|
Name |
Accession |
Description |
Interval |
E-value |
| FepB |
COG0614 |
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ... |
61-310 |
2.31e-53 |
|
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 440379 [Multi-domain] Cd Length: 264 Bit Score: 175.57 E-value: 2.31e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671141 61 ATLSMGDMDIIHALGG--KIIGRPDTK-LTLPE-ELKKAQVIGNAHQPNFEQIASLKPDVLVANNGF--QKNVPTVEGQG 134
Cdd:COG0614 4 VSLSPSATELLLALGAgdRLVGVSDWGyCDYPElELKDLPVVGGTGEPNLEAILALKPDLVLASSSGndEEDYEQLEKIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671141 135 TKVVISTANSVQDIQKNIEIYGAVMKKEDKAKELNQKMNDQMKKYEKKSD-----VKALLVYGAPGTYLAALPTSLSGDI 209
Cdd:COG0614 84 IPVVVLDPRSLEDLYESIRLLGELLGREERAEALIAEYEARLAAVRARLAgaeerPTVLYEIWSGDPLYTAGGGSFIGEL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671141 210 LEKTGGKNIAAGFPEMkeypqYAQLSVERIIEANPDVIYLITHGDPNSVKKAFEGEMMKNEAWKNLDAVKQNRVVILPPD 289
Cdd:COG0614 164 LELAGGRNVAADLGGG-----YPEVSLEQVLALDPDVIILSGGGYDAETAEEALEALLADPGWQSLPAVKNGRVYVVPGD 238
|
250 260
....*....|....*....|.
gi 446671141 290 LFgSNPGTKVTEAMDFMYKSI 310
Cdd:COG0614 239 LL-SRPGPRLLLALEDLAKAL 258
|
|
| IsdE |
TIGR03659 |
heme ABC transporter, heme-binding protein isdE; This family of ABC substrate-binding proteins ... |
2-308 |
2.81e-51 |
|
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: 170.92 E-value: 2.81e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671141 2 KKSITLFTAILSVFFLlIGCnakGNDKASATKTEKGKEKIEITdlsgrkvtfdktpesfATlSMGDMDIIHALGGKIIGR 81
Cdd:TIGR03659 1 KKILSLVLLAVLSLGL-TGC---SSSKEKSKVSNKKSKEERIV----------------AT-SVAVTEILDKLDLDLVGV 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671141 82 PDTKLTLPEELKKAQVIGNAHQPNFEQIASLKPDVLVANNGFQKNV-PTVEGQGTKVVISTANSVQDIQKNIEIYGAVMK 160
Cdd:TIGR03659 60 PTSQKTLPKRYKDVPEVGNPMSPDMEKIKSLKPTVVLSVTTLEEDLgPKFKQLGVEATFLNLTSVDGMKKSITELGEKYG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671141 161 KEDKAKELNQKMNDQMKKYEKKSD----VKALLVYGAPGTYLAALPTSLSGDILEKTGGKNIAAGfpemkEYPQYAQLSV 236
Cdd:TIGR03659 140 REEQAEKLVKEINEKEAEVKKKVKgkkkPKVLILMGVPGSYLVATENSYIGDLVKLAGGENVYKG-----NKQEYLSSNT 214
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446671141 237 ERIIEANPDVIYLITHGDPNSVKKAFEGEMMKNEAWKNLDAVKQNRVVILPPDLFGSNPGTKVTEAMDFMYK 308
Cdd:TIGR03659 215 EYLLKANPDIILRAAHGMPDEVKKMFDEEFKTNDIWKHFEAVKNNRVYDLDEELFGMTANLKVAEALDELKK 286
|
|
| FatB |
cd01140 |
Siderophore binding protein FatB. These proteins have been shown to function as ABC-type ... |
50-312 |
4.36e-42 |
|
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: 146.63 E-value: 4.36e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671141 50 KVTFDKTPESFATLSMGDMDIIHALGGKIIGRPDTKlTLPEELKKAQ-----VIGNAHQPNFEQIASLKPDVLVANNGFQ 124
Cdd:cd01140 5 ETKVPKNPEKVVVFDVGALDTLDALGVKVVGVPKSS-TLPEYLKKYKddkyaNVGTLFEPDLEAIAALKPDLIIIGGRLA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671141 125 -------KNVPTVEGQgtkvvISTANSVQDIQKNIEIYGAVMKKEDKAKELNQKMNDQMKKYEK--KSDVKALLVYGAPG 195
Cdd:cd01140 84 ekydelkKIAPTIDLG-----ADLKNYLESVKQNIETLGKIFGKEEEAKELVAEIDASIAEAKSaaKGKKKALVVLVNGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671141 196 TYLAALPTSLSGDILEKTGGKNIAagfPEMKEYPQYAQLSVERIIEANPDVIYLITHGDPNSVKKAFEGEMMKNEAWKNL 275
Cdd:cd01140 159 KLSAFGPGSRFGWLHDLLGFEPAD---ENIKASSHGQPVSFEYILEANPDWLFVIDRGAAIGAEGSSAKEVLDNDLVKNT 235
|
250 260 270
....*....|....*....|....*....|....*..
