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Conserved domains on  [gi|1195228150|gb|OUG69649|]
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Iron(3+)-hydroxamate-binding protein FhuD [Klebsiella pneumoniae]

Protein Classification

Fe(3+)-hydroxamate ABC transporter substrate-binding protein FhuD( domain architecture ID 10793420)

Fe(3+)-hydroxamate ABC transporter substrate-binding protein FhuD functions as the initial receptor of the ABC transporter complex FhuCDB that is involved in iron(3+)-hydroxamate import

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK10576 PRK10576
Fe(3+)-hydroxamate ABC transporter substrate-binding protein FhuD;
4-293 0e+00

Fe(3+)-hydroxamate ABC transporter substrate-binding protein FhuD;


:

Pssm-ID: 236719  Cd Length: 292  Bit Score: 558.47  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195228150   4 PTLITRRRLLIAMALSPLLWQMRGAQAADVDPQRVVALEWLPAELLLALGVTPYGVADIPNYRLWVNEPALPDSVIDVGL 83
Cdd:PRK10576    1 LPDISRRRLLTAMALSPLLWQMNTAAAAAIDPNRIVALEWLPVELLLALGVTPYGVADTHNYRLWVSEPALPDSVIDVGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195228150  84 RTEPNLELLTQMKPSFIVWSAGYGPSPEKLARIAPGRGFTFSDGKRPLAMAQRSLLEMADLLGKTQQAKRHLAEFDALME 163
Cdd:PRK10576   81 RTEPNLELLTQMKPSLILWSAGYGPSPEKLARIAPGRGFAFSDGKKPLAVARKSLVELAQRLNLEAAAETHLAQFDDFIA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195228150 164 SLRPRFAGRGDRPLLMISLLDPRHVLVFGENCLFQEVLDRFGIKNAWHGEAAFWGSVSVGIDRLAAFNEADVICFDHGNE 243
Cdd:PRK10576  161 SAKPRLAGRGQRPLLLTSLIDPRHALVFGPNSLFQEVLDELGIENAWQGETNFWGSTVVGIERLAAYKDADVICFDHGNS 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1195228150 244 RDMAQLLATPLWQAMPFVRAGRFQRVPAVWFYGATLSAMHFARVLADAQG 293
Cdd:PRK10576  241 KDMQQLMATPLWQAMPFVRAGRFQRVPAVWFYGATLSAMHFVRVLDNALG 290
 
Name Accession Description Interval E-value
PRK10576 PRK10576
Fe(3+)-hydroxamate ABC transporter substrate-binding protein FhuD;
4-293 0e+00

Fe(3+)-hydroxamate ABC transporter substrate-binding protein FhuD;


Pssm-ID: 236719  Cd Length: 292  Bit Score: 558.47  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195228150   4 PTLITRRRLLIAMALSPLLWQMRGAQAADVDPQRVVALEWLPAELLLALGVTPYGVADIPNYRLWVNEPALPDSVIDVGL 83
Cdd:PRK10576    1 LPDISRRRLLTAMALSPLLWQMNTAAAAAIDPNRIVALEWLPVELLLALGVTPYGVADTHNYRLWVSEPALPDSVIDVGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195228150  84 RTEPNLELLTQMKPSFIVWSAGYGPSPEKLARIAPGRGFTFSDGKRPLAMAQRSLLEMADLLGKTQQAKRHLAEFDALME 163
Cdd:PRK10576   81 RTEPNLELLTQMKPSLILWSAGYGPSPEKLARIAPGRGFAFSDGKKPLAVARKSLVELAQRLNLEAAAETHLAQFDDFIA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195228150 164 SLRPRFAGRGDRPLLMISLLDPRHVLVFGENCLFQEVLDRFGIKNAWHGEAAFWGSVSVGIDRLAAFNEADVICFDHGNE 243
Cdd:PRK10576  161 SAKPRLAGRGQRPLLLTSLIDPRHALVFGPNSLFQEVLDELGIENAWQGETNFWGSTVVGIERLAAYKDADVICFDHGNS 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1195228150 244 RDMAQLLATPLWQAMPFVRAGRFQRVPAVWFYGATLSAMHFARVLADAQG 293
Cdd:PRK10576  241 KDMQQLMATPLWQAMPFVRAGRFQRVPAVWFYGATLSAMHFVRVLDNALG 290
FhuD cd01146
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial ...
 34-285 2.66e-74

