|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10576 |
PRK10576 |
Fe(3+)-hydroxamate ABC transporter substrate-binding protein FhuD; |
8-301 |
0e+00 |
|
Fe(3+)-hydroxamate ABC transporter substrate-binding protein FhuD;
Pssm-ID: 236719 Cd Length: 292 Bit Score: 513.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359192518 8 SHDPLRRRLLMALALSPLLGSLPGRAAdAPPDIARVAALEWLPIELLLALGVTPLAVADVHNYNLWVAEPKLPATVVDVG 87
Cdd:PRK10576 1 LPDISRRRLLTAMALSPLLWQMNTAAA-AAIDPNRIVALEWLPVELLLALGVTPYGVADTHNYRLWVSEPALPDSVIDVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359192518 88 QRTEPNLELLQQLQPSLVLLSQGYGPTPQKIQPIAPTMSFGFNDGsGKPLTVARQSLLALGQRLGIESRAVQHLAQFDRF 167
Cdd:PRK10576 80 LRTEPNLELLTQMKPSLILWSAGYGPSPEKLARIAPGRGFAFSDG-KKPLAVARKSLVELAQRLNLEAAAETHLAQFDDF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359192518 168 MQDARQRLQSYTRQPLLLFSLIDTRHALIIGQKSLFQEAMDQLGIRNAWQEETNFWGTAVVGIERLATVRNARVIYLDHG 247
Cdd:PRK10576 159 IASAKPRLAGRGQRPLLLTSLIDPRHALVFGPNSLFQEVLDELGIENAWQGETNFWGSTVVGIERLAAYKDADVICFDHG 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1359192518 248 NQAMMDKVSATPLWQSLPFVRQNQLRQVPAVWFYGATLSTMRFCRLLAQAQESA 301
Cdd:PRK10576 239 NSKDMQQLMATPLWQAMPFVRAGRFQRVPAVWFYGATLSAMHFVRVLDNALGGK 292
|
|
| FhuD |
cd01146 |
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial ... |
42-290 |
3.16e-57 |
|
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: 184.80 E-value: 3.16e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359192518 42 RVAALEWLPIELLLALGVTPLAVADVHNYNLWVAEPKLPA-TVVDVGQRTEPNLELLQQLQPSLVLLSQGYGPTP-QKIQ 119
Cdd:cd01146 5 RIVALDWGALETLLALGVKPVGVADTAGYKPWIPEPALPLeGVVDVGTRGQPNLEAIAALKPDLILGSASRHDEIyDQLS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359192518 120 PIAPTMSFGFNDGSGKpltvARQSLLALGQRLGIESRAVQHLAQFDRFMQDARQRLQSYTRQPLLLFSLIDTRHALIIGQ 199
Cdd:cd01146 85 QIAPTVLLDSSPWLAE----WKENLRLIAKALGKEEEAEKLLAEYDQRLAELRQKLPDKGPKPVSVVRFSDAGSIRLYGP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359192518 200 KSLFQEAMDQLGIRNAW-QEETNFWGTAVVGIERLATVrNARVIYLDH-GNQAMMDKVSATPLWQSLPFVRQNQLRQVPA 277
Cdd:cd01146 161 NSFAGSVLEDLGLQNPWaQETTNDSGFATISLERLAKA-DADVLFVFTyEDEELAQALQANPLWQNLPAVKNGRVYVVDD 239
|
250
....*....|....
