|
Name |
Accession |
Description |
Interval |
E-value |
| CeuA |
COG4607 |
ABC-type enterochelin transport system, periplasmic component [Inorganic ion transport and ... |
1-316 |
1.59e-155 |
|
ABC-type enterochelin transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443657 [Multi-domain] Cd Length: 310 Bit Score: 437.31 E-value: 1.59e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654964714 1 MKKVLVMFVAVLTAIVVAACGNqgaKETTGGESKQKETVTVTDQFNKdgIKIEKNPKKVVVFSMGALDTLDKLGVEVAGL 80
Cdd:COG4607 1 MKKTLLAALALAAALALAACGS---SSAAAASAAAAETVTVEHALGT--VEVPKNPKRVVVFDNGALDTLDALGVEVAGV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654964714 81 PKQAIPEYLSKYQDDKYANVGGLKEPDFEKIAELKPDLIIIQGRQADSFDEFSKIAPTIYIDTDNQHYMKSFKENTKVLG 160
Cdd:COG4607 76 PKGLLPDYLSKYADDKYANVGTLFEPDLEAIAALKPDLIIIGGRSAKKYDELSKIAPTIDLTVDGEDYLESLKRNTETLG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654964714 161 QIFDKEDQAKKDLAAIDKQIADLKKQADKlDKKALVMMANDSKMTAFGPGSKYGLIHDVFGIKAADDSLDpSAKHGQSIA 240
Cdd:COG4607 156 EIFGKEDEAEELVADLDAKIAALKAAAAG-KGTALIVLTNGGKISAYGPGSRFGPIHDVLGFKPADEDIE-ASTHGQAIS 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 654964714 241 YEYLVKQNPDYLFVVDRGAAIGEK-SSAKQIVENEYVKEVNAVKNNHVVYLDPGLWYLSGGGLESMAGMIKEIKAGI 316
Cdd:COG4607 234 FEFIAEANPDWLFVIDRDAAIGGEgPAAKQVLDNELVKQTTAWKNGQIVYLDPDAWYLAGGGIQSLTEMLDEVADAL 310
|
|
| FatB |
cd01140 |
Siderophore binding protein FatB. These proteins have been shown to function as ABC-type ... |
46-314 |
4.11e-117 |
|
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: 338.46 E-value: 4.11e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654964714 46 NKDGIKIEKNPKKVVVFSMGALDTLDKLGVEVAGLPKQA-IPEYLSKYQDDKYANVGGLKEPDFEKIAELKPDLIIIQGR 124
Cdd:cd01140 2 ALGETKVPKNPEKVVVFDVGALDTLDALGVKVVGVPKSStLPEYLKKYKDDKYANVGTLFEPDLEAIAALKPDLIIIGGR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654964714 125 QADSFDEFSKIAPTIYIDTDNQHYMKSFKENTKVLGQIFDKEDQAKKDLAAIDKQIADLKKQADKlDKKALVMMANDSKM 204
Cdd:cd01140 82 LAEKYDELKKIAPTIDLGADLKNYLESVKQNIETLGKIFGKEEEAKELVAEIDASIAEAKSAAKG-KKKALVVLVNGGKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654964714 205 TAFGPGSKYGLIHDVFGIKAADDSLDPSaKHGQSIAYEYLVKQNPDYLFVVDRGAAIG-EKSSAKQIVENEYVKEVNAVK 283
Cdd:cd01140 161 SAFGPGSRFGWLHDLLGFEPADENIKAS-SHGQPVSFEYILEANPDWLFVIDRGAAIGaEGSSAKEVLDNDLVKNTTAWK 239
|
250 260 270
....*....|....*....|....*....|.
gi 654964714 284 NNHVVYLDPGLWYLSGGGLESMAGMIKEIKA 314
Cdd:cd01140 240 NGKVIYLDPDLWYLSGGGLESLKQMIDDLKK 270
|
|
| FecB |
COG4594 |
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and ... |
1-300 |
4.94e-54 |
|
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443650 [Multi-domain] Cd Length: 316 Bit Score: 178.96 E-value: 4.94e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654964714 1 MKKVLVMFVAVLTAIVVAACGNQgaKETTGGESKQKETVTVTDQFNKdgIKIEKNPKKVVVFSMGALDTLDKLGVE---V 77
Cdd:COG4594 1 MKKLLLLLILLLALLLLAACGSS--SSDSSSSEAAAGARTVKHAMGE--TTIPGTPKRVVVLEWSFADALLALGVTpvgI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654964714 78 AGLPKQ-AIPEYLSKyQDDKYANVGGLKEPDFEKIAELKPDLIII-QGRQADSFDEFSKIAPTIYIDTDNQHYMKSFKEn 155
Cdd:COG4594 77 ADDNDYdRWVPYLRD-LIKGVTSVGTRSQPNLEAIAALKPDLIIAdKSRHEAIYDQLSKIAPTVLFKSRNGDYQENLES- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654964714 156 TKVLGQIFDKEDQAKKDLAAIDKQIADLKKQ--ADKLDKKALVMMANDSKMTAFGPGSKYGLIHDVFGIKAADDSLDPSA 233
Cdd:COG4594 155 FKTIAKALGKEEEAEAVLADHDQRIAEAKAKlaAADKGKKVAVGQFRADGLRLYTPNSFAGSVLAALGFENPPKQSKDNG 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 654964714 234 KHGQSIAYEYLVKQNPDYLFVVdrgaAIGEKSSAKQIVENEYVKEVNAVKNNHVVYLDPGLWYLSGG 300
Cdd:COG4594 235 YGYSEVSLEQLPALDPDVLFIA----TYDDPSILKEWKNNPLWKNLKAVKNGRVYEVDGDLWTRGRG 297
|
|
| FhuD |
cd01146 |
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial ... |
54-300 |
2.05e-42 |
|
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: 147.05 E-value: 2.05e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654964714 54 KNPKKVVVFSMGALDTLDKLGVEVAGLPKQA--IPEYLSKYQDDK-YANVGGLKEPDFEKIAELKPDLIII-QGRQADSF 129
Cdd:cd01146 1 AKPQRIVALDWGALETLLALGVKPVGVADTAgyKPWIPEPALPLEgVVDVGTRGQPNLEAIAALKPDLILGsASRHDEIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654964714 130 DEFSKIAPTIYIDTDNQhyMKSFKENTKVLGQIFDKEDQAKKDLAAIDKQIADLKKQ-ADKLDKKALVMMANDS-KMTAF 207
Cdd:cd01146 81 DQLSQIAPTVLLDSSPW--LAEWKENLRLIAKALGKEEEAEKLLAEYDQRLAELRQKlPDKGPKPVSVVRFSDAgSIRLY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654964714 208 GPGSKYG-LIHDVfGIKAADDSLDPSAKHGQSIAYEYLVKQNPDYLFVVDRGAAIGekssAKQIVENEYVKEVNAVKNNH 286
Cdd:cd01146 159 GPNSFAGsVLEDL-GLQNPWAQETTNDSGFATISLERLAKADADVLFVFTYEDEEL----AQALQANPLWQNLPAVKNGR 233
|
250
....*....|....
gi 654964714 287 VVYLDPGLWYLSGG 300
Cdd:cd01146 234 VYVVDDVWWFFGGG 247
|
|
| FepB |
COG0614 |
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ... |
58-309 |
1.11e-38 |
|
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 440379 [Multi-domain] Cd Length: 264 Bit Score: 137.44 E-value: 1.11e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654964714 58 KVVVFSMGALDTLDKLGVE--VAGLPKQAIPEYlSKYQDDKYANVGGLKEPDFEKIAELKPDLIIIQ--GRQADSFDEFS 133
Cdd:COG0614 2 RIVSLSPSATELLLALGAGdrLVGVSDWGYCDY-PELELKDLPVVGGTGEPNLEAILALKPDLVLASssGNDEEDYEQLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654964714 134 KI-APTIYIDTdnqHYMKSFKENTKVLGQIFDKEDQAKKDLAAIDKQIADLKKQADKLDKK--ALVMMANDSKMTAFGPG 210
Cdd:COG0614 81 KIgIPVVVLDP---RSLEDLYESIRLLGELLGREERAEALIAEYEARLAAVRARLAGAEERptVLYEIWSGDPLYTAGGG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654964714 211 SkygLIHDVF----GIKAADDSLDPSAKhgqsIAYEYLVKQNPDYLFVVDRGAAIGE-KSSAKQIVENEYVKEVNAVKNN 285
Cdd:COG0614 158 S---FIGELLelagGRNVAADLGGGYPE----VSLEQVLALDPDVIILSGGGYDAETaEEALEALLADPGWQSLPAVKNG 230
|
250 260
....*....|....*....|....*...
gi 654964714 286 HVVYLDPGLWYLSG----GGLESMAGMI 309
Cdd:COG0614 231 RVYVVPGDLLSRPGprllLALEDLAKAL 258
|
|
| Peripla_BP_2 |
pfam01497 |
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ... |
60-292 |
9.85e-36 |
|
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: 129.03 E-value: 9.85e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654964714 60 VVFSMGALDTLDKLGVEVAGLPKQAIPEYLSKYQDDKY-ANVGGLKEPDFEKIAELKPDLIIIQGR--QADSFDEFSKIA 136
Cdd:pfam01497 1 AALSPAYTEILYALGATDSIVGVDAYTRDPLKADAVAAiVKVGAYGEINVERLAALKPDLVILSTGylTDEAEELLSLII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654964714 137 PTIYIDTDNQHYmkSFKENTKVLGQIFDKEDQAKKDLAAIDKQIADLKKQADKLDKKALVMM--ANDSKMTAFGPGSKYG 214
Cdd:pfam01497 81 PTVIFESSSTGE--SLKEQIKQLGELLGLEDEAEELVAEIDSALAAAKKAVPSLTRKPVLVFggADGGGYVVAGSNTYIG 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 654964714 215 LIHDVFGIKAADDSLDPSAkhGQSIAYEYLVKQNPDYLFVVDRGAAIgeKSSAKQIVENEYVKEVNAVKNNHVVYLDP 292
Cdd:pfam01497 159 DLLRILGIENIAAELSGSE--YAPISFEAILSSNPDVIIVSGRDSFT--KTGPEFVAANPLWAGLPAVKNGRVYTLPS 232
|
|
| FeuA |
cd01138 |
Periplasmic binding protein FeuA. These proteins have predicted to function as initial ... |
50-300 |
2.98e-27 |
|
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: 107.03 E-value: 2.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654964714 50 IKIEKNPKKVVV---FSMGALdtldKLGVEVAGLPKQAIP-EYLSKYQDDKyaNVGGLKEPDFEKIAELKPDLIIIQGRQ 125
Cdd:cd01138 3 VEIPAKPKRIVAlsgETEGLA----LLGIKPVGAASIGGKnPYYKKKTLAK--VVGIVDEPNLEKVLELKPDLIIVSSKQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654964714 126 ADSFDEFSKIAPTIYIDTDNQHYMKSFKEntkvLGQIFDKEDQAKKDLAAIDKQIADLKKQ-ADKLDKKALVM-MANDSK 203
Cdd:cd01138 77 EENYEKLSKIAPTVPVSYNSSDWEEQLKE----IGKLLNKEDEAEKWLADYKQKAKEAKEKiKKKLGNDKSVAvLRGRKQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654964714 204 MTAFGPGSKY-GLIHDVF-GIKAADDSLDPSAKHGQ-SIAYEYLVKQNPDYLFVVDRgaaiGEKSSAKQIVENEYVKEVN 280
Cdd:cd01138 153 IYVFGEDGRGgGPILYADlGLKAPEKVKEIEDKPGYaAISLEVLPEFDADYIFLLFF----TGPEAKADFESLPIWKNLP 228
|
250 260
....*....|....*....|
gi 654964714 281 AVKNNHVVYLDPGLWYLSGG 300
Cdd:cd01138 229 AVKNNHVYIVDAWVFYFADG 248
|
|
| fecB |
PRK11411 |
iron-dicitrate transporter substrate-binding subunit; Provisional |
33-312 |
4.03e-26 |
|
iron-dicitrate transporter substrate-binding subunit; Provisional
Pssm-ID: 183123 [Multi-domain] Cd Length: 303 Bit Score: 105.14 E-value: 4.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654964714 33 SKQKETVTVTDQfnKDGIKIEKNPKKVVVFSMGALDTLDKLGVEVAGL-----PKQAIPEYLSKYQddKYANVGGLKEPD 107