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: 228.32  E-value: 2.66e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195228150  34 DPQRVVALEWLPAELLLALGVTPYGVADIPNYRLWVNEPALP-DSVIDVGLRTEPNLELLTQMKPSFIVWSAGYGP-SPE 111
Cdd:cd01146     2 KPQRIVALDWGALETLLALGVKPVGVADTAGYKPWIPEPALPlEGVVDVGTRGQPNLEAIAALKPDLILGSASRHDeIYD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195228150 112 KLARIAPGRGFTFSDgkrPLAMAQRSLLEMADLLGKTQQAKRHLAEFDALMESLRPRFAGRGDRPLLMISLLDPRHVLVF 191
Cdd:cd01146    82 QLSQIAPTVLLDSSP---WLAEWKENLRLIAKALGKEEEAEKLLAEYDQRLAELRQKLPDKGPKPVSVVRFSDAGSIRLY 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195228150 192 GENCLFQEVLDRFGIKNAWHGEAA-FWGSVSVGIDRLAAFNeADVICFDH-GNERDMAQLLATPLWQAMPFVRAGRFQRV 269
Cdd:cd01146   159 GPNSFAGSVLEDLGLQNPWAQETTnDSGFATISLERLAKAD-ADVLFVFTyEDEELAQALQANPLWQNLPAVKNGRVYVV 237

                         250
                  ....*....|....*..
gi 1195228150 270 PAV-WFYGATLSAMHFA 285
Cdd:cd01146   238 DDVwWFFGGGLSAARLL 254
FecB COG4594
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and ...
 34-291 2.15e-42

ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and metabolism];


Pssm-ID: 443650 [Multi-domain]  Cd Length: 316  Bit Score: 148.14  E-value: 2.15e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195228150  34 DPQRVVALEWLPAELLLALGVTPYGVADIPNYRLWVNEPA-LPDSVIDVGLRTEPNLELLTQMKPSFIVWS-----AGYg 107
Cdd:COG4594    51 TPKRVVVLEWSFADALLALGVTPVGIADDNDYDRWVPYLRdLIKGVTSVGTRSQPNLEAIAALKPDLIIADksrheAIY- 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195228150 108 pspEKLARIAPgrgfT--FSDGKRPLAMAQRSLLEMADLLGKTQQAKRHLAEFDALMESLRPRF-AGRGDRPLLMISLLD 184
Cdd:COG4594   130 ---DQLSKIAP----TvlFKSRNGDYQENLESFKTIAKALGKEEEAEAVLADHDQRIAEAKAKLaAADKGKKVAVGQFRA 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195228150 185 PrHVLVFGENCLFQEVLDRFGIKNAWH-GEAAFWGSVSVGIDRLAAFNeADVI-CFDHGNERDMAQLLATPLWQAMPFVR 262
Cdd:COG4594   203 D-GLRLYTPNSFAGSVLAALGFENPPKqSKDNGYGYSEVSLEQLPALD-PDVLfIATYDDPSILKEWKNNPLWKNLKAVK 280

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1195228150 263 AGRFQRVP-AVW-FYGATLSAMHFARVLADA 291
Cdd:COG4594   281 NGRVYEVDgDLWtRGRGPLAAELMADDLVEI 311
Peripla_BP_2 pfam01497
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ...
 39-271 2.57e-33