gi 446671141 276 DAVKQNRVVILPPDLFGSNPGtkVTEAMDFMYKSIQD 312
Cdd:cd01140 236 TAWKNGKVIYLDPDLWYLSGG--GLESLKQMIDDLKK 270
|
|
| Peripla_BP_2 |
pfam01497 |
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ... |
61-289 |
1.39e-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: 117.85 E-value: 1.39e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671141 61 ATLSMGDMDIIHALGGKIIGRPDTKLTLPEELKKAQ----VIGNAHQPNFEQIASLKPDVLVANNGFQ---------KNV 127
Cdd:pfam01497 1 AALSPAYTEILYALGATDSIVGVDAYTRDPLKADAVaaivKVGAYGEINVERLAALKPDLVILSTGYLtdeaeellsLII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671141 128 PTVEgqgtkvvISTANSVQDIQKNIEIYGAVMKKEDKAKELNQKMNDQM----KKYEKKSDVKALLVYGAP-GTYLAALP 202
Cdd:pfam01497 81 PTVI-------FESSSTGESLKEQIKQLGELLGLEDEAEELVAEIDSALaaakKAVPSLTRKPVLVFGGADgGGYVVAGS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671141 203 TSLSGDILEKTGGKNIAAGfpEMKEypQYAQLSVERIIEANPDVIYLITHGDPNSVKKAFegeMMKNEAWKNLDAVKQNR 282
Cdd:pfam01497 154 NTYIGDLLRILGIENIAAE--LSGS--EYAPISFEAILSSNPDVIIVSGRDSFTKTGPEF---VAANPLWAGLPAVKNGR 226
|
....*..
gi 446671141 283 VVILPPD 289
Cdd:pfam01497 227 VYTLPSD 233
|
|
| btuF |
PRK09534 |
corrinoid ABC transporter substrate-binding protein; Reviewed |
9-306 |
2.08e-17 |
|
corrinoid ABC transporter substrate-binding protein; Reviewed
Pssm-ID: 236552 [Multi-domain] Cd Length: 359 Bit Score: 81.49 E-value: 2.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671141 9 TAILSVFFLLIGCNAKGNDKASATKTEKGKEK------IEITDLSGRKVTFDKTPESFATLSMGDMDIIHALGGK--IIG 80
Cdd:PRK09534 6 FRSLVIVALAVTMTAAGGALAPAPAAQHADADracsfpVTETDATGTEITLDERPERVVTLNPSAAQTMWELGARdrVVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671141 81 RPDTKLTLPEELKKAQVIGNA-HQPNFEQIASLKPDVLVANNGFQ-KNVPTVEGQGTKVV-ISTANSVQDIQKNIEIYGA 157
Cdd:PRK09534 86 VTQYASYLDGAEERTNVSGGQpFGVNVEAVVGLDPDLVLAPNAVAgDTVTRLREAGITVFhFPAATSIEDVAEKTATIGR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671141 158 VMKKEDKAKELNQKMNDQMKKYEKKS---DVKALLVYGAPGTYLAAlPTSLSGDILEKTGGKNIAAGfpemKEYPQYAQL 234
Cdd:PRK09534 166 LTGNCEAAAETNAEMRDRVDAVEDRTadvDDRPRVLYPLGDGYTAG-GNTFIGALIEAAGGHNVAAD----ATTDGYPQL 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446671141 235 SVERIIEANPDVIYLITHGDPnsvkkafegeMMKNEAWKNLDAVKQNRVVILPPDLFgSNPGTKVTEAMDFM 306
Cdd:PRK09534 241 SEEVIVQQDPDVIVVATASAL----------VAETEPYASTTAGETGNVVTVNVNHI-NQPAPRIVESMATM 301
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| FepB |
COG0614 |
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ... |
61-310 |
2.31e-53 |
|
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 440379 [Multi-domain] Cd Length: 264 Bit Score: 175.57 E-value: 2.31e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671141 61 ATLSMGDMDIIHALGG--KIIGRPDTK-LTLPE-ELKKAQVIGNAHQPNFEQIASLKPDVLVANNGF--QKNVPTVEGQG 134
Cdd:COG0614 4 VSLSPSATELLLALGAgdRLVGVSDWGyCDYPElELKDLPVVGGTGEPNLEAILALKPDLVLASSSGndEEDYEQLEKIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671141 135 TKVVISTANSVQDIQKNIEIYGAVMKKEDKAKELNQKMNDQMKKYEKKSD-----VKALLVYGAPGTYLAALPTSLSGDI 209
Cdd:COG0614 84 IPVVVLDPRSLEDLYESIRLLGELLGREERAEALIAEYEARLAAVRARLAgaeerPTVLYEIWSGDPLYTAGGGSFIGEL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671141 210 LEKTGGKNIAAGFPEMkeypqYAQLSVERIIEANPDVIYLITHGDPNSVKKAFEGEMMKNEAWKNLDAVKQNRVVILPPD 289
Cdd:COG0614 164 LELAGGRNVAADLGGG-----YPEVSLEQVLALDPDVIILSGGGYDAETAEEALEALLADPGWQSLPAVKNGRVYVVPGD 238
|
250 260
....*....|....*....|.
gi 446671141 290 LFgSNPGTKVTEAMDFMYKSI 310
Cdd:COG0614 239 LL-SRPGPRLLLALEDLAKAL 258
|
|
| IsdE |
TIGR03659 |
heme ABC transporter, heme-binding protein isdE; This family of ABC substrate-binding proteins ... |
2-308 |
2.81e-51 |
|
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: 170.92 E-value: 2.81e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671141 2 KKSITLFTAILSVFFLlIGCnakGNDKASATKTEKGKEKIEITdlsgrkvtfdktpesfATlSMGDMDIIHALGGKIIGR 81
Cdd:TIGR03659 1 KKILSLVLLAVLSLGL-TGC---SSSKEKSKVSNKKSKEERIV----------------AT-SVAVTEILDKLDLDLVGV 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671141 82 PDTKLTLPEELKKAQVIGNAHQPNFEQIASLKPDVLVANNGFQKNV-PTVEGQGTKVVISTANSVQDIQKNIEIYGAVMK 160
Cdd:TIGR03659 60 PTSQKTLPKRYKDVPEVGNPMSPDMEKIKSLKPTVVLSVTTLEEDLgPKFKQLGVEATFLNLTSVDGMKKSITELGEKYG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671141 161 KEDKAKELNQKMNDQMKKYEKKSD----VKALLVYGAPGTYLAALPTSLSGDILEKTGGKNIAAGfpemkEYPQYAQLSV 236
Cdd:TIGR03659 140 REEQAEKLVKEINEKEAEVKKKVKgkkkPKVLILMGVPGSYLVATENSYIGDLVKLAGGENVYKG-----NKQEYLSSNT 214
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446671141 237 ERIIEANPDVIYLITHGDPNSVKKAFEGEMMKNEAWKNLDAVKQNRVVILPPDLFGSNPGTKVTEAMDFMYK 308
Cdd:TIGR03659 215 EYLLKANPDIILRAAHGMPDEVKKMFDEEFKTNDIWKHFEAVKNNRVYDLDEELFGMTANLKVAEALDELKK 286
|
|
| FatB |
cd01140 |
Siderophore binding protein FatB. These proteins have been shown to function as ABC-type ... |
50-312 |
4.36e-42 |
|
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: 146.63 E-value: 4.36e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671141 50 KVTFDKTPESFATLSMGDMDIIHALGGKIIGRPDTKlTLPEELKKAQ-----VIGNAHQPNFEQIASLKPDVLVANNGFQ 124
Cdd:cd01140 5 ETKVPKNPEKVVVFDVGALDTLDALGVKVVGVPKSS-TLPEYLKKYKddkyaNVGTLFEPDLEAIAALKPDLIIIGGRLA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671141 125 -------KNVPTVEGQgtkvvISTANSVQDIQKNIEIYGAVMKKEDKAKELNQKMNDQMKKYEK--KSDVKALLVYGAPG 195
Cdd:cd01140 84 ekydelkKIAPTIDLG-----ADLKNYLESVKQNIETLGKIFGKEEEAKELVAEIDASIAEAKSaaKGKKKALVVLVNGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671141 196 TYLAALPTSLSGDILEKTGGKNIAagfPEMKEYPQYAQLSVERIIEANPDVIYLITHGDPNSVKKAFEGEMMKNEAWKNL 275
Cdd:cd01140 159 KLSAFGPGSRFGWLHDLLGFEPAD---ENIKASSHGQPVSFEYILEANPDWLFVIDRGAAIGAEGSSAKEVLDNDLVKNT 235
|
250 260 270
....*....|....*....|....*....|....*..
gi 446671141 276 DAVKQNRVVILPPDLFGSNPGtkVTEAMDFMYKSIQD 312
Cdd:cd01140 236 TAWKNGKVIYLDPDLWYLSGG--GLESLKQMIDDLKK 270
|
|
| FecB |
COG4594 |
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and ... |
1-303 |
2.50e-39 |
|
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443650 [Multi-domain] Cd Length: 316 Bit Score: 140.44 E-value: 2.50e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671141 1 MKKsITLFTAILSVFFLLIGCnakGNDKASATKTEKGKEKIEITDLSGrKVTFDKTPESFATLSMGDMDIIHALGGKIIG 80
Cdd:COG4594 1 MKK-LLLLLILLLALLLLAAC---GSSSSDSSSSEAAAGARTVKHAMG-ETTIPGTPKRVVVLEWSFADALLALGVTPVG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671141 81 RPDTKLTLP------EELKKAQVIGNAHQPNFEQIASLKPDVLVANNGFQKNV--------PTVEGQgtkvviSTANSVQ 146
Cdd:COG4594 76 IADDNDYDRwvpylrDLIKGVTSVGTRSQPNLEAIAALKPDLIIADKSRHEAIydqlskiaPTVLFK------SRNGDYQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671141 147 DIQKNIEIYGAVMKKEDKAKELNQKMNDQMKKY-----EKKSDVKALLVYGAPGTYLAALPTSLSGDILEKTGGKNIAAG 221
Cdd:COG4594 150 ENLESFKTIAKALGKEEEAEAVLADHDQRIAEAkaklaAADKGKKVAVGQFRADGLRLYTPNSFAGSVLAALGFENPPKQ 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671141 222 fPEMKEYPqYAQLSVERIIEANPDVIYLITHGDPnsvkkAFEGEMMKNEAWKNLDAVKQNRVVILPPDLFGSNPGTKVTE 301
Cdd:COG4594 230 -SKDNGYG-YSEVSLEQLPALDPDVLFIATYDDP-----SILKEWKNNPLWKNLKAVKNGRVYEVDGDLWTRGRGPLAAE 302
|
..
gi 446671141 302 AM 303
Cdd:COG4594 303 LM 304
|
|
| FhuD |
cd01146 |
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial ... |
55-304 |
3.12e-39 |
|
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: 138.57 E-value: 3.12e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671141 55 KTPESFATLSMGDMDIIHALGGKIIGRPDTK------LTLPEELKKAQVIGNAHQPNFEQIASLKPDVLVANNGFQKNV- 127
Cdd:cd01146 1 AKPQRIVALDWGALETLLALGVKPVGVADTAgykpwiPEPALPLEGVVDVGTRGQPNLEAIAALKPDLILGSASRHDEIy 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671141 128 -------PTvegqgtkVVISTANSVQDIQKNIEIYGAVMKKEDKAKELNQKMNDQM----KKYEKKSDVKALLV-YGAPG 195
Cdd:cd01146 81 dqlsqiaPT-------VLLDSSPWLAEWKENLRLIAKALGKEEEAEKLLAEYDQRLaelrQKLPDKGPKPVSVVrFSDAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671141 196 TYLAALPTSLSGDILEKTGGKNIAAgfPEMKEYPQYAQLSVERIIEANPDVIYLITHGDPNSVKKafegeMMKNEAWKNL 275
Cdd:cd01146 154 SIRLYGPNSFAGSVLEDLGLQNPWA--QETTNDSGFATISLERLAKADADVLFVFTYEDEELAQA-----LQANPLWQNL 226
|
250 260
....*....|....*....|....*....
gi 446671141 276 DAVKQNRVVILPPDLFGSNPGTKVTEAMD 304
Cdd:cd01146 227 PAVKNGRVYVVDDVWWFFGGGLSAARLLL 255
|
|
| CeuA |
COG4607 |
ABC-type enterochelin transport system, periplasmic component [Inorganic ion transport and ... |
1-291 |
5.19e-37 |
|
ABC-type enterochelin transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443657 [Multi-domain] Cd Length: 310 Bit Score: 134.15 E-value: 5.19e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671141 1 MKKSITLFTAILSVFfLLIGCNAKGNDKASATKtekgKEKIEITDLSGrKVTFDKTPESFATLSMGDMDIIHALGGKIIG 80
Cdd:COG4607 1 MKKTLLAALALAAAL-ALAACGSSSAAAASAAA----AETVTVEHALG-TVEVPKNPKRVVVFDNGALDTLDALGVEVAG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671141 81 RPDTklTLPEELKK-----AQVIGNAHQPNFEQIASLKPDVLVANNGFQKN-------VPTVEgqgtkVVISTANSVQDI 148
Cdd:COG4607 75 VPKG--LLPDYLSKyaddkYANVGTLFEPDLEAIAALKPDLIIIGGRSAKKydelskiAPTID-----LTVDGEDYLESL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671141 149 QKNIEIYGAVMKKEDKAKELNQKMNDQM----KKYEKKSDVKALLVYGapGTYLAALPTSLSGDILEKTG----GKNIAA 220
Cdd:COG4607 148 KRNTETLGEIFGKEDEAEELVADLDAKIaalkAAAAGKGTALIVLTNG--GKISAYGPGSRFGPIHDVLGfkpaDEDIEA 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446671141 221 GfpemkeypQYAQ-LSVERIIEANPDVIYLI-----THGDPNSVKkafegEMMKNEAWKNLDAVKQNRVVILPPDLF 291
Cdd:COG4607 226 S--------THGQaISFEFIAEANPDWLFVIdrdaaIGGEGPAAK-----QVLDNELVKQTTAWKNGQIVYLDPDAW 289
|
|
| Peripla_BP_2 |
pfam01497 |
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ... |
61-289 |
1.39e-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: 117.85 E-value: 1.39e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671141 61 ATLSMGDMDIIHALGGKIIGRPDTKLTLPEELKKAQ----VIGNAHQPNFEQIASLKPDVLVANNGFQ---------KNV 127
Cdd:pfam01497 1 AALSPAYTEILYALGATDSIVGVDAYTRDPLKADAVaaivKVGAYGEINVERLAALKPDLVILSTGYLtdeaeellsLII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671141 128 PTVEgqgtkvvISTANSVQDIQKNIEIYGAVMKKEDKAKELNQKMNDQM----KKYEKKSDVKALLVYGAP-GTYLAALP 202
Cdd:pfam01497 81 PTVI-------FESSSTGESLKEQIKQLGELLGLEDEAEELVAEIDSALaaakKAVPSLTRKPVLVFGGADgGGYVVAGS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671141 203 TSLSGDILEKTGGKNIAAGfpEMKEypQYAQLSVERIIEANPDVIYLITHGDPNSVKKAFegeMMKNEAWKNLDAVKQNR 282
Cdd:pfam01497 154 NTYIGDLLRILGIENIAAE--LSGS--EYAPISFEAILSSNPDVIIVSGRDSFTKTGPEF---VAANPLWAGLPAVKNGR 226
|
....*..
gi 446671141 283 VVILPPD 289
Cdd:pfam01497 227 VYTLPSD 233
|
|
| TroA_e |
cd01142 |
Periplasmic binding protein TroA_e. These proteins are predicted to function as initial ... |
42-287 |
2.27e-30 |
|
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: 116.30 E-value: 2.27e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671141 42 EITDLSGRKVTFDKTPESFATLSMGDMDIIHALGG--KIIGRPDTKLTLPE------ELKKAQVIGNAHQPNFEQIASLK 113
Cdd:cd01142 9 TITDMAGRKVTIPDEVKRIAALWGAGNAVVAALGGgkLIVATTSTVQQEPWlyrlapSLENVATGGTGNDVNIEELLALK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671141 114 PDVLVANNGFQKNVPTVEGQGTKVVISTANSVQDIQKNIEIYGAVMKKEDKAKELNQKMNDQMKKYEKK----SDVKALL 189
Cdd:cd01142 89 PDVVIVWSTDGKEAGKAVLRLLNALSLRDAELEEVKLTIALLGELLGRQEKAEALVAYFDDNLAYVAARtkklPDSERPR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671141 190 VYGAPGTYLAALPT-SLSGDILEKTGGKNIA--AGFPEMKEYpqyaqlSVERIIEANPDVIyLITHGDPnsvKKAFEGem 266
Cdd:cd01142 169 VYYAGPDPLTTDGTgSITNSWIDLAGGINVAseATKKGSGEV------SLEQLLKWNPDVI-IVGNADT---KAAILA-- 236
|
250 260
....*....|....*....|.
gi 446671141 267 mkNEAWKNLDAVKQNRVVILP 287
Cdd:cd01142 237 --DPRWQNLRAVKNGRVYVNP 255
|
|
| ChuT |
COG4558 |
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism] ... |
69-292 |
1.33e-29 |
|
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443619 [Multi-domain] Cd Length: 285 Bit Score: 113.75 E-value: 1.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671141 69 DIIHALG--GKIIGRpDTKLTLPEELKKAQVIGNAHQPNFEQIASLKPDVLVANNGFQKnvPTV----EGQGTKVV-IST 141
Cdd:COG4558 39 EIVYALGagDRLVGV-DTTSTYPAAAKALPDVGYMRQLSAEGILSLKPTLVLASEGAGP--PEVldqlRAAGVPVVvVPA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671141 142 ANSVQDIQKNIEIYGAVMKKEDKAKELNQKMNDQMKKYEK-----KSDVKALLVYG-APGTYLAALPTSLSGDILEKTGG 215
Cdd:COG4558 116 APSLEGVLAKIRAVAAALGVPEAGEALAARLEADLAALAArvaaiGKPPRVLFLLSrGGGRPMVAGRGTAADALIRLAGG 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671141 216 KNIAAGFPEMKeypqyaQLSVERIIEANPDVIYLITHGdpnsvKKAFEG--EMMKNEAWKNLDAVKQNRVVILPPDL--- 290
Cdd:COG4558 196 VNAAAGFEGYK------PLSAEALIAAAPDVILVMTRG-----LESLGGvdGLLALPGLAQTPAGKNKRIVAMDDLLllg 264
|
..
gi 446671141 291 FG 292
Cdd:COG4558 265 FG 266
|
|
| TroA_a |
cd01148 |
Metal binding protein TroA_a. These proteins are predicted to function as initial receptors ... |
48-302 |
8.06e-28 |
|
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: 109.35 E-value: 8.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671141 48 GRKVTFDKTPESFATLSMGDMDIIHALG--GKIIGR--PDTKL--TLPEELKKAQVIGnAHQPNFEQIASLKPDVLVA-- 119
Cdd:cd01148 9 GRSVTFDKAPQRVVSNDQNTTEMMLALGlqDRMVGTagIDNKDlpELKAKYDKVPELA-KKYPSKETVLAARPDLVFGgw 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671141 120 NNGFQKNVP----TVEGQGTKVVISTAN--------SVQDIQKNIEIYGAVMKKEDKAKELNQKMNDQ----MKKYEKKS 183
Cdd:cd01148 88 SYGFDKGGLgtpdSLAELGIKTYILPEScgqrrgeaTLDDVYNDIRNLGKIFDVEDRADKLVADLKARlaeiSAKVKGDG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671141 184 DVKALLVY----GAPGTYLAAlptSLSGDILEKTGGKNIAAgfpEMKEypQYAQLSVERIIEANPDVIYLITHGDPNSVK 259
Cdd:cd01148 168 KKVAVFVYdsgeDKPFTSGRG---GIPNAIITAAGGRNVFA---DVDE--SWTTVSWETVIARNPDVIVIIDYGDQNAAE 239
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 446671141 260 KAfEGEMMKNEAWKNLDAVKQNRVVILPpdLFGSNPGTKVTEA 302
Cdd:cd01148 240 QK-IKFLKENPALKNVPAVKNNRFIVLP--LAEATPGIRNVDA 279
|
|
| YvrC |
cd01143 |
Periplasmic binding protein YvrC. These proteins are predicted to function as initial ... |
55-247 |
3.59e-27 |
|
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: 105.05 E-value: 3.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671141 55 KTPESFATLSMGDMDIIHALGG--KIIGRpDTKLTLPEELKKAQVIGNAHQPNFEQIASLKPDVLVANNGFQK-NVPTVE 131
Cdd:cd01143 1 KEPERIVSLSPSITEILFALGAgdKIVGV-DTYSNYPKEVRKKPKVGSYSNPNVEKIVALKPDLVIVSSSSLAeLLEKLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671141 132 GQGTKVVIS-TANSVQDIQKNIEIYGAVMKKEDKAKELNQKMNDQMKKYEKK-SDVKALLVY---GAPGTYLAALPTSLs 206
Cdd:cd01143 80 DAGIPVVVLpAASSLDEIYDQIELIGKITGAEEEAEKLVKEMKQKIDKVKDKgKTIKKSKVYievSLGGPYTAGKNTFI- 158
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446671141 207 GDILEKTGGKNIAAgfpemkEYPQYAQLSVERIIEANPDVI 247
Cdd:cd01143 159 NELIRLAGAKNIAA------DSGGWPQVSPEEILKANPDVI 193
|
|
| HemV-2 |
cd01147 |
Metal binding protein HemV-2. These proteins are predicted to function as initial receptors ... |
58-293 |
4.80e-25 |
|
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: 101.26 E-value: 4.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671141 58 ESFATLSMGDMDIIHALGG--KIIGRPDTKLT--------LPEELKKAQVIGNAH---QPNFEQIASLKPDVLVA--NNG 122
Cdd:cd01147 6 ERVVAAGPGALRLLYALAApdKIVGVDDAEKSdegrpyflASPELKDLPVIGRGGrgnTPNYEKIAALKPDVVIDvgSDD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671141 123 FQKNVPTVEGQG--TKVVISTANSVQDIQKNIEIYGAVMKKEDKAKELNQKMNDQMKKYEKK----SDVKALLVYGAPGT 196
Cdd:cd01147 86 PTSIADDLQKKTgiPVVVLDGGDSLEDTPEQIRLLGKVLGKEERAEELISFIESILADVEERtkdiPDEEKPTVYFGRIG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671141 197 YLAA--LPTSLSGDI--LEKTGGKNIAAGfpemKEYPQYAQLSVERIIEANPDVIYLithgDPNSVKKAFEGEMMKNEAW 272
Cdd:cd01147 166 TKGAagLESGLAGSIevFELAGGINVADG----LGGGGLKEVSPEQILLWNPDVIFL----DTGSFYLSLEGYAKNRPFW 237
|
250 260
....*....|....*....|.
gi 446671141 273 KNLDAVKQNRVVILPPDLFGS 293
Cdd:cd01147 238 QSLKAVKNGRVYLLPALPFNW 258
|
|
| BtuF |
cd01144 |
Cobalamin binding protein BtuF. These proteins have been shown to function as initial ... |
69-308 |
2.19e-24 |
|
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: 98.91 E-value: 2.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671141 69 DIIHALG--GKIIGRPDtKLTLPEELKKAQVIGNAHQPNFEQIASLKPDVLVANNGFQK--NVPTVEGQGTKVVISTANS 144
Cdd:cd01144 12 ELLYALGlgDQLVGVTD-YCDYPPEAKKLPRVGGFYQLDLERVLALKPDLVIAWDDCNVcaVVDQLRAAGIPVLVSEPQT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671141 145 VQDIQKNIE----IYGAVMKKEDKAKELNQKMNDQMKKYEKKSDVKALL------VYGAPGTYLAalptslsgDILEKTG 214
Cdd:cd01144 91 LDDILADIRrlgtLAGRPARAEELAEALRRRLAALRKQYASKPPPRVFYqewidpLMTAGGDWVP--------ELIALAG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671141 215 GKNIAAGFPEmkEYPqyaQLSVERIIEANPDVIylITHGDPNSVKKAFEGemmKNEAWKNLDAVKQNRVVILPPDLFGsN 294
Cdd:cd01144 163 GVNVFADAGE--RSP---QVSWEDVLAANPDVI--VLSPCGFGFTPAILR---KEPAWQALPAVRNGRVYAVDGNWYF-R 231
|
250
....*....|....
gi 446671141 295 PGTKVTEAMDFMYK 308
Cdd:cd01144 232 PSPRLVDGLEQLAA 245
|
|
| TroA_f |
cd01139 |
Periplasmic binding protein TroA_f. These proteins are predicted to function as initial ... |
41-283 |
1.11e-22 |
|
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: 96.22 E-value: 1.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671141 41 IEITDLSGRKVTFDKTPESFAtlsMGDMDIIHAL--------GGKIIG-RPDTKLTLPE----------ELKKAQVIGNA 101
Cdd:cd01139 1 ITVTDVAGRKVTLDAPVERVL---LGEGRQLYALallegenpFARIVGwGGDLKKGDPDtyakykekfpEIADIPLIGST 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671141 102 HQPNF--EQIASLKPDVLVANNGFQKN------VPTVEGQGTKVVISTANsvQDIQKN----IEIYGAVMKKEDKAKELN 169
Cdd:cd01139 78 YNGDFsvEKVLTLKPDLVILNIWAKTTaeesgiLEKLEQAGIPVVFVDFR--QKPLKNttpsMRLLGKALGREERAEEFI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671141 170 QKMNDQMKKY--------EKKSDVKALLVYGAPGTYLAALPTSLSGDILEKTGGKNIAAGFPEMkeypQYAQLSVERIIE 241
Cdd:cd01139 156 EFYQERIDRIrdrlakinEPKPKVFIELGAGGPEECCSTYGNGNWGELVDAAGGDNIADGLIPG----TSGELNAEYVIA 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 446671141 242 ANPDvIYLITHGD----PNSV-----------KKAFEGEMMKNEAWKNLDAVKQNRV 283
Cdd:cd01139 232 ANPE-IIIATGGNwakdPSGVslgpdgttadaKESLLRALLKRPGWSSLQAVKNGRV 287
|
|
| HutB |
cd01149 |
Hemin binding protein HutB. These proteins have been shown to function as initial receptors ... |
70-255 |
3.08e-20 |
|
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: 87.32 E-value: 3.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671141 70 IIHALGG--KIIGRpDTKLTLPEELKKAQVIGNAHQPNFEQIASLKPDVLVAN--NGFQKNVPTVEGQGTKVV-ISTANS 144
Cdd:cd01149 14 IVYALGAgdRLVGV-DSTSTYPEAAAKLPDVGYMRQLSAEGVLSLKPTLVIASdeAGPPEALDQLRAAGVPVVtVPSTPT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671141 145 VQDIQKNIEIYGAVMKKEDKAKELNQKMNDQMKKYEK-----KSDVKALLVYG-APGTYLAALPTSLSGDILEKTGGKNI 218
Cdd:cd01149 93 LDGLLTKIRQVAQALGVPEKGEALAQEVRQRLAALRKtvaahKKPPRVLFLLShGGGAAMAAGRNTAADAIIALAGAVNA 172
|
170 180 190
....*....|....*....|....*....|....*..
gi 446671141 219 AAGFPemkeypQYAQLSVERIIEANPDVIYLITHGDP 255
Cdd:cd01149 173 AAGFR------GYKPLSAEALIAAQPDVILVMSRGLD 203
|
|
| FeuA |
cd01138 |
Periplasmic binding protein FeuA. These proteins have predicted to function as initial ... |
49-296 |
5.33e-19 |
|
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: 84.31 E-value: 5.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671141 49 RKVTFDKTPESFATLSMGDMDIIhALGGKIIGRPDTKLTLPEELKK--AQVIGNAHQPNFEQIASLKPDVLVANNGFQKN 126
Cdd:cd01138 1 GEVEIPAKPKRIVALSGETEGLA-LLGIKPVGAASIGGKNPYYKKKtlAKVVGIVDEPNLEKVLELKPDLIIVSSKQEEN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671141 127 VPTVEGQGTKVVISTANSvqDIQKNIEIYGAVMKKEDKAKELNQKMNDQMKKYEKKSD--------------VKALLVYG 192
Cdd:cd01138 80 YEKLSKIAPTVPVSYNSS--DWEEQLKEIGKLLNKEDEAEKWLADYKQKAKEAKEKIKkklgndksvavlrgRKQIYVFG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671141 193 APGTYlaalptslSGDILEKTGGKNIAAGFPEMKEYPQYAQLSVERIIEANPDVIYLITHGDPnSVKKAFEgemmKNEAW 272
Cdd:cd01138 158 EDGRG--------GGPILYADLGLKAPEKVKEIEDKPGYAAISLEVLPEFDADYIFLLFFTGP-EAKADFE----SLPIW 224
|
250 260
....*....|....*....|....
gi 446671141 273 KNLDAVKQNRVVILPPDLFGSNPG 296
Cdd:cd01138 225 KNLPAVKNNHVYIVDAWVFYFADG 248
|
|
| btuF |
PRK09534 |
corrinoid ABC transporter substrate-binding protein; Reviewed |
9-306 |
2.08e-17 |
|
corrinoid ABC transporter substrate-binding protein; Reviewed
Pssm-ID: 236552 [Multi-domain] Cd Length: 359 Bit Score: 81.49 E-value: 2.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671141 9 TAILSVFFLLIGCNAKGNDKASATKTEKGKEK------IEITDLSGRKVTFDKTPESFATLSMGDMDIIHALGGK--IIG 80
Cdd:PRK09534 6 FRSLVIVALAVTMTAAGGALAPAPAAQHADADracsfpVTETDATGTEITLDERPERVVTLNPSAAQTMWELGARdrVVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671141 81 RPDTKLTLPEELKKAQVIGNA-HQPNFEQIASLKPDVLVANNGFQ-KNVPTVEGQGTKVV-ISTANSVQDIQKNIEIYGA 157
Cdd:PRK09534 86 VTQYASYLDGAEERTNVSGGQpFGVNVEAVVGLDPDLVLAPNAVAgDTVTRLREAGITVFhFPAATSIEDVAEKTATIGR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671141 158 VMKKEDKAKELNQKMNDQMKKYEKKS---DVKALLVYGAPGTYLAAlPTSLSGDILEKTGGKNIAAGfpemKEYPQYAQL 234
Cdd:PRK09534 166 LTGNCEAAAETNAEMRDRVDAVEDRTadvDDRPRVLYPLGDGYTAG-GNTFIGALIEAAGGHNVAAD----ATTDGYPQL 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446671141 235 SVERIIEANPDVIYLITHGDPnsvkkafegeMMKNEAWKNLDAVKQNRVVILPPDLFgSNPGTKVTEAMDFM 306
Cdd:PRK09534 241 SEEVIVQQDPDVIVVATASAL----------VAETEPYASTTAGETGNVVTVNVNHI-NQPAPRIVESMATM 301
|
|
| TroA-like |
cd00636 |
Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function ... |
61-182 |
4.14e-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: 74.13 E-value: 4.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671141 61 ATLSMGDMDIIHALGG--KIIGRPDTKLT---LPEELKKAQVIGNAHQPNFEQIASLKPDVLVANNGFQ-KNVPTVEGQG 134
Cdd:cd00636 4 VALDPGATELLLALGGddKPVGVADPSGYppeAKALLEKVPDVGHGYEPNLEKIAALKPDLIIANGSGLeAWLDKLSKIA 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 446671141 135 TKVVI---STANSVQDIQKNIEIYGAVMKKEDKAKELNQKMNDQMKKYEKK 182
Cdd:cd00636 84 IPVVVvdeASELSLENIKESIRLIGKALGKEENAEELIAELDARLAELRAK 134
|
|
