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Conserved domains on  [gi|445938138|ref|WP_000015993|]
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MULTISPECIES: Fe(3+)-hydroxamate ABC transporter substrate-binding protein FhuD [Enterobacteriaceae]

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;
4-295 0e+00

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


:

Pssm-ID: 236719  Cd Length: 292  Bit Score: 579.66  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445938138   4 LPLISRRRLLTAMALSPLLWQMNTAHAAAIDPNRIVALEWLPVELLLALGIVPYGVADTINYRLWVSEPPLPDSVIDVGL 83
Cdd:PRK10576   1 LPDISRRRLLTAMALSPLLWQMNTAAAAAIDPNRIVALEWLPVELLLALGVTPYGVADTHNYRLWVSEPALPDSVIDVGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445938138  84 RTEPNLELLTEMKPSFMVWSAGYGPSSEMLARIAPGRGFNFSDGKQPLAMARKSLTEMADLLNLQSAAETHLAHYEDFIR 163
Cdd:PRK10576  81 RTEPNLELLTQMKPSLILWSAGYGPSPEKLARIAPGRGFAFSDGKKPLAVARKSLVELAQRLNLEAAAETHLAQFDDFIA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445938138 164 SMKPRFVKRGERPLLLTTLIDPRHMLVFGPNSLFQEILDEYGIPNAWQGETNFWGSTAVSIDRLAAYKDVDVLCFDHDNS 243
Cdd:PRK10576 161 SAKPRLAGRGQRPLLLTSLIDPRHALVFGPNSLFQEVLDELGIENAWQGETNFWGSTVVGIERLAAYKDADVICFDHGNS 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 445938138 244 KDMDALMATPLWQAMPFVRAGRFQRVPAVWFYGATLSAMHFVRVLDNAIGGK 295
Cdd:PRK10576 241 KDMQQLMATPLWQAMPFVRAGRFQRVPAVWFYGATLSAMHFVRVLDNALGGK 292
 
Name Accession Description Interval E-value
PRK10576 PRK10576
Fe(3+)-hydroxamate ABC transporter substrate-binding protein FhuD;
4-295 0e+00

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


Pssm-ID: 236719  Cd Length: 292  Bit Score: 579.66  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445938138   4 LPLISRRRLLTAMALSPLLWQMNTAHAAAIDPNRIVALEWLPVELLLALGIVPYGVADTINYRLWVSEPPLPDSVIDVGL 83
Cdd:PRK10576   1 LPDISRRRLLTAMALSPLLWQMNTAAAAAIDPNRIVALEWLPVELLLALGVTPYGVADTHNYRLWVSEPALPDSVIDVGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445938138  84 RTEPNLELLTEMKPSFMVWSAGYGPSSEMLARIAPGRGFNFSDGKQPLAMARKSLTEMADLLNLQSAAETHLAHYEDFIR 163
Cdd:PRK10576  81 RTEPNLELLTQMKPSLILWSAGYGPSPEKLARIAPGRGFAFSDGKKPLAVARKSLVELAQRLNLEAAAETHLAQFDDFIA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445938138 164 SMKPRFVKRGERPLLLTTLIDPRHMLVFGPNSLFQEILDEYGIPNAWQGETNFWGSTAVSIDRLAAYKDVDVLCFDHDNS 243
Cdd:PRK10576 161 SAKPRLAGRGQRPLLLTSLIDPRHALVFGPNSLFQEVLDELGIENAWQGETNFWGSTVVGIERLAAYKDADVICFDHGNS 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 445938138 244 KDMDALMATPLWQAMPFVRAGRFQRVPAVWFYGATLSAMHFVRVLDNAIGGK 295
Cdd:PRK10576 241 KDMQQLMATPLWQAMPFVRAGRFQRVPAVWFYGATLSAMHFVRVLDNALGGK 292
FhuD cd01146
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial ...
 34-285 1.50e-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: 228.71  E-value: 1.50e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445938138  34 DPNRIVALEWLPVELLLALGIVPYGVADTINYRLWVSEPPLP-DSVIDVGLRTEPNLELLTEMKPSFMVWSAGYGPSS-E 111
Cdd:cd01146    2 KPQRIVALDWGALETLLALGVKPVGVADTAGYKPWIPEPALPlEGVVDVGTRGQPNLEAIAALKPDLILGSASRHDEIyD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445938138 112 MLARIAPGRGFNFSDgkqPLAMARKSLTEMADLLNLQSAAETHLAHYEDFIRSMKPRFVKRGERPLLLTTLIDPRHMLVF 191
Cdd:cd01146   82 QLSQIAPTVLLDSSP---WLAEWKENLRLIAKALGKEEEAEKLLAEYDQRLAELRQKLPDKGPKPVSVVRFSDAGSIRLY 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445938138 192 GPNSLFQEILDEYGIPNAW-QGETNFWGSTAVSIDRLAAYkDVDVLCFDHD-NSKDMDALMATPLWQAMPFVRAGRFQRV 269
Cdd:cd01146  159 GPNSFAGSVLEDLGLQNPWaQETTNDSGFATISLERLAKA-DADVLFVFTYeDEELAQALQANPLWQNLPAVKNGRVYVV 237