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: 122.09  E-value: 2.57e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195228150  39 VALEWLPAELLLALGVTPYGVADIPNYRLWVNEPALPDsVIDVGLRTEPNLELLTQMKPSFIVWSAGYGPSP--EKLARI 116
Cdd:pfam01497   1 AALSPAYTEILYALGATDSIVGVDAYTRDPLKADAVAA-IVKVGAYGEINVERLAALKPDLVILSTGYLTDEaeELLSLI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195228150 117 APGRGFTFSDGKRPLamaQRSLLEMADLLGKTQQAKRHLAEFDALMESLRPRFAGRGDRPLLMISLLDPRHVLVFGENCL 196
Cdd:pfam01497  80 IPTVIFESSSTGESL---KEQIKQLGELLGLEDEAEELVAEIDSALAAAKKAVPSLTRKPVLVFGGADGGGYVVAGSNTY 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1195228150 197 FQEVLDRFGIKNaWHGEAAFWGSVSVGIDRLAAFNEADVICFDHGNERDM--AQLLATPLWQAMPFVRAGRFQRVPA 271
Cdd:pfam01497 157 IGDLLRILGIEN-IAAELSGSEYAPISFEAILSSNPDVIIVSGRDSFTKTgpEFVAANPLWAGLPAVKNGRVYTLPS 232
 
Name Accession Description Interval E-value
PRK10576 PRK10576
Fe(3+)-hydroxamate ABC transporter substrate-binding protein FhuD;
4-293 0e+00

Fe(3+)-hydroxamate ABC transporter substrate-binding protein FhuD;


Pssm-ID: 236719  Cd Length: 292  Bit Score: 558.47  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195228150   4 PTLITRRRLLIAMALSPLLWQMRGAQAADVDPQRVVALEWLPAELLLALGVTPYGVADIPNYRLWVNEPALPDSVIDVGL 83
Cdd:PRK10576    1 LPDISRRRLLTAMALSPLLWQMNTAAAAAIDPNRIVALEWLPVELLLALGVTPYGVADTHNYRLWVSEPALPDSVIDVGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195228150  84 RTEPNLELLTQMKPSFIVWSAGYGPSPEKLARIAPGRGFTFSDGKRPLAMAQRSLLEMADLLGKTQQAKRHLAEFDALME 163
Cdd:PRK10576   81 RTEPNLELLTQMKPSLILWSAGYGPSPEKLARIAPGRGFAFSDGKKPLAVARKSLVELAQRLNLEAAAETHLAQFDDFIA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195228150 164 SLRPRFAGRGDRPLLMISLLDPRHVLVFGENCLFQEVLDRFGIKNAWHGEAAFWGSVSVGIDRLAAFNEADVICFDHGNE 243
Cdd:PRK10576  161 SAKPRLAGRGQRPLLLTSLIDPRHALVFGPNSLFQEVLDELGIENAWQGETNFWGSTVVGIERLAAYKDADVICFDHGNS 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1195228150 244 RDMAQLLATPLWQAMPFVRAGRFQRVPAVWFYGATLSAMHFARVLADAQG 293
Cdd:PRK10576  241 KDMQQLMATPLWQAMPFVRAGRFQRVPAVWFYGATLSAMHFVRVLDNALG 290
FhuD cd01146
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial ...
 34-285 2.66e-74

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: 228.32  E-value: 2.66e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195228150  34 DPQRVVALEWLPAELLLALGVTPYGVADIPNYRLWVNEPALP-DSVIDVGLRTEPNLELLTQMKPSFIVWSAGYGP-SPE 111
Cdd:cd01146     2 KPQRIVALDWGALETLLALGVKPVGVADTAGYKPWIPEPALPlEGVVDVGTRGQPNLEAIAALKPDLILGSASRHDeIYD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195228150 112 KLARIAPGRGFTFSDgkrPLAMAQRSLLEMADLLGKTQQAKRHLAEFDALMESLRPRFAGRGDRPLLMISLLDPRHVLVF 191
Cdd:cd01146    82 QLSQIAPTVLLDSSP---WLAEWKENLRLIAKALGKEEEAEKLLAEYDQRLAELRQKLPDKGPKPVSVVRFSDAGSIRLY 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195228150 192 GENCLFQEVLDRFGIKNAWHGEAA-FWGSVSVGIDRLAAFNeADVICFDH-GNERDMAQLLATPLWQAMPFVRAGRFQRV 269
Cdd:cd01146   159 GPNSFAGSVLEDLGLQNPWAQETTnDSGFATISLERLAKAD-ADVLFVFTyEDEELAQALQANPLWQNLPAVKNGRVYVV 237