Cdd:PRK11411 18 SSHAFAVTVQDE--QGTFTLEKTPQRIVVLELSFVDALAAVGVSPVGVaddndAKRILPEVRAHLK--PWQSVGTRSQPS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654964714 108 FEKIAELKPDLIIIQ-GRQADSFDEFSKIAPTIYIDTDNQHYMKSFKENTKVlGQIFDKEDQAKKDLAAIDKQIADLKKQ 186
Cdd:PRK11411 94 LEAIAALKPDLIIADsSRHAGVYIALQKIAPTLLLKSRNETYQENLQSAAII-GEVLGKKREMQARIEQHKERMAQFASQ 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654964714 187 ADKlDKKALVMMANDSKMTAFGPGSKYGLIHDVFGIKAAddSLDPSAKHGQSIAYEYLVKQNPDYLFVvdrgAAIGEKSS 266
Cdd:PRK11411 173 LPK-GTRVAFGTSREQQFNLHSPESYTGSVLAALGLNVP--KAPMNGAAMPSISLEQLLALNPDWLLV----AHYRQESI 245
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 654964714 267 AKQIVENEYVKEVNAVKNNHVVYLDPGLWYLSGGGL--ESMAGMIKEI 312
Cdd:PRK11411 246 VKRWQQDPLWQMLTAAKKQQVASVDSNTWARMRGIFaaERIAKDTVKI 293
|
|
| TroA-like |
cd00636 |
Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function ... |
57-198 |
9.94e-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: 94.55 E-value: 9.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654964714 57 KKVVVFSMGALDTLDKLGVE--VAGLPKQAIPEYLSKYQDDKYANVGGLKEPDFEKIAELKPDLIIIQGRQADSF-DEFS 133
Cdd:cd00636 1 KRVVALDPGATELLLALGGDdkPVGVADPSGYPPEAKALLEKVPDVGHGYEPNLEKIAALKPDLIIANGSGLEAWlDKLS 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 654964714 134 KIA-PTIYIDTDNQHYMKSFKENTKVLGQIFDKEDQAKKDLAAIDKQIADLKKQADKLDKKALVMM 198
Cdd:cd00636 81 KIAiPVVVVDEASELSLENIKESIRLIGKALGKEENAEELIAELDARLAELRAKLAKIPKKKVSLV 146
|
|
| FepB |
COG4592 |
ABC-type Fe2+-enterobactin transport system, periplasmic component [Inorganic ion transport ... |
1-292 |
4.05e-19 |
|
ABC-type Fe2+-enterobactin transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443649 [Multi-domain] Cd Length: 330 Bit Score: 86.15 E-value: 4.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654964714 1 MKKVLVMFVAVLTAIVVAACGNQGAKETTGGESKQKE-TVTVTDQfnKDGIKIEKNPKKVVVFSMGALDTLDKLGVEVAG 79
Cdd:COG4592 3 RRRLAAAAALLAAALLLAGCSSADSTASGTSTAAAGGwPRTVTTE--KGTVTLPAKPQRIVSTSVTLTGSLLAIDAPVVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654964714 80 lpkqAIPEYLSKYQDDK-----YANVG---GLK------EPDFEKIAELKPDLIIIQGRQADS----FDEFSKIAPTIYI 141
Cdd:COG4592 81 ----SGATTPNNVTDDQgffrqWADVAkerGVKrlyiglEPNAEAIAAAAPDLIIGSATGGDSaldlYDQLSAIAPTLVV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654964714 142 DTDNqhymKSFKENTKVLGQIFDKEDQAKKDLAAIDKQIADLkKQADKL--DKKALVMMANDSKMTAFGPGSKYGLIHDV 219
Cdd:COG4592 157 NYDD----KSWQELATQLGEATGHEAQADAVIAAFDARVAEV-KAAITLppQPVSALVYNEDGGANLWTPESAQGQLLQA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654964714 220 FGIKAAD--DSLDPSAKHGQS-----IAYEYLVKQ-NPDYLFVVDrgaaiGEKSSAKQIVENEYVKEVNAVKNNHVVYLD 291
Cdd:COG4592 232 LGFTLAPlpAELATSTSQGKRgdivqLSGENLAAAlTGPTLFLFA-----ADDKDVDALKADPLLAHLPAVQAGRVYALG 306
|
.
gi 654964714 292 P 292
Cdd:COG4592 307 P 307
|
|
| TroA_e |
cd01142 |
Periplasmic binding protein TroA_e. These proteins are predicted to function as initial ... |
32-312 |
1.69e-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: 83.94 E-value: 1.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654964714 32 ESKQKETVTVTDQFNKdGIKIEKNPKKVVVFSMGALDTldklgVEVAGLPKQAIPEYLSKYQDDKY----------ANVG 101
Cdd:cd01142 1 PAATAATRTITDMAGR-KVTIPDEVKRIAALWGAGNAV-----VAALGGGKLIVATTSTVQQEPWLyrlapslenvATGG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654964714 102 GLKEPDFEKIAELKPDLII-IQGRQADSFDEFSKIAPTIYIDTDNqhyMKSFKENTKVLGQIFDKEDQAKKDLAAIDKQI 180
Cdd:cd01142 75 TGNDVNIEELLALKPDVVIvWSTDGKEAGKAVLRLLNALSLRDAE---LEEVKLTIALLGELLGRQEKAEALVAYFDDNL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654964714 181 ADLKKQADKL--DKKALVMMANDSKMTAFGPGSkyglIHDVF-----GIKAADDSLDpsaKHGQSIAYEYLVKQNPDYLF 253
Cdd:cd01142 152 AYVAARTKKLpdSERPRVYYAGPDPLTTDGTGS----ITNSWidlagGINVASEATK---KGSGEVSLEQLLKWNPDVII 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 654964714 254 VvdrgaaiGEKSSAKQIVENEYVKEVNAVKNNHvVYLDPGLWYLSGGGLESMAGMIKEI 312
Cdd:cd01142 225 V-------GNADTKAAILADPRWQNLRAVKNGR-VYVNPEGAFWWDRPSAEEALLGLWL 275
|
|
| HemV-2 |
cd01147 |
Metal binding protein HemV-2. These proteins are predicted to function as initial receptors ... |
66-296 |
1.07e-16 |
|
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: 78.15 E-value: 1.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654964714 66 ALDTLDKL-GVEVAGLPKQAIPEYLSKYQDDKYANVGGL---KEPDFEKIAELKPDLIIIQGRQADS--FDEFSKIA--P 137
Cdd:cd01147 21 ALAAPDKIvGVDDAEKSDEGRPYFLASPELKDLPVIGRGgrgNTPNYEKIAALKPDVVIDVGSDDPTsiADDLQKKTgiP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654964714 138 TIYIDtdnqhYMKSFKENT---KVLGQIFDKEDQAKKDLAAIDKQIADLKKQADKL--DKKALVMMANDSKMTAFG---P 209
Cdd:cd01147 101 VVVLD-----GGDSLEDTPeqiRLLGKVLGKEERAEELISFIESILADVEERTKDIpdEEKPTVYFGRIGTKGAAGlesG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654964714 210 GSKYGLIHDVFGIK-AADdslDPSAKHGQSIAYEYLVKQNPDYLFVVDRGAAIGEKSSAKQiveNEYVKEVNAVKNNHvV 288
Cdd:cd01147 176 LAGSIEVFELAGGInVAD---GLGGGGLKEVSPEQILLWNPDVIFLDTGSFYLSLEGYAKN---RPFWQSLKAVKNGR-V 248
|
250
....*....|.
gi 654964714 289 YLDPGL---WY 296
Cdd:cd01147 249 YLLPALpfnWY 259
|
|
| TroA_a |
cd01148 |
Metal binding protein TroA_a. These proteins are predicted to function as initial receptors ... |
40-291 |
5.65e-16 |
|
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: 76.61 E-value: 5.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654964714 40 TVTDQFNKDGIKIEKNPKKVVVFSMGALDTLDKLGVE-----VAGLPKQAIPEYLSKYqddKYANVGGLKEPDFEKIAEL 114
Cdd:cd01148 2 PLTVENCGRSVTFDKAPQRVVSNDQNTTEMMLALGLQdrmvgTAGIDNKDLPELKAKY---DKVPELAKKYPSKETVLAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654964714 115 KPDLIIIQ-----GRQAD-SFDEFSKIAPTIYIDT------DNQHYMKSFKENTKVLGQIFDKEDQAKKDLAAIDKQIAD 182
Cdd:cd01148 79 RPDLVFGGwsygfDKGGLgTPDSLAELGIKTYILPescgqrRGEATLDDVYNDIRNLGKIFDVEDRADKLVADLKARLAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654964714 183 LKKQADKLDKKALVMMAnDSKMTAFGPGSKYGLIHDVfgIKAA--DDSLDPSAKHGQSIAYEYLVKQNPDYLFVVDRGAA 260
Cdd:cd01148 159 ISAKVKGDGKKVAVFVY-DSGEDKPFTSGRGGIPNAI--ITAAggRNVFADVDESWTTVSWETVIARNPDVIVIIDYGDQ 235
|
250 260 270
....*....|....*....|....*....|.
gi 654964714 261 IGEKSSAKQIVENEYVKEVNAVKNNHVVYLD 291
Cdd:cd01148 236 NAAEQKIKFLKENPALKNVPAVKNNRFIVLP 266
|
|
| PRK10957 |
PRK10957 |
iron-enterobactin transporter periplasmic binding protein; Provisional |
105-292 |
1.13e-14 |
|
iron-enterobactin transporter periplasmic binding protein; Provisional
Pssm-ID: 236806 [Multi-domain] Cd Length: 317 Bit Score: 73.47 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654964714 105 EPDFEKIAELKPDLIIIQGRQADS----FDEFSKIAPTIYIDTDNQhymkSFKENTKVLGQIFDKEDQAKKDLAAIDKQI 180
Cdd:PRK10957 103 EPDAEAVAAQMPDLIVISATGGDSalalYDQLSAIAPTLVIDYDDK----SWQELATQLGEATGLEKQAAAVIAQFDAQL 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654964714 181 ADLkKQADKLDKK---ALVMMANDSKMTAFGPGSKYG-LIHDV-FGIKAADDSLDPSAKHGQS-----IAYEYLVKQ-NP 249
Cdd:PRK10957 179 AEV-KAKITLPPQpvsALVYNGAGHSANLWTPESAQGqLLEQLgFTLAELPAGLQASTSQGKRhdiiqLGGENLAAGlNG 257
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 654964714 250 DYLFVVdrgaaIGEKSSAKQIVENEYVKEVNAVKNNHVVYLDP 292
Cdd:PRK10957 258 ETLFLF-----AGDDKDADAFLADPLLANLPAVQNKQVYALGT 295
|
|
| TroA_f |
cd01139 |
Periplasmic binding protein TroA_f. These proteins are predicted to function as initial ... |
39-287 |
1.22e-13 |
|
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: 70.41 E-value: 1.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654964714 39 VTVTDQFNKDgIKIEKNPKKVVVFSMGALDTL-----DKLGVEVAGLP---KQAIPEYLSKYQD-----DKYANVGGLKE 105
Cdd:cd01139 1 ITVTDVAGRK-VTLDAPVERVLLGEGRQLYALallegENPFARIVGWGgdlKKGDPDTYAKYKEkfpeiADIPLIGSTYN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654964714 106 PDF--EKIAELKPDLIIIQGRQADSFDEFSKIA-------PTIYIDTdNQHYMKSFKENTKVLGQIFDKEDQAKKDLAAI 176
Cdd:cd01139 80 GDFsvEKVLTLKPDLVILNIWAKTTAEESGILEkleqagiPVVFVDF-RQKPLKNTTPSMRLLGKALGREERAEEFIEFY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654964714 177 DKQIADLKKQADKLD-KKALVMM-----ANDSKMTAFGPGSKYGLIHDVFGIKAADDSLDPSAKhgqSIAYEYLVKQNPD 250
Cdd:cd01139 159 QERIDRIRDRLAKINePKPKVFIelgagGPEECCSTYGNGNWGELVDAAGGDNIADGLIPGTSG---ELNAEYVIAANPE 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 654964714 251 YLFVVD-------RGAAIG--------EKSSAKQIVENEYVKEVNAVKNNHV 287
Cdd:cd01139 236 IIIATGgnwakdpSGVSLGpdgttadaKESLLRALLKRPGWSSLQAVKNGRV 287
|
|
| YvrC |
cd01143 |
Periplasmic binding protein YvrC. These proteins are predicted to function as initial ... |
54-254 |
9.47e-13 |
|
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: 65.76 E-value: 9.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654964714 54 KNPKKVVVFSMGALDTLDKLGVE--VAGLPKQAI-PEYLSKYQDdkyanVGGLKEPDFEKIAELKPDLII-IQGRQADSF 129
Cdd:cd01143 1 KEPERIVSLSPSITEILFALGAGdkIVGVDTYSNyPKEVRKKPK-----VGSYSNPNVEKIVALKPDLVIvSSSSLAELL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654964714 130 DEFSKIA-PTIYIDTDNQhyMKSFKENTKVLGQIFDKEDQAKKDLAAIDKQIADLKKQADKLDK-KALVMMANDSKMTAf 207
Cdd:cd01143 76 EKLKDAGiPVVVLPAASS--LDEIYDQIELIGKITGAEEEAEKLVKEMKQKIDKVKDKGKTIKKsKVYIEVSLGGPYTA- 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 654964714 208 GPGSkygLIHDVF----GIKAADDSLDPSakhgqSIAYEYLVKQNPDYLFV 254
Cdd:cd01143 153 GKNT---FINELIrlagAKNIAADSGGWP-----QVSPEEILKANPDVIIL 195
|
|
| BtuF |
cd01144 |
Cobalamin binding protein BtuF. These proteins have been shown to function as initial ... |