gi 1359192518 278 V-WFYGATLSTMRF 290
Cdd:cd01146 240 VwWFFGGGLSAARL 253
|
|
| Peripla_BP_2 |
pfam01497 |
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ... |
44-277 |
1.20e-43 |
|
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: 149.06 E-value: 1.20e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359192518 44 AALEWLPIELLLALGVTPLAVADVHNYNLWVAEPKLPAtVVDVGQRTEPNLELLQQLQPSLVLLSQGYGP--TPQKIQPI 121
Cdd:pfam01497 1 AALSPAYTEILYALGATDSIVGVDAYTRDPLKADAVAA-IVKVGAYGEINVERLAALKPDLVILSTGYLTdeAEELLSLI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359192518 122 APTMSFGFNDGSGKPLTvarqSLLALGQRLGIESRAVQHLAQFDRFMQDARQRLQSYTRQPLLLFSLIDTRHALIIGQKS 201
Cdd:pfam01497 80 IPTVIFESSSTGESLKE----QIKQLGELLGLEDEAEELVAEIDSALAAAKKAVPSLTRKPVLVFGGADGGGYVVAGSNT 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1359192518 202 LFQEAMDQLGIRNaWQEETNFWGTAVVGIERLATvRNARVIYL---DHGNQAMMDKVSATPLWQSLPFVRQNQLRQVPA 277
Cdd:pfam01497 156 YIGDLLRILGIEN-IAAELSGSEYAPISFEAILS-SNPDVIIVsgrDSFTKTGPEFVAANPLWAGLPAVKNGRVYTLPS 232
|
|
| FepB |
COG0614 |
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ... |
42-297 |
1.93e-37 |
|
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 440379 [Multi-domain] Cd Length: 264 Bit Score: 133.58 E-value: 1.93e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359192518 42 RVAALEWLPIELLLALGVTPLAVAdVHNYNLWVAEPKLPATVVDVGQRTEPNLELLQQLQPSLVLLSQGYGP--TPQKIQ 119
Cdd:COG0614 2 RIVSLSPSATELLLALGAGDRLVG-VSDWGYCDYPELELKDLPVVGGTGEPNLEAILALKPDLVLASSSGNDeeDYEQLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359192518 120 PI-APTMSFGFNDgsgkpLTVARQSLLALGQRLGIESRAVQHLAQFDRFMQDARQRLQSYTRQPLLLFSLIDTRHALIIG 198
Cdd:COG0614 81 KIgIPVVVLDPRS-----LEDLYESIRLLGELLGREERAEALIAEYEARLAAVRARLAGAEERPTVLYEIWSGDPLYTAG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359192518 199 QKSLFQEAMDQLGIRNAWQEETNFWGTavVGIERLAtVRNARVIYLDHGN------QAMMDKVSATPLWQSLPFVRQNQL 272
Cdd:COG0614 156 GGSFIGELLELAGGRNVAADLGGGYPE--VSLEQVL-ALDPDVIILSGGGydaetaEEALEALLADPGWQSLPAVKNGRV 232
|
250 260
....*....|....*....|....*
gi 1359192518 273 RQVPAVWFYGATLSTMRFCRLLAQA 297
Cdd:COG0614 233 YVVPGDLLSRPGPRLLLALEDLAKA 257
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10576 |
PRK10576 |
Fe(3+)-hydroxamate ABC transporter substrate-binding protein FhuD; |
8-301 |
0e+00 |
|
Fe(3+)-hydroxamate ABC transporter substrate-binding protein FhuD;
Pssm-ID: 236719 Cd Length: 292 Bit Score: 513.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359192518 8 SHDPLRRRLLMALALSPLLGSLPGRAAdAPPDIARVAALEWLPIELLLALGVTPLAVADVHNYNLWVAEPKLPATVVDVG 87
Cdd:PRK10576 1 LPDISRRRLLTAMALSPLLWQMNTAAA-AAIDPNRIVALEWLPVELLLALGVTPYGVADTHNYRLWVSEPALPDSVIDVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359192518 88 QRTEPNLELLQQLQPSLVLLSQGYGPTPQKIQPIAPTMSFGFNDGsGKPLTVARQSLLALGQRLGIESRAVQHLAQFDRF 167