                         250
                  ....*....|....*..
gi 1195228150 270 PAV-WFYGATLSAMHFA 285
Cdd:cd01146   238 DDVwWFFGGGLSAARLL 254
FecB COG4594
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and ...
 34-291 2.15e-42

ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and metabolism];


Pssm-ID: 443650 [Multi-domain]  Cd Length: 316  Bit Score: 148.14  E-value: 2.15e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195228150  34 DPQRVVALEWLPAELLLALGVTPYGVADIPNYRLWVNEPA-LPDSVIDVGLRTEPNLELLTQMKPSFIVWS-----AGYg 107
Cdd:COG4594    51 TPKRVVVLEWSFADALLALGVTPVGIADDNDYDRWVPYLRdLIKGVTSVGTRSQPNLEAIAALKPDLIIADksrheAIY- 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195228150 108 pspEKLARIAPgrgfT--FSDGKRPLAMAQRSLLEMADLLGKTQQAKRHLAEFDALMESLRPRF-AGRGDRPLLMISLLD 184
Cdd:COG4594   130 ---DQLSKIAP----TvlFKSRNGDYQENLESFKTIAKALGKEEEAEAVLADHDQRIAEAKAKLaAADKGKKVAVGQFRA 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195228150 185 PrHVLVFGENCLFQEVLDRFGIKNAWH-GEAAFWGSVSVGIDRLAAFNeADVI-CFDHGNERDMAQLLATPLWQAMPFVR 262
Cdd:COG4594   203 D-GLRLYTPNSFAGSVLAALGFENPPKqSKDNGYGYSEVSLEQLPALD-PDVLfIATYDDPSILKEWKNNPLWKNLKAVK 280

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1195228150 263 AGRFQRVP-AVW-FYGATLSAMHFARVLADA 291
Cdd:COG4594   281 NGRVYEVDgDLWtRGRGPLAAELMADDLVEI 311
FepB COG0614
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ...
 37-291 3.56e-40

ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and metabolism];


Pssm-ID: 440379 [Multi-domain]  Cd Length: 264  Bit Score: 140.90  E-value: 3.56e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195228150  37 RVVALEWLPAELLLALGVTPYGVAdIPNYRLWVNEPALPDSVIDVGLRTEPNLELLTQMKPSFIV--WSAGYGPSPEKLA 114
Cdd:COG0614     2 RIVSLSPSATELLLALGAGDRLVG-VSDWGYCDYPELELKDLPVVGGTGEPNLEAILALKPDLVLasSSGNDEEDYEQLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195228150 115 RI-APgrgfTFSDGKRPLAMAQRSLLEMADLLGKTQQAKRHLAEFDALMESLRPRFAGRGDRPLLMISLLDPRHVLVFGE 193
Cdd:COG0614    81 KIgIP----VVVLDPRSLEDLYESIRLLGELLGREERAEALIAEYEARLAAVRARLAGAEERPTVLYEIWSGDPLYTAGG 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195228150 194 NCLFQEVLDRFGIKNAWHGEAAFWGSVSvgIDRLAAFNeADVICFDHGN------ERDMAQLLATPLWQAMPFVRAGRFQ 267
Cdd:COG0614   157 GSFIGELLELAGGRNVAADLGGGYPEVS--LEQVLALD-PDVIILSGGGydaetaEEALEALLADPGWQSLPAVKNGRVY 233

                         250       260
                  ....*....|....*....|....
gi 1195228150 268 RVPAVWFYGATLSAMHFARVLADA 291
Cdd:COG0614   234 VVPGDLLSRPGPRLLLALEDLAKA 257
Peripla_BP_2 pfam01497
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ...
 39-271 2.57e-33

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: 122.09  E-value: 2.57e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195228150  39 VALEWLPAELLLALGVTPYGVADIPNYRLWVNEPALPDsVIDVGLRTEPNLELLTQMKPSFIVWSAGYGPSP--EKLARI 116
Cdd:pfam01497   1 AALSPAYTEILYALGATDSIVGVDAYTRDPLKADAVAA-IVKVGAYGEINVERLAALKPDLVILSTGYLTDEaeELLSLI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195228150 117 APGRGFTFSDGKRPLamaQRSLLEMADLLGKTQQAKRHLAEFDALMESLRPRFAGRGDRPLLMISLLDPRHVLVFGENCL 196
Cdd:pfam01497  80 IPTVIFESSSTGESL---KEQIKQLGELLGLEDEAEELVAEIDSALAAAKKAVPSLTRKPVLVFGGADGGGYVVAGSNTY 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1195228150 197 FQEVLDRFGIKNaWHGEAAFWGSVSVGIDRLAAFNEADVICFDHGNERDM--AQLLATPLWQAMPFVRAGRFQRVPA 271
Cdd:pfam01497 157 IGDLLRILGIEN-IAAELSGSEYAPISFEAILSSNPDVIIVSGRDSFTKTgpEFVAANPLWAGLPAVKNGRVYTLPS 232
TroA-like cd00636
Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function ...
 36-180 5.50e-21

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: 86.84  E-value: 5.50e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195228150  36 QRVVALEWLPAELLLALG--VTPYGVADIPNYRLWVNEPalPDSVIDVGLRTEPNLELLTQMKPSFIVWSAGYGPS-PEK 112
Cdd:cd00636     1 KRVVALDPGATELLLALGgdDKPVGVADPSGYPPEAKAL--LEKVPDVGHGYEPNLEKIAALKPDLIIANGSGLEAwLDK 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1195228150 113 LARIAPGRGFTFSDGKRPLAMAQRSLLEMADLLGKTQQAKRHLAEFDALMESLRPRFAGRGDRPLLMI 180
Cdd:cd00636    79 LSKIAIPVVVVDEASELSLENIKESIRLIGKALGKEENAEELIAELDARLAELRAKLAKIPKKKVSLV 146
FatB cd01140
Siderophore binding protein FatB. These proteins have been shown to function as ABC-type ...
 35-209 7.80e-18

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: 81.15  E-value: 7.80e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195228150  35 PQRVVALEWLPAELLLALGVTPYGVAD---IPNYRlwvnEPALPDSVIDVGLRTEPNLELLTQMKPSFIVWSAGYGPSPE 111
Cdd:cd01140    12 PEKVVVFDVGALDTLDALGVKVVGVPKsstLPEYL----KKYKDDKYANVGTLFEPDLEAIAALKPDLIIIGGRLAEKYD 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195228150 112 KLARIAPGRGFtFSDGKRPLAMAQRSLLEMADLLGKTQQAKRHLAEFDALMESLRPRFAGRGDrplLMISLLDPRHVLVF 191
Cdd:cd01140    88 ELKKIAPTIDL-GADLKNYLESVKQNIETLGKIFGKEEEAKELVAEIDASIAEAKSAAKGKKK---ALVVLVNGGKLSAF 163

                         170
                  ....*....|....*...
gi 1195228150 192 GENCLFQEVLDRFGIKNA 209
Cdd:cd01140   164 GPGSRFGWLHDLLGFEPA 181
FeuA cd01138
Periplasmic binding protein FeuA. These proteins have predicted to function as initial ...
 33-265 1.30e-15

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: 74.68  E-value: 1.30e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195228150  33 VDPQRVVALEwLPAELLLALGVTPYGVADIPNyrlwvnepALPD-----SVIDVGLRTEPNLELLTQMKPSFIVWSAGYG 107
Cdd:cd01138     7 AKPKRIVALS-GETEGLALLGIKPVGAASIGG--------KNPYykkktLAKVVGIVDEPNLEKVLELKPDLIIVSSKQE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195228150 108 PSPEKLARIAPgrgfTFS---DGKRPLAmaqrSLLEMADLLGKTQQAKRHLAEFDALMESLRPRFAGRGDRPLLMISLLD 184
Cdd:cd01138    78 ENYEKLSKIAP----TVPvsyNSSDWEE----QLKEIGKLLNKEDEAEKWLADYKQKAKEAKEKIKKKLGNDKSVAVLRG 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195228150 185 PRHVLVFGENCLF-QEVLDRF-------GIKNAWHGEAafWGSVSvgIDRLAAFNeAD--VICFDHGNErDMAQLLATPL 254
Cdd:cd01138   150 RKQIYVFGEDGRGgGPILYADlglkapeKVKEIEDKPG--YAAIS--LEVLPEFD-ADyiFLLFFTGPE-AKADFESLPI 223

                         250
                  ....*....|.
gi 1195228150 255 WQAMPFVRAGR 265
Cdd:cd01138   224 WKNLPAVKNNH 234
CeuA COG4607
ABC-type enterochelin transport system, periplasmic component [Inorganic ion transport and ...
 25-232 3.32e-15

ABC-type enterochelin transport system, periplasmic component [Inorganic ion transport and metabolism];


Pssm-ID: 443657 [Multi-domain]  Cd Length: 310  Bit Score: 74.45  E-value: 3.32e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195228150  25 MRGAQAADVDPQRVVALEWLPAELLLALGVTPYGVAD--IPNYrlwvNEPALPDSVIDVGLRTEPNLELLTQMKPSFIVW 102
Cdd:COG4607    41 ALGTVEVPKNPKRVVVFDNGALDTLDALGVEVAGVPKglLPDY----LSKYADDKYANVGTLFEPDLEAIAALKPDLIII 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195228150 103 SAGYGPSPEKLARIAPgrgfTFS---DGKRPLAMAQRSLLEMADLLGKTQQAKRHLAEFDALMESLRPRFAGRGDRPLLM 179
Cdd:COG4607   117 GGRSAKKYDELSKIAP----TIDltvDGEDYLESLKRNTETLGEIFGKEDEAEELVADLDAKIAALKAAAAGKGTALIVL 192

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1195228150 180 -----ISLLDPRHVL-----VFGenclFQEVLDrfGIKNAWHGEAafwgsVSVG------------IDRLAAFNE 232
Cdd:COG4607   193 tnggkISAYGPGSRFgpihdVLG----FKPADE--DIEASTHGQA-----ISFEfiaeanpdwlfvIDRDAAIGG 256
fecB PRK11411
iron-dicitrate transporter substrate-binding subunit; Provisional
 10-272 7.88e-11

iron-dicitrate transporter substrate-binding subunit; Provisional


Pssm-ID: 183123 [Multi-domain]  Cd Length: 303  Bit Score: 61.61  E-value: 7.88e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195228150  10 RRLLIAMALSPLLWQMRG-AQAADVD-----------PQRVVALEWLPAELLLALGVTPYGVAD--IPNYRLwvnePALP 75
Cdd:PRK11411    2 LAFIRLLFAGLLLLSGSShAFAVTVQdeqgtftlektPQRIVVLELSFVDALAAVGVSPVGVADdnDAKRIL----PEVR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195228150  76 DSV---IDVGLRTEPNLELLTQMKPSFIV-----WSAGYgpspEKLARIAP-----GRGFTFSDGkrpLAMAQRslleMA 142
Cdd:PRK11411   78 AHLkpwQSVGTRSQPSLEAIAALKPDLIIadssrHAGVY----IALQKIAPtlllkSRNETYQEN---LQSAAI----IG 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195228150 143 DLLGKTQQAKRHLAEFDALMESLRPRFAgRGDRPLLMISLLDprHVLVFGENCLFQEVLDRFGIK--NAWHGEAAFwgsV 220
Cdd:PRK11411  147 EVLGKKREMQARIEQHKERMAQFASQLP-KGTRVAFGTSREQ--QFNLHSPESYTGSVLAALGLNvpKAPMNGAAM---P 220

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1195228150 221 SVGIDRLAAFNEADVICFDHGNERDMAQLLATPLWQAMPFVRAgrfQRVPAV 272
Cdd:PRK11411  221 SISLEQLLALNPDWLLVAHYRQESIVKRWQQDPLWQMLTAAKK---QQVASV 269
TroA_e cd01142
Periplasmic binding protein TroA_e. These proteins are predicted to function as initial ...
 34-275 1.86e-07

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: 51.59  E-value: 1.86e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195228150  34 DPQRVVALEWLPAELLLALGVTPYGVADIPnyrLWVNEPALP------DSVIDVGLRTEPNLELLTQMKPSFIVWSAGYG 107
Cdd:cd01142    23 EVKRIAALWGAGNAVVAALGGGKLIVATTS---TVQQEPWLYrlapslENVATGGTGNDVNIEELLALKPDVVIVWSTDG 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195228150 108 PSP-EKLARIAPGRGFTFSDGKRplamAQRSLLEMADLLGKTQQAKRHLAEFDALMESLRPRFAGR--GDRPLLMISLLD 184
Cdd:cd01142   100 KEAgKAVLRLLNALSLRDAELEE----VKLTIALLGELLGRQEKAEALVAYFDDNLAYVAARTKKLpdSERPRVYYAGPD 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195228150 185 PrhVLVFGENCLFQEVLDRFGIKNAwHGEAAFWGSVSVGIDRLAAFNeADVICFDHGNERDmaQLLATPLWQAMPFVRAG 264
Cdd:cd01142   176 P--LTTDGTGSITNSWIDLAGGINV-ASEATKKGSGEVSLEQLLKWN-PDVIIVGNADTKA--AILADPRWQNLRAVKNG 249

                         250
                  ....*....|.
gi 1195228150 265 RFQRVPAVWFY 275
Cdd:cd01142   250 RVYVNPEGAFW 260
TroA_a cd01148
Metal binding protein TroA_a. These proteins are predicted to function as initial receptors ...
 35-272 5.18e-07

Metal binding protein TroA_a. These proteins are predicted to function as initial receptors in ABC transport of metal ions in eubacteria. They belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind the metal ion in the cleft between these domains.


Pssm-ID: 238568 [Multi-domain]  Cd Length: 284  Bit Score: 50.03  E-value: 5.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195228150  35 PQRVVALEWLPAELLLALGVTPYGVA-------DIPNYRlwvnepALPDSVIDVGlRTEPNLELLTQMKPSFIVWSAGYG 107
Cdd:cd01148    18 PQRVVSNDQNTTEMMLALGLQDRMVGtagidnkDLPELK------AKYDKVPELA-KKYPSKETVLAARPDLVFGGWSYG 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195228150 108 PSPEKLARIA------------------PGRGFTFSDGKrplamaqRSLLEMADLLGKTQQAKRHLAEFDALMESLRPRF 169
Cdd:cd01148    91 FDKGGLGTPDslaelgiktyilpescgqRRGEATLDDVY-------NDIRNLGKIFDVEDRADKLVADLKARLAEISAKV 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195228150 170 AGRGDRP-LLMISLLDPRhVLVFGENCLFQEVLDRFGIKNAWHGEAAFWGSVSVgiDRLAAFNeADVICF-DHGNERDMA 247
Cdd:cd01148   164 KGDGKKVaVFVYDSGEDK-PFTSGRGGIPNAIITAAGGRNVFADVDESWTTVSW--ETVIARN-PDVIVIiDYGDQNAAE 239

                         250       260
                  ....*....|....*....|....*....
gi 1195228150 248 Q----LLATPLWQAMPFVRAGRFQRVPAV 272
Cdd:cd01148   240 QkikfLKENPALKNVPAVKNNRFIVLPLA 268
YvrC cd01143
Periplasmic binding protein YvrC. These proteins are predicted to function as initial ...
 35-216 5.61e-07

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: 49.20  E-value: 5.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195228150  35 PQRVVALewLPA--ELLLALGVTPY--GVADIPNYrlwvnEPALPDSVIdVGLRTEPNLELLTQMKPSFIVWSAGYGPSP 110
Cdd:cd01143     3 PERIVSL--SPSitEILFALGAGDKivGVDTYSNY-----PKEVRKKPK-VGSYSNPNVEKIVALKPDLVIVSSSSLAEL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195228150 111 -EKLARiapgRGFT--FSDGKRPLAMAQRSLLEMADLLGKTQQAKRHLAEFDALMESLRPrfAGRGDRPLLMISLLDPRH 187
Cdd:cd01143    75 lEKLKD----AGIPvvVLPAASSLDEIYDQIELIGKITGAEEEAEKLVKEMKQKIDKVKD--KGKTIKKSKVYIEVSLGG 148

                         170       180
                  ....*....|....*....|....*....
gi 1195228150 188 VLVFGENCLFQEVLDRFGIKNAWHGEAAF 216
Cdd:cd01143   149 PYTAGKNTFINELIRLAGAKNIAADSGGW 177
BtuF cd01144
Cobalamin binding protein BtuF. These proteins have been shown to function as initial ...
 36-275 9.94e-07

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: 48.84  E-value: 9.94e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195228150  36 QRVVALewLPA--ELLLALGV--TPYGVADIPNYrlwvnePALPDSVIDVGLRTEPNLELLTQMKPSFIV-WSAGYGPSp 110
Cdd:cd01144     1 MRIVSL--APSatELLYALGLgdQLVGVTDYCDY------PPEAKKLPRVGGFYQLDLERVLALKPDLVIaWDDCNVCA- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195228150 111 ekLARIAPGRGFT--FSDGKRPLAMAQrSLLEMADLLGKTQQAKRHLAEFDALMESLRPRFAGRGDRPLLMISLLDPrhv 188
Cdd:cd01144    72 --VVDQLRAAGIPvlVSEPQTLDDILA-DIRRLGTLAGRPARAEELAEALRRRLAALRKQYASKPPPRVFYQEWIDP--- 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195228150 189 LVFGENCLFQEVLDRFGIKNAWHGEAAFWGSVSvgIDRLAAFNeADVICF-DHGNERDMAQLLATPLWQAMPFVRAGRFQ 267
Cdd:cd01144   146 LMTAGGDWVPELIALAGGVNVFADAGERSPQVS--WEDVLAAN-PDVIVLsPCGFGFTPAILRKEPAWQALPAVRNGRVY 222


                  ....*...
gi 1195228150 268 RVPAVWFY 275
Cdd:cd01144   223 AVDGNWYF 230
TroA_d cd01141
Periplasmic binding protein TroA_d. These proteins are predicted to function as initial ...
 28-108 2.00e-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: 47.42  E-value: 2.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195228150  28 AQAADVDPQRVVALEWLPAELLLALGVTPyGVADIPNYRLWVNEPALPDSV-IDVGLRTEPNLELLTQMKPSFIVWSAGY 106
Cdd:cd01141     1 AKTIKVPPKRIVVLSPTHVDLLLALDKAD-KIVGVSASAYDLNTPAVKERIdIQVGPTGSLNVELIVALKPDLVILYGGF 79


                  ..
gi 1195228150 107 GP 108
Cdd:cd01141    80 QA 81
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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