| fecB |
PRK11411 |
iron-dicitrate transporter substrate-binding subunit; Provisional |
1-303 |
4.70e-10 |
|
iron-dicitrate transporter substrate-binding subunit; Provisional
Pssm-ID: 183123 [Multi-domain] Cd Length: 303 Bit Score: 59.69 E-value: 4.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671141 1 MKKSITLFTAILSVFFLLIGCNAkgndkasatktekgkekIEITDLSGrKVTFDKTPESFATLSMGDMDIIHALGGKIIG 80
Cdd:PRK11411 1 MLAFIRLLFAGLLLLSGSSHAFA-----------------VTVQDEQG-TFTLEKTPQRIVVLELSFVDALAAVGVSPVG 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671141 81 RPD---TKLTLPE---ELKKAQVIGNAHQPNFEQIASLKPDVLVAN--------NGFQKNVPTVegqgtkVVISTANSVQ 146
Cdd:PRK11411 63 VADdndAKRILPEvraHLKPWQSVGTRSQPSLEAIAALKPDLIIADssrhagvyIALQKIAPTL------LLKSRNETYQ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671141 147 DIQKNIEIYGAVMKKEDKAKELNQKMNDQMKKYEKKSDVKALLVYG----------APGTYLAALPTSLSgdilektggk 216
Cdd:PRK11411 137 ENLQSAAIIGEVLGKKREMQARIEQHKERMAQFASQLPKGTRVAFGtsreqqfnlhSPESYTGSVLAALG---------- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671141 217 nIAAGFPEMKEYPqYAQLSVERIIEANPDVIYLITHGDPNSVKKafegeMMKNEAWKNLDAVKQNRVVILPPDLFGSNPG 296
Cdd:PRK11411 207 -LNVPKAPMNGAA-MPSISLEQLLALNPDWLLVAHYRQESIVKR-----WQQDPLWQMLTAAKKQQVASVDSNTWARMRG 279
|
....*..
gi 446671141 297 TKVTEAM 303
Cdd:PRK11411 280 IFAAERI 286
|
|
| PRK03379 |
PRK03379 |
vitamin B12-transporter protein BtuF; Provisional |
89-272 |
1.66e-07 |
|
vitamin B12-transporter protein BtuF; Provisional
Pssm-ID: 179575 [Multi-domain] Cd Length: 260 Bit Score: 51.61 E-value: 1.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671141 89 PEELKKAQVIGNAHQPNFEQIASLKPDVLVANNG--FQKNVPTVEGQGTKVVISTANSVQDIQKNIEIYGAVMKKEDKAK 166
Cdd:PRK03379 48 PPQAKKIEQVATWQGMNLERIVALKPDLVLAWRGgnAERQVDQLASLGIKVMWVDATSIEQIANALRQLAPWSPQPEKAE 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671141 167 ----ELNQKMNDQMKKYEKKSDVKALLVYGAPGTYLAAlPTSLSGDILEKTGGKNIAAGFPemkeYPqYAQLSVERIIEA 242
Cdd:PRK03379 128 qaaqSLLQQYAALKAQYADKPKKRVFLQFGTNPLFTSG-KHSIQSQVLSLCGGENIFADSR----VP-WPQVSREQVLAR 201
|
170 180 190
....*....|....*....|....*....|....*...
gi 446671141 243 NPDVIylITHGDPNSVKK--AFEGEMMK------NEAW 272
Cdd:PRK03379 202 KPQAI--VITGGPDQIPKikQFWGPQLKipviplNSDW 237
|
|
| TroA_d |
cd01141 |
Periplasmic binding protein TroA_d. These proteins are predicted to function as initial ... |
51-219 |
5.19e-06 |
|
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: 46.26 E-value: 5.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671141 51 VTFDKTPESFATLSMGDMDIIHALGG--KIIGRPDTKLTL--PEELKKAQV-IGNAHQPNFEQIASLKPDVLVANNGFQK 125
Cdd:cd01141 2 KTIKVPPKRIVVLSPTHVDLLLALDKadKIVGVSASAYDLntPAVKERIDIqVGPTGSLNVELIVALKPDLVILYGGFQA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446671141 126 N--VPTVEGQGTKVVI-----STANSVQDIQKNIEIYGAvmKKEDKAKELnqkMNDQMKKYEkksDVKALLVYGAPGTYL 198
Cdd:cd01141 82 QtiLDKLEQLGIPVLYvneypSPLGRAEWIKFAAAFYGV--GKEDKADEA---FAQIAGRYR---DLAKKVSNLNKPTVA 153
|
170 180
....*....|....*....|.
gi 446671141 199 AALPTslSGDILEKTGGKNIA 219
Cdd:cd01141 154 IGKPV--KGLWYMPGGNSYVA 172
|
|
| |