Cdd:PRK10576 80 LRTEPNLELLTQMKPSLILWSAGYGPSPEKLARIAPGRGFAFSDG-KKPLAVARKSLVELAQRLNLEAAAETHLAQFDDF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359192518 168 MQDARQRLQSYTRQPLLLFSLIDTRHALIIGQKSLFQEAMDQLGIRNAWQEETNFWGTAVVGIERLATVRNARVIYLDHG 247
Cdd:PRK10576 159 IASAKPRLAGRGQRPLLLTSLIDPRHALVFGPNSLFQEVLDELGIENAWQGETNFWGSTVVGIERLAAYKDADVICFDHG 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1359192518 248 NQAMMDKVSATPLWQSLPFVRQNQLRQVPAVWFYGATLSTMRFCRLLAQAQESA 301
Cdd:PRK10576 239 NSKDMQQLMATPLWQAMPFVRAGRFQRVPAVWFYGATLSAMHFVRVLDNALGGK 292
|
|
| FhuD |
cd01146 |
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial ... |
42-290 |
3.16e-57 |
|
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: 184.80 E-value: 3.16e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359192518 42 RVAALEWLPIELLLALGVTPLAVADVHNYNLWVAEPKLPA-TVVDVGQRTEPNLELLQQLQPSLVLLSQGYGPTP-QKIQ 119
Cdd:cd01146 5 RIVALDWGALETLLALGVKPVGVADTAGYKPWIPEPALPLeGVVDVGTRGQPNLEAIAALKPDLILGSASRHDEIyDQLS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359192518 120 PIAPTMSFGFNDGSGKpltvARQSLLALGQRLGIESRAVQHLAQFDRFMQDARQRLQSYTRQPLLLFSLIDTRHALIIGQ 199
Cdd:cd01146 85 QIAPTVLLDSSPWLAE----WKENLRLIAKALGKEEEAEKLLAEYDQRLAELRQKLPDKGPKPVSVVRFSDAGSIRLYGP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359192518 200 KSLFQEAMDQLGIRNAW-QEETNFWGTAVVGIERLATVrNARVIYLDH-GNQAMMDKVSATPLWQSLPFVRQNQLRQVPA 277
Cdd:cd01146 161 NSFAGSVLEDLGLQNPWaQETTNDSGFATISLERLAKA-DADVLFVFTyEDEELAQALQANPLWQNLPAVKNGRVYVVDD 239
|
250
....*....|....
gi 1359192518 278 V-WFYGATLSTMRF 290
Cdd:cd01146 240 VwWFFGGGLSAARL 253
|
|
| Peripla_BP_2 |
pfam01497 |
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ... |
44-277 |
1.20e-43 |
|
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: 149.06 E-value: 1.20e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359192518 44 AALEWLPIELLLALGVTPLAVADVHNYNLWVAEPKLPAtVVDVGQRTEPNLELLQQLQPSLVLLSQGYGP--TPQKIQPI 121
Cdd:pfam01497 1 AALSPAYTEILYALGATDSIVGVDAYTRDPLKADAVAA-IVKVGAYGEINVERLAALKPDLVILSTGYLTdeAEELLSLI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359192518 122 APTMSFGFNDGSGKPLTvarqSLLALGQRLGIESRAVQHLAQFDRFMQDARQRLQSYTRQPLLLFSLIDTRHALIIGQKS 201
Cdd:pfam01497 80 IPTVIFESSSTGESLKE----QIKQLGELLGLEDEAEELVAEIDSALAAAKKAVPSLTRKPVLVFGGADGGGYVVAGSNT 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1359192518 202 LFQEAMDQLGIRNaWQEETNFWGTAVVGIERLATvRNARVIYL---DHGNQAMMDKVSATPLWQSLPFVRQNQLRQVPA 277
Cdd:pfam01497 156 YIGDLLRILGIEN-IAAELSGSEYAPISFEAILS-SNPDVIIVsgrDSFTKTGPEFVAANPLWAGLPAVKNGRVYTLPS 232
|
|
| FepB |
COG0614 |
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ... |
42-297 |
1.93e-37 |
|
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 440379 [Multi-domain] Cd Length: 264 Bit Score: 133.58 E-value: 1.93e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359192518 42 RVAALEWLPIELLLALGVTPLAVAdVHNYNLWVAEPKLPATVVDVGQRTEPNLELLQQLQPSLVLLSQGYGP--TPQKIQ 119
Cdd:COG0614 2 RIVSLSPSATELLLALGAGDRLVG-VSDWGYCDYPELELKDLPVVGGTGEPNLEAILALKPDLVLASSSGNDeeDYEQLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359192518 120 PI-APTMSFGFNDgsgkpLTVARQSLLALGQRLGIESRAVQHLAQFDRFMQDARQRLQSYTRQPLLLFSLIDTRHALIIG 198
Cdd:COG0614 81 KIgIPVVVLDPRS-----LEDLYESIRLLGELLGREERAEALIAEYEARLAAVRARLAGAEERPTVLYEIWSGDPLYTAG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359192518 199 QKSLFQEAMDQLGIRNAWQEETNFWGTavVGIERLAtVRNARVIYLDHGN------QAMMDKVSATPLWQSLPFVRQNQL 272
Cdd:COG0614 156 GGSFIGELLELAGGRNVAADLGGGYPE--VSLEQVL-ALDPDVIILSGGGydaetaEEALEALLADPGWQSLPAVKNGRV 232
|
250 260
....*....|....*....|....*
gi 1359192518 273 RQVPAVWFYGATLSTMRFCRLLAQA 297
Cdd:COG0614 233 YVVPGDLLSRPGPRLLLALEDLAKA 257
|
|
| FecB |
COG4594 |
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and ... |
42-282 |
1.09e-36 |
|
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443650 [Multi-domain] Cd Length: 316 Bit Score: 133.12 E-value: 1.09e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359192518 42 RVAALEWLPIELLLALGVTPLAVADVHNYNLWVAEP-KLPATVVDVGQRTEPNLELLQQLQPSLVLLSQGYGptpQKIQP 120
Cdd:COG4594 54 RVVVLEWSFADALLALGVTPVGIADDNDYDRWVPYLrDLIKGVTSVGTRSQPNLEAIAALKPDLIIADKSRH---EAIYD 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359192518 121 ----IAPTMSFGFNDGSGKPLTvarQSLLALGQRLGIESRAVQHLAQFDRFMQDARQRLQSYTRQPLLLFSLIDTRHALI 196
Cdd:COG4594 131 qlskIAPTVLFKSRNGDYQENL---ESFKTIAKALGKEEEAEAVLADHDQRIAEAKAKLAAADKGKKVAVGQFRADGLRL 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359192518 197 IGQKSLFQEAMDQLGIRNAW-QEETNFWGTAVVGIERLATVrNARVIYLDH-GNQAMMDKVSATPLWQSLPFVRQNQLRQ 274
Cdd:COG4594 208 YTPNSFAGSVLAALGFENPPkQSKDNGYGYSEVSLEQLPAL-DPDVLFIATyDDPSILKEWKNNPLWKNLKAVKNGRVYE 286
|
....*....
gi 1359192518 275 VP-AVWFYG 282
Cdd:COG4594 287 VDgDLWTRG 295
|
|
| TroA-like |
cd00636 |
Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function ... |
42-186 |
4.97e-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: 4.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359192518 42 RVAALEWLPIELLLALGVTPLAVADVHNYNLWVAEPKLPATVVDVGQRTEPNLELLQQLQPSLVLLSQGYGP-TPQKIQP 120
Cdd:cd00636 2 RVVALDPGATELLLALGGDDKPVGVADPSGYPPEAKALLEKVPDVGHGYEPNLEKIAALKPDLIIANGSGLEaWLDKLSK 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1359192518 121 IA-PTMSfgFNDGSGKPLTVARQSLLALGQRLGIESRAVQHLAQFDRFMQDARQRLQSYTRQPLLLF 186
Cdd:cd00636 82 IAiPVVV--VDEASELSLENIKESIRLIGKALGKEENAEELIAELDARLAELRAKLAKIPKKKVSLV 146
|
|
| TroA_e |
cd01142 |
Periplasmic binding protein TroA_e. These proteins are predicted to function as initial ... |
31-281 |
3.20e-11 |
|
Periplasmic binding protein TroA_e. These proteins are predicted to function as initial receptors in the ABC metal ion uptake in eubacteria and archaea. They belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind their ligands in the cleft between these domains.
Pssm-ID: 238562 [Multi-domain] Cd Length: 289 Bit Score: 62.76 E-value: 3.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359192518 31 GRAADAPPDIARVAALEWLPIELLLALGVTPLAVADVHnynLWVAEPKLP------ATVVDVGQRTEPNLELLQQLQPSL 104
Cdd:cd01142 15 GRKVTIPDEVKRIAALWGAGNAVVAALGGGKLIVATTS---TVQQEPWLYrlapslENVATGGTGNDVNIEELLALKPDV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359192518 105 VLLSQGYGPTP-QKIQPIAPTMSFGFndgsGKPLTVaRQSLLALGQRLGIESRAVQHLAQFDRFMQ---------DARQR 174
Cdd:cd01142 92 VIVWSTDGKEAgKAVLRLLNALSLRD----AELEEV-KLTIALLGELLGRQEKAEALVAYFDDNLAyvaartkklPDSER 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359192518 175 LQSYTRQPlllfSLIDTRhaliiGQKSLFQEAMDQLGIRNAwQEETNFWGTAVVGIERLATVrNARVIYLdhGNQAMMDK 254
Cdd:cd01142 167 PRVYYAGP----DPLTTD-----GTGSITNSWIDLAGGINV-ASEATKKGSGEVSLEQLLKW-NPDVIIV--GNADTKAA 233
|
250 260
....*....|....*....|....*..
gi 1359192518 255 VSATPLWQSLPFVRQNQLRQVPAVWFY 281
Cdd:cd01142 234 ILADPRWQNLRAVKNGRVYVNPEGAFW 260
|
|
| FatB |
cd01140 |
Siderophore binding protein FatB. These proteins have been shown to function as ABC-type ... |
41-281 |
1.02e-10 |
|
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: 61.12 E-value: 1.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359192518 41 ARVAALEWLPIELLLALGVTPLAVADVHN--YNLwvaEPKLPATVVDVGQRTEPNLELLQQLQPSLVLLSQGYGPTPQKI 118
Cdd:cd01140 13 EKVVVFDVGALDTLDALGVKVVGVPKSSTlpEYL---KKYKDDKYANVGTLFEPDLEAIAALKPDLIIIGGRLAEKYDEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359192518 119 QPIAPTMSFGFNdgSGKPLTVARQSLLALGQRLGIESRAVQHLAQFDRFMQDARQRLQSYTRqPLLLfsLIDTRHALIIG 198
Cdd:cd01140 90 KKIAPTIDLGAD--LKNYLESVKQNIETLGKIFGKEEEAKELVAEIDASIAEAKSAAKGKKK-ALVV--LVNGGKLSAFG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359192518 199 QKSLFQEAMDQLGIRNAWQEETNFWGTAVVGIERLATVrNARVIY-LDH----GNQAMMDK-VSATPLWQSLPFVRQNQL 272
Cdd:cd01140 165 PGSRFGWLHDLLGFEPADENIKASSHGQPVSFEYILEA-NPDWLFvIDRgaaiGAEGSSAKeVLDNDLVKNTTAWKNGKV 243
|
....*....
gi 1359192518 273 RQVPAVWFY 281
Cdd:cd01140 244 IYLDPDLWY 252
|
|
| CeuA |
COG4607 |
ABC-type enterochelin transport system, periplasmic component [Inorganic ion transport and ... |
42-173 |
3.14e-10 |
|
ABC-type enterochelin transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443657 [Multi-domain] Cd Length: 310 Bit Score: 59.81 E-value: 3.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359192518 42 RVAALEWLPIELLLALGVTPLAVADVHnynlwvaepkLPAT--------VVDVGQRTEPNLELLQQLQPSLVLLSQGYGP 113
Cdd:COG4607 53 RVVVFDNGALDTLDALGVEVAGVPKGL----------LPDYlskyaddkYANVGTLFEPDLEAIAALKPDLIIIGGRSAK 122
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359192518 114 TPQKIQPIAPTMSFGFNDgsGKPLTVARQSLLALGQRLGIESRAVQHLAQFDRFMQDARQ 173
Cdd:COG4607 123 KYDELSKIAPTIDLTVDG--EDYLESLKRNTETLGEIFGKEDEAEELVADLDAKIAALKA 180
|
|
| FeuA |
cd01138 |
Periplasmic binding protein FeuA. These proteins have predicted to function as initial ... |
36-281 |
2.68e-09 |
|
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: 56.57 E-value: 2.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359192518 36 APPDiaRVAALEwLPIELLLALGVTPLAVADVHNYNlwvaePKLPATV--VDVGQRTEPNLELLQQLQPSLVLLSQGYGP 113
Cdd:cd01138 7 AKPK--RIVALS-GETEGLALLGIKPVGAASIGGKN-----PYYKKKTlaKVVGIVDEPNLEKVLELKPDLIIVSSKQEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359192518 114 TPQKIQPIAPTMSFGFNdgsgkpLTVARQSLLALGQRLGIESRAVQHLAQFDRFMQDARQRLQS-----------YTRQP 182
Cdd:cd01138 79 NYEKLSKIAPTVPVSYN------SSDWEEQLKEIGKLLNKEDEAEKWLADYKQKAKEAKEKIKKklgndksvavlRGRKQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359192518 183 LLLFSLIDTRhaliiGQKSLFqeAMDQLGIRNAWQEETNFWGTAVVGIERLATVRNARVIYLDHGNQAMMDKVSATPLWQ 262
Cdd:cd01138 153 IYVFGEDGRG-----GGPILY--ADLGLKAPEKVKEIEDKPGYAAISLEVLPEFDADYIFLLFFTGPEAKADFESLPIWK 225
|
250
....*....|....*....
gi 1359192518 263 SLPFVRQNQLRQVPAVWFY 281
Cdd:cd01138 226 NLPAVKNNHVYIVDAWVFY 244
|
|
| fecB |
PRK11411 |
iron-dicitrate transporter substrate-binding subunit; Provisional |
12-279 |
3.69e-07 |
|
iron-dicitrate transporter substrate-binding subunit; Provisional
Pssm-ID: 183123 [Multi-domain] Cd Length: 303 Bit Score: 50.83 E-value: 3.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359192518 12 LRRRLLMALALSPLLGSLPGRAA-----------DAPPdiARVAALEWLPIELLLALGVTPLAVADVHNynlwvAEPKLP 80
Cdd:PRK11411 2 LAFIRLLFAGLLLLSGSSHAFAVtvqdeqgtftlEKTP--QRIVVLELSFVDALAAVGVSPVGVADDND-----AKRILP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359192518 81 AtVVD-------VGQRTEPNLELLQQLQPSLVLL-SQGYGPTPQKIQPIAPTMSFgfnDGSGKPLTVARQSLLALGQRLG 152
Cdd:PRK11411 75 E-VRAhlkpwqsVGTRSQPSLEAIAALKPDLIIAdSSRHAGVYIALQKIAPTLLL---KSRNETYQENLQSAAIIGEVLG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359192518 153 IESRAVQHLAQFDRFMQDARQRLQSYTRqplLLFSLIDTRHALIIGQKSLFQEAMDQLGIRNAWQEETNfWGTAVVGIER 232
Cdd:PRK11411 151 KKREMQARIEQHKERMAQFASQLPKGTR---VAFGTSREQQFNLHSPESYTGSVLAALGLNVPKAPMNG-AAMPSISLEQ 226
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1359192518 233 LATVRNARVIYLDHGNQAMMDKVSATPLWQSLPFVRQNQLRQV-PAVW 279
Cdd:PRK11411 227 LLALNPDWLLVAHYRQESIVKRWQQDPLWQMLTAAKKQQVASVdSNTW 274
|
|
| TroA_a |
cd01148 |
Metal binding protein TroA_a. These proteins are predicted to function as initial receptors ... |
35-270 |
1.36e-05 |
|
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: 45.79 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359192518 35 DAPPDiaRVAALEWLPIELLLALGVTPLAVADVHNYNLWVAEPKLPATVVDVGQRTEPNLELLQQLQPSLVLLSQGYG-- 112
Cdd:cd01148 15 DKAPQ--RVVSNDQNTTEMMLALGLQDRMVGTAGIDNKDLPELKAKYDKVPELAKKYPSKETVLAARPDLVFGGWSYGfd 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359192518 113 ----PTPQKIQPI-APTM---SFGFNDGSGKPLTVARQSLLALGQRLGIESRAVQHLAQFDRFMQDARQRLQSYTRQPLL 184
Cdd:cd01148 93 kgglGTPDSLAELgIKTYilpESCGQRRGEATLDDVYNDIRNLGKIFDVEDRADKLVADLKARLAEISAKVKGDGKKVAV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359192518 185 LFSLIDTRHALIIGQKSLFQEAMDQLGIRNAWQEETNFWGTavVGIERLAtVRNARVI-YLDHGNQ-AMMDKVSA---TP 259
Cdd:cd01148 173 FVYDSGEDKPFTSGRGGIPNAIITAAGGRNVFADVDESWTT--VSWETVI-ARNPDVIvIIDYGDQnAAEQKIKFlkeNP 249
|
250
....*....|.
gi 1359192518 260 LWQSLPFVRQN 270
Cdd:cd01148 250 ALKNVPAVKNN 260
|
|
| PRK10957 |
PRK10957 |
iron-enterobactin transporter periplasmic binding protein; Provisional |
90-271 |
2.76e-05 |
|
iron-enterobactin transporter periplasmic binding protein; Provisional
Pssm-ID: 236806 [Multi-domain] Cd Length: 317 Bit Score: 44.96 E-value: 2.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359192518 90 TEPNLELLQQLQPSLVLLSQGYGPTPQK----IQPIAPTMSFGFNDGSGkpltvarQSLLA-LGQRLGIESRAVQHLAQF 164
Cdd:PRK10957 102 GEPDAEAVAAQMPDLIVISATGGDSALAlydqLSAIAPTLVIDYDDKSW-------QELATqLGEATGLEKQAAAVIAQF 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359192518 165 DRFMQDARQRLQsYTRQPLLLFSLIDTRHALIIGQKSLFQ-EAMDQLGIR-----NAWQEETNFWGT---AVVGIERLAT 235
Cdd:PRK10957 175 DAQLAEVKAKIT-LPPQPVSALVYNGAGHSANLWTPESAQgQLLEQLGFTlaelpAGLQASTSQGKRhdiIQLGGENLAA 253
|
170 180 190
....*....|....*....|....*....|....*.
gi 1359192518 236 VRNARVIYLDHGNQAMMDKVSATPLWQSLPFVRQNQ 271
Cdd:PRK10957 254 GLNGETLFLFAGDDKDADAFLADPLLANLPAVQNKQ 289
|
|
| HemV-2 |
cd01147 |
Metal binding protein HemV-2. These proteins are predicted to function as initial receptors ... |
37-280 |
3.75e-05 |
|
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: 44.25 E-value: 3.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359192518 37 PPDIARVAALEWLPIELLLALGVTPLAVA------DVHNYNLWVAEP---KLPaTVVDVGQRTEPNLELLQQLQPSLVLL 107
Cdd:cd01147 2 PKPVERVVAAGPGALRLLYALAAPDKIVGvddaekSDEGRPYFLASPelkDLP-VIGRGGRGNTPNYEKIAALKPDVVID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359192518 108 SQGYGPT--PQKIQPIAptmsfgfndgsGKPLTVA---------RQSLLALGQRLGIESRAVQHLAQFDRFMQDARQRLQ 176
Cdd:cd01147 81 VGSDDPTsiADDLQKKT-----------GIPVVVLdggdsledtPEQIRLLGKVLGKEERAEELISFIESILADVEERTK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359192518 177 --SYTRQPLLLFSLIDTR--HALIIGQKSLfQEAMDQLGIRNAWQEEtNFWGTAVVGIERLaTVRNARVIYLDHGN--QA 250
Cdd:cd01147 150 diPDEEKPTVYFGRIGTKgaAGLESGLAGS-IEVFELAGGINVADGL-GGGGLKEVSPEQI-LLWNPDVIFLDTGSfyLS 226
|
250 260 270
....*....|....*....|....*....|
gi 1359192518 251 MMDKVSATPLWQSLPFVRQNQLRQVPAVWF 280
Cdd:cd01147 227 LEGYAKNRPFWQSLKAVKNGRVYLLPALPF 256
|
|
| ChuT |
COG4558 |
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism] ... |
14-215 |
6.38e-05 |
|
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism];
Pssm-ID: 443619 [Multi-domain] Cd Length: 285 Bit Score: 43.64 E-value: 6.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359192518 14 RRLLMALALSpLLGSLPGRAADAPPDIARVAALEWLPIELLLALGVTPLAVA-DVhnYNLWVAE-PKLPatvvDVGQRTE 91
Cdd:COG4558 2 KRLALALLLL-ALAALAAGASVAAAAAERIVSLGGSVTEIVYALGAGDRLVGvDT--TSTYPAAaKALP----DVGYMRQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359192518 92 PNLELLQQLQPSLVLLSQGYGPtPQKIQPIAptmsfgfndGSGKPLTV--ARQSL-------LALGQRLGIESRAVQHLA 162
Cdd:COG4558 75 LSAEGILSLKPTLVLASEGAGP-PEVLDQLR---------AAGVPVVVvpAAPSLegvlakiRAVAAALGVPEAGEALAA 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1359192518 163 QFDRFMQDARQRLQSYTRQPLLLFSLI-DTRHALIIGQKSLFQEAMDQLGIRNA 215
Cdd:COG4558 145 RLEADLAALAARVAAIGKPPRVLFLLSrGGGRPMVAGRGTAADALIRLAGGVNA 198
|
|
| BtuF |
cd01144 |
Cobalamin binding protein BtuF. These proteins have been shown to function as initial ... |
52-281 |
1.20e-04 |
|
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: 42.67 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359192518 52 ELLLALGVTPLAVADVHnynlWVAEPKLPATVVDVGQRTEPNLELLQQLQPSLVLLSQGYGPTPQkiqpIAPTMSFGFND 131
Cdd:cd01144 12 ELLYALGLGDQLVGVTD----YCDYPPEAKKLPRVGGFYQLDLERVLALKPDLVIAWDDCNVCAV----VDQLRAAGIPV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1359192518 132 GSGKPLTVAR--QSLLALGQRLGIESRAVQHLAQFDRFMQDARQrlQSYTRQPLLLFSLIDTRhALIIGQKSLFQEAMDQ 209
Cdd:cd01144 84 LVSEPQTLDDilADIRRLGTLAGRPARAEELAEALRRRLAALRK--QYASKPPPRVFYQEWID-PLMTAGGDWVPELIAL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1359192518 210 LGIRNAWQEETNFWGTavVGIERlatVRNAR---VIYLDHGNQAMMDKVSATPLWQSLPFVRQNQLRQVPAVWFY 281
Cdd:cd01144 161 AGGVNVFADAGERSPQ--VSWED---VLAANpdvIVLSPCGFGFTPAILRKEPAWQALPAVRNGRVYAVDGNWYF 230
|
|
| TroA_d |
cd01141 |
Periplasmic binding protein TroA_d. These proteins are predicted to function as initial ... |
42-113 |
8.55e-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: 8.55e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1359192518 42 RVAALEWLPIELLLALGVTPlAVADVHNYNLWVAEPKLPATVV-DVGQRTEPNLELLQQLQPSLVLLSQGYGP 113
Cdd:cd01141 10 RIVVLSPTHVDLLLALDKAD-KIVGVSASAYDLNTPAVKERIDiQVGPTGSLNVELIVALKPDLVILYGGFQA 81
|
|
| |