95-306 |
1.16e-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: 66.55 E-value: 1.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654964714 95 DKYANVGGLKEPDFEKIAELKPDLIIIQG---RQADsFDEFSKIAPTIYIdtDNQHYMKSFKENTKVLGQIFDKEDQAKK 171
Cdd:cd01144 37 KKLPRVGGFYQLDLERVLALKPDLVIAWDdcnVCAV-VDQLRAAGIPVLV--SEPQTLDDILADIRRLGTLAGRPARAEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654964714 172 DLAAIDKQIADLKKQ-ADKLDKKALVMMANDSKMTAfgpGSKYglIHDVFGIKAADDSLDPSAKHGQSIAYEYLVKQNPD 250
Cdd:cd01144 114 LAEALRRRLAALRKQyASKPPPRVFYQEWIDPLMTA---GGDW--VPELIALAGGVNVFADAGERSPQVSWEDVLAANPD 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 654964714 251 YLFVVDRGAAIGEKSSAKqiveNEYVKEVNAVKNNHVVYLDPGlWYLSGG-----GLESMA 306
Cdd:cd01144 189 VIVLSPCGFGFTPAILRK----EPAWQALPAVRNGRVYAVDGN-WYFRPSprlvdGLEQLA 244
|
|
| ChuT |
COG4558 |
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism] ... |
98-302 |
1.64e-11 |
|
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443619 [Multi-domain] Cd Length: 285 Bit Score: 63.67 E-value: 1.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654964714 98 ANVGGLKEPDFEKIAELKPDLIII-----------QGRQAdsfdefsKIaPTIYIDTDNQhyMKSFKENTKVLGQIFDKE 166
Cdd:COG4558 67 PDVGYMRQLSAEGILSLKPTLVLAsegagppevldQLRAA-------GV-PVVVVPAAPS--LEGVLAKIRAVAAALGVP 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654964714 167 DQAKKDLAAIDKQIADLKKQADKLD--KKALVMMAND-SKMTAFGPGSKY-GLIHDVFGIKAADDsldpsAKHGQSIAYE 242
Cdd:COG4558 137 EAGEALAARLEADLAALAARVAAIGkpPRVLFLLSRGgGRPMVAGRGTAAdALIRLAGGVNAAAG-----FEGYKPLSAE 211
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 654964714 243 YLVKQNPDYLFVVDRG-AAIGeksSAKQIVENEYVKEVNAVKNNHVVYLDPGlwYLSGGGL 302
Cdd:COG4558 212 ALIAAAPDVILVMTRGlESLG---GVDGLLALPGLAQTPAGKNKRIVAMDDL--LLLGFGP 267
|
|
| PRK10576 |
PRK10576 |
Fe(3+)-hydroxamate ABC transporter substrate-binding protein FhuD; |
99-225 |
1.83e-09 |
|
Fe(3+)-hydroxamate ABC transporter substrate-binding protein FhuD;
Pssm-ID: 236719 Cd Length: 292 Bit Score: 57.72 E-value: 1.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654964714 99 NVGGLKEPDFEKIAELKPDLIIIQGRQADSFDEFSKIAPTIYID-TDNQHYMKSFKENTKVLGQIFDKEDQAKKDLAAID 177
Cdd:PRK10576 77 DVGLRTEPNLELLTQMKPSLILWSAGYGPSPEKLARIAPGRGFAfSDGKKPLAVARKSLVELAQRLNLEAAAETHLAQFD 156
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 654964714 178 KQIADLKKQADKLDKKALVMMAN-DSK-MTAFGPGSKYGLIHDVFGIKAA 225
Cdd:PRK10576 157 DFIASAKPRLAGRGQRPLLLTSLiDPRhALVFGPNSLFQEVLDELGIENA 206
|
|
| TroA_d |
cd01141 |
Periplasmic binding protein TroA_d. These proteins are predicted to function as initial ... |
49-227 |
2.50e-09 |
|
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: 55.89 E-value: 2.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654964714 49 GIKIEKNPKKVVVFSMGALDTLDKLGV--EVAGLPKQAIPEYLSKYQDDKYANVGGLKEPDFEKIAELKPDLIIIQGR-- 124
Cdd:cd01141 1 AKTIKVPPKRIVVLSPTHVDLLLALDKadKIVGVSASAYDLNTPAVKERIDIQVGPTGSLNVELIVALKPDLVILYGGfq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654964714 125 QADSFDEFSKIAPTIYIDTDNQHYMKSFKENTKVLGQ-IFDKEDQAKKDLAAIDKQIADLKKQAdKLDKKALVMMANDSK 203
Cdd:cd01141 81 AQTILDKLEQLGIPVLYVNEYPSPLGRAEWIKFAAAFyGVGKEDKADEAFAQIAGRYRDLAKKV-SNLNKPTVAIGKPVK 159
|
170 180
....*....|....*....|....*.
gi 654964714 204 MTAFGPGSK--YGLIHDVFGIKAADD 227
Cdd:cd01141 160 GLWYMPGGNsyVAKMLRDAGGRYLSA 185
|
|
| PRK14048 |
PRK14048 |
ferrichrome/ferrioxamine B periplasmic transporter; Provisional |
39-295 |
5.23e-07 |
|
ferrichrome/ferrioxamine B periplasmic transporter; Provisional
Pssm-ID: 172540 [Multi-domain] Cd Length: 374 Bit Score: 50.67 E-value: 5.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654964714 39 VTVTDQFNKDgIKIEKNPKKVVV---FSMGALDTL--DKLGVEV--AGLPKQAIPEYLSKYQDdKYANVGGLKEPD---- 107
Cdd:PRK14048 32 MTVTDAVGRE-VTIPAPPKAVLLgsgFNLIALSLIhpDPVSLLAgwSGDMKGDNPEIYESFLR-KFPELADVPLIDdgsg 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654964714 108 ----FEKIAELKPDLIIIQGRQADS------FDEFSKIA-PTIYIDTDNqHYMKSFKENTKVLGQIFDKEDQAKKDLAAI 176
Cdd:PRK14048 110 pglsFETILTLKADLAILANWQADTeagqraIEYLESIGvPVIVVDFNN-EALKNTPDNMRLLGKVFEREEQAEDFARFY 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654964714 177 DKQIADLKKQADKL-DKKALVMM----ANDSKMTAFGPGSKYGLIHDVFGIKAADDSLdpsAKHGQSIAYEYLVKQNPDY 251
Cdd:PRK14048 189 EERLARIRDRVAKHsEPGPTVLMeafpAADRCCWAYGRGGLGEFIALTGSRNIAEGAL---PRPGGMMNAEAIMAENPDV 265
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 654964714 252 LFVVD------RGAAIGEKSSAKQ-------IVENEYVKEVNAVKNNHVvyldPGLW 295
Cdd:PRK14048 266 YIATSspggkySGFSIGPGVSAEEaettlanVVDKPVMASIAAVRDGRV----HGLW 318
|
|
| NlpA |
COG1464 |
ABC-type metal ion transport system, periplasmic component/surface antigen [Inorganic ion ... |
1-63 |
2.75e-03 |
|
ABC-type metal ion transport system, periplasmic component/surface antigen [Inorganic ion transport and metabolism];
Pssm-ID: 441073 [Multi-domain] Cd Length: 270 Bit Score: 38.55 E-value: 2.75e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 654964714 1 MKKVLVMFVAVLTAIVVAACGNQGAKETtggeSKQKETVTV--------------TDQFNKDGIKIEknpkkVVVFS 63
Cdd:COG1464 1 MKKLLALLLALALALALAACGSSSAAAA----AADKKTIKVgatpgphaeilevvKPELAKKGIDLE-----IVEFT 68
|
|
| YifL |
COG5567 |
Small periplasmic lipoprotein YifL (function unknown) [Function unknown]; |
1-40 |
4.17e-03 |
|
Small periplasmic lipoprotein YifL (function unknown) [Function unknown];
Pssm-ID: 444309 Cd Length: 43 Bit Score: 34.50 E-value: 4.17e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 654964714 1 MKKVLVMFVAVLTAIVVAACGNQGAKETTGGESKQKETVT 40
Cdd:COG5567 1 MKKLLRLLLLLLLLFTLAGCGLKGPLYLPPAEKEKQPSQK 40
|
|
| |