                        250
                 ....*....|....*..
gi 445938138 270 PAV-WFYGATLSAMHFV 285
Cdd:cd01146  238 DDVwWFFGGGLSAARLL 254
FecB COG4594
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and ...
 34-296 1.88e-35

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


Pssm-ID: 443650 [Multi-domain]  Cd Length: 316  Bit Score: 129.66  E-value: 1.88e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445938138  34 DPNRIVALEWLPVELLLALGIVPYGVADTINYRLWVSEP-PLPDSVIDVGLRTEPNLELLTEMKP-----SFMVWSAGYg 107
Cdd:COG4594   51 TPKRVVVLEWSFADALLALGVTPVGIADDNDYDRWVPYLrDLIKGVTSVGTRSQPNLEAIAALKPdliiaDKSRHEAIY- 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445938138 108 pssEMLARIAPGRGFNFSDGkqPLAMARKSLTEMADLLNLQSAAETHLAHYEDFIRSMKPRFVKRGE-RPLLLTTLIDPr 186
Cdd:COG4594  130 ---DQLSKIAPTVLFKSRNG--DYQENLESFKTIAKALGKEEEAEAVLADHDQRIAEAKAKLAAADKgKKVAVGQFRAD- 203

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445938138 187 HMLVFGPNSLFQEILDEYGIPNAW-QGETNFWGSTAVSIDRLAAYkDVDVL-CFDHDNSKDMDALMATPLWQAMPFVRAG 264
Cdd:COG4594  204 GLRLYTPNSFAGSVLAALGFENPPkQSKDNGYGYSEVSLEQLPAL-DPDVLfIATYDDPSILKEWKNNPLWKNLKAVKNG 282

                        250       260       270
                 ....*....|....*....|....*....|....
gi 445938138 265 RFQRVP-AVW-FYGATLSAMHFVRVLDNAIGGKA 296
Cdd:COG4594  283 RVYEVDgDLWtRGRGPLAAELMADDLVEILLKKK 316
Peripla_BP_2 pfam01497
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ...
 39-271 2.85e-30

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: 114.00  E-value: 2.85e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445938138   39 VALEWLPVELLLALGIVPYGVADtINYRLWVSEPPLPDSVIDVGLRTEPNLELLTEMKPSFMVWSAGYGPSS--EMLARI 116
Cdd:pfam01497   1 AALSPAYTEILYALGATDSIVGV-DAYTRDPLKADAVAAIVKVGAYGEINVERLAALKPDLVILSTGYLTDEaeELLSLI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445938138  117 APGRGFNFSDGKQPLamaRKSLTEMADLLNLQSAAETHLAHYEDFIRSMKPRFVKRGERPLLLTTLIDPRHMLVFGPNSL 196
Cdd:pfam01497  80 IPTVIFESSSTGESL---KEQIKQLGELLGLEDEAEELVAEIDSALAAAKKAVPSLTRKPVLVFGGADGGGYVVAGSNTY 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 445938138  197 FQEILDEYGIPNaWQGETNFWGSTAVSIDRLAAYkDVDVL---CFDHDNSKDMDALMATPLWQAMPFVRAGRFQRVPA 271
Cdd:pfam01497 157 IGDLLRILGIEN-IAAELSGSEYAPISFEAILSS-NPDVIivsGRDSFTKTGPEFVAANPLWAGLPAVKNGRVYTLPS 232
 
Name Accession Description Interval E-value
PRK10576 PRK10576
Fe(3+)-hydroxamate ABC transporter substrate-binding protein FhuD;
4-295 0e+00

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


Pssm-ID: 236719  Cd Length: 292  Bit Score: 579.66  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445938138   4 LPLISRRRLLTAMALSPLLWQMNTAHAAAIDPNRIVALEWLPVELLLALGIVPYGVADTINYRLWVSEPPLPDSVIDVGL 83
Cdd:PRK10576   1 LPDISRRRLLTAMALSPLLWQMNTAAAAAIDPNRIVALEWLPVELLLALGVTPYGVADