVFEQLQSNPIWKDLKAVKANHVYMIPEQPW-LDYSALGAKMALDNA 303
Cdd:PRK11411 217 ---AAMPSISLEQLLALNPDWLLVAHYRQ---ESIVKRWQQDPLWQMLTAAKKQQVASVDSNTWaRMRGIFAAERIAKDT 290
|
....*.
gi 517499693 304 EEIFSK 309
Cdd:PRK11411 291 VKIFHH 296
|
|
| BtuF |
cd01144 |
Cobalamin binding protein BtuF. These proteins have been shown to function as initial ... |
48-289 |
2.03e-12 |
|
Cobalamin binding protein BtuF. These proteins have been shown to function as initial receptors in ABC transport of vitamin B12 (cobalamin) in eubacterial and some archaeal species. They belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind the metal ion in the cleft between these domains. In addition, these proteins sometimes have a low complexity region containing a metal-binding histidine-rich motif (repetitive HDH sequence).
Pssm-ID: 238564 [Multi-domain] Cd Length: 245 Bit Score: 65.78 E-value: 2.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517499693 48 RIASMSIHLTNNLLALGI--TPVGSVIGGDLksflPHVADRLKdtkPLGVVADPDMEALLALKPD-VIYVDQQYAGNDLS 124
Cdd:cd01144 2 RIVSLAPSATELLYALGLgdQLVGVTDYCDY----PPEAKKLP---RVGGFYQLDLERVLALKPDlVIAWDDCNVCAVVD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517499693 125 KFKK------ITETHSFnldDGTWrDALKKVGKLVDREQQAETFIKDYEAQAERVKQLVHNKigdgtvmgirvtgKELRV 198
Cdd:cd01144 75 QLRAagipvlVSEPQTL---DDIL-ADIRRLGTLAGRPARAEELAEALRRRLAALRKQYASK-------------PPPRV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517499693 199 F---STRRPM---GPLLYDDLGLkpANGVEKLNK--KKAFEVISQEVL---PDfdadaifVIVNNRGGADKVFEQLQSNP 267
Cdd:cd01144 138 FyqeWIDPLMtagGDWVPELIAL--AGGVNVFADagERSPQVSWEDVLaanPD-------VIVLSPCGFGFTPAILRKEP 208
|
250 260
....*....|....*....|..
gi 517499693 268 IWKDLKAVKANHVYMIPEqPWL 289
Cdd:cd01144 209 AWQALPAVRNGRVYAVDG-NWY 229
|
|
| TroA_e |
cd01142 |
Periplasmic binding protein TroA_e. These proteins are predicted to function as initial ... |
34-291 |
2.94e-12 |
|
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: 65.84 E-value: 2.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517499693 34 KGQTAEQPADKKepRIASMSIHLTNNLLALGITPVgsVIGGDLKS----FLPHVADRLKDTKPLGVVADPDMEALLALKP 109
Cdd:cd01142 14 AGRKVTIPDEVK--RIAALWGAGNAVVAALGGGKL--IVATTSTVqqepWLYRLAPSLENVATGGTGNDVNIEELLALKP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517499693 110 DVIYVdQQYAGNDLSKfKKITETHSFNLDDGT---WRDALKKVGKLVDREQQAETFIKDYEAQAERVKQLVhNKIGDgtv 186
Cdd:cd01142 90 DVVIV-WSTDGKEAGK-AVLRLLNALSLRDAEleeVKLTIALLGELLGRQEKAEALVAYFDDNLAYVAART-KKLPD--- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517499693 187 mgirvtGKELRVF-------STRrpmGPLLYDDLGLKPANGV---EKLNKKKAFEViSQEVLPDFDADAIfvIVNNRGGA 256
Cdd:cd01142 164 ------SERPRVYyagpdplTTD---GTGSITNSWIDLAGGInvaSEATKKGSGEV-SLEQLLKWNPDVI--IVGNADTK 231
|
250 260 270
....*....|....*....|....*....|....*.
gi 517499693 257 DKVFeqlqSNPIWKDLKAVKANHVYMIPEQP-WLDY 291
Cdd:cd01142 232 AAIL----ADPRWQNLRAVKNGRVYVNPEGAfWWDR 263
|
|
| PRK10576 |
PRK10576 |
Fe(3+)-hydroxamate ABC transporter substrate-binding protein FhuD; |
60-305 |
6.92e-10 |
|
Fe(3+)-hydroxamate ABC transporter substrate-binding protein FhuD;
Pssm-ID: 236719 Cd Length: 292 Bit Score: 58.87 E-value: 6.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517499693 60 LLALGITPVGsviggdlksflphVAD----RLKDTKP--------LGVVADPDMEALLALKPDVIYVDQQYaGNDLSKFK 127
Cdd:PRK10576 46 LLALGVTPYG-------------VADthnyRLWVSEPalpdsvidVGLRTEPNLELLTQMKPSLILWSAGY-GPSPEKLA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517499693 128 KITETHSFNLDDG-----TWRDALKKVGKLVDREQQAETFIKDYEAQAERVKQLVHNKIGDGTVMGIRVTGKELRVFSTR 202
Cdd:PRK10576 112 RIAPGRGFAFSDGkkplaVARKSLVELAQRLNLEAAAETHLAQFDDFIASAKPRLAGRGQRPLLLTSLIDPRHALVFGPN 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517499693 203 RPMGPLLyDDLGLKPAngvekLNKKKAF---EVISQEVLPDF-DADAI-FVivnnrGGADKVFEQLQSNPIWKDLKAVKA 277
Cdd:PRK10576 192 SLFQEVL-DELGIENA-----WQGETNFwgsTVVGIERLAAYkDADVIcFD-----HGNSKDMQQLMATPLWQAMPFVRA 260
|
250 260 270
....*....|....*....|....*....|..
gi 517499693 278 NHVYMIPeQPWLdYSALGAKM----ALDNAEE 305
Cdd:PRK10576 261 GRFQRVP-AVWF-YGATLSAMhfvrVLDNALG 290
|
|
| YvrC |
cd01143 |
Periplasmic binding protein YvrC. These proteins are predicted to function as initial ... |
45-180 |
6.89e-09 |
|
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: 54.59 E-value: 6.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517499693 45 KEP-RIASMSIHLTNNLLALGITpvGSVIGGDLKSFLPhvaDRLKDTKPLGVVADPDMEALLALKPDVIYVDQQYAGNDL 123
Cdd:cd01143 1 KEPeRIVSLSPSITEILFALGAG--DKIVGVDTYSNYP---KEVRKKPKVGSYSNPNVEKIVALKPDLVIVSSSSLAELL 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517499693 124 SKFKK--ITethSFNLDDGTW----RDALKKVGKLVDREQQAETFIKDYEAQAERVKQLVHNK 180
Cdd:cd01143 76 EKLKDagIP---VVVLPAASSldeiYDQIELIGKITGAEEEAEKLVKEMKQKIDKVKDKGKTI 135
|
|
| TroA_a |
cd01148 |
Metal binding protein TroA_a. These proteins are predicted to function as initial receptors ... |
43-284 |
1.16e-07 |
|
Metal binding protein TroA_a. These proteins are predicted to function as initial receptors in ABC transport of metal ions in eubacteria. They belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind the metal ion in the cleft between these domains.
Pssm-ID: 238568 [Multi-domain] Cd Length: 284 Bit Score: 51.95 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517499693 43 DKKEPRIASMSIHLTNNLLALGITPvgSVIG--GDLKSFLPhvadRLKD-TKPLGVVA--DPDMEALLALKPDVIYVDQQ 117
Cdd:cd01148 15 DKAPQRVVSNDQNTTEMMLALGLQD--RMVGtaGIDNKDLP----ELKAkYDKVPELAkkYPSKETVLAARPDLVFGGWS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517499693 118 YaGNDLSKF--------KKI-----TETHSFNLDDGTWRDA---LKKVGKLVDREQQAETFIKDYEAQAERVKQLVhnKI 181
Cdd:cd01148 89 Y-GFDKGGLgtpdslaeLGIktyilPESCGQRRGEATLDDVyndIRNLGKIFDVEDRADKLVADLKARLAEISAKV--KG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517499693 182 GDGTVMGIRVTGKELRVFSTRR-PMGPLLYDDLGLKpaNGVEKLnKKKAFEViSQEVLPDFDADAIFVI-VNNRGGADKV 259
Cdd:cd01148 166 DGKKVAVFVYDSGEDKPFTSGRgGIPNAIITAAGGR--NVFADV-DESWTTV-SWETVIARNPDVIVIIdYGDQNAAEQK 241
|
250 260
....*....|....*....|....*
gi 517499693 260 FEQLQSNPIWKDLKAVKANHVYMIP 284
Cdd:cd01148 242 IKFLKENPALKNVPAVKNNRFIVLP 266
|
|
| HutB |
cd01149 |
Hemin binding protein HutB. These proteins have been shown to function as initial receptors ... |
48-271 |
1.70e-04 |
|
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: 42.25 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517499693 48 RIASMSIHLTNNLLALGITpvGSVIGGDLKSFLPHVADRLKDtkpLGVVADPDMEALLALKPDVIYVDQQyAGNDLSkFK 127
Cdd:cd01149 3 RIVSLGGSVTEIVYALGAG--DRLVGVDSTSTYPEAAAKLPD---VGYMRQLSAEGVLSLKPTLVIASDE-AGPPEA-LD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517499693 128 KITETHS-FNLDDGTWR-DALK----KVGKLVDREQQAETFIKDYEAQAERVKQLVHNKIGDGTVMGIRVTGkelrvfsT 201
Cdd:cd01149 76 QLRAAGVpVVTVPSTPTlDGLLtkirQVAQALGVPEKGEALAQEVRQRLAALRKTVAAHKKPPRVLFLLSHG-------G 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517499693 202 RRPM--GPLLYDDLGLKPANGVEKLNKKKAFEVISQEVLPDFDADAIFVIVNNR---GGADKVFEQ--LQSNPIWKD 271
Cdd:cd01149 149 GAAMaaGRNTAADAIIALAGAVNAAAGFRGYKPLSAEALIAAQPDVILVMSRGLdavGGVDGLLKLpgLAQTPAGRN 225
|
|
| ChuT |
COG4558 |
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism] ... |
1-180 |
6.66e-04 |
|
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443619 [Multi-domain] Cd Length: 285 Bit Score: 40.56 E-value: 6.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517499693 1 MKeKLMIFMCILSIFVLSACGQSTSQSnhtestkgqtaeqpadkkEPRIASMSIHLTNNLLALGITPvgSVIGGDLKSFL 80
Cdd:COG4558 1 MK-RLALALLLLALAALAAGASVAAAA------------------AERIVSLGGSVTEIVYALGAGD--RLVGVDTTSTY 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517499693 81 PHVADRLKDtkpLGVVADPDMEALLALKPDVIYVDQQyAGNDLS---------KFKKITETHSFnldDGTwRDALKKVGK 151
Cdd:COG4558 60 PAAAKALPD---VGYMRQLSAEGILSLKPTLVLASEG-AGPPEVldqlraagvPVVVVPAAPSL---EGV-LAKIRAVAA 131
|
170 180
....*....|....*....|....*....
gi 517499693 152 LVDREQQAETFIKDYEAQAERVKQLVHNK 180
Cdd:COG4558 132 ALGVPEAGEALAARLEADLAALAARVAAI 160
|
|
| TroA_d |
cd01141 |
Periplasmic binding protein TroA_d. These proteins are predicted to function as initial ... |
35-187 |
8.85e-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: 39.71 E-value: 8.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517499693 35 GQTAEQPAdkkePRIASMSIHLTNNLLALGItpVGSVIGGDLKSF---LPHVADRLKDTkpLGVVADPDMEALLALKPDV 111
Cdd:cd01141 1 AKTIKVPP----KRIVVLSPTHVDLLLALDK--ADKIVGVSASAYdlnTPAVKERIDIQ--VGPTGSLNVELIVALKPDL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517499693 112 IYVdqqYAGND-LSKFKKITETH----SFNLDDGTWR--DALKKVGKLVD--REQQAETFIKDYEAQAERVKQLVHNKiG 182
Cdd:cd01141 73 VIL---YGGFQaQTILDKLEQLGipvlYVNEYPSPLGraEWIKFAAAFYGvgKEDKADEAFAQIAGRYRDLAKKVSNL-N 148
|
....*
gi 517499693 183 DGTVM 187
Cdd:cd01141 149 KPTVA 153
|
|
| TroA_f |
cd01139 |
Periplasmic binding protein TroA_f. These proteins are predicted to function as initial ... |
68-207 |
3.52e-03 |
|
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: 38.44 E-value: 3.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517499693 68 VGSviGGDLKSFLPHVADRLKDTKP-------LGVVADPD--MEALLALKPDVIYV--DQQYAGNDLSKFKKITETH--- 133
Cdd:cd01139 44 VGW--GGDLKKGDPDTYAKYKEKFPeiadiplIGSTYNGDfsVEKVLTLKPDLVILniWAKTTAEESGILEKLEQAGipv 121
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517499693 134 ---SFN--LDDGTwRDALKKVGKLVDREQQAETFIKDYEAQAERVKQlvhnkigdgTVMGIRvtGKELRVFSTRRPMGP 207
Cdd:cd01139 122 vfvDFRqkPLKNT-TPSMRLLGKALGREERAEEFIEFYQERIDRIRD---------RLAKIN--EPKPKVFIELGAGGP 188
|
|
| |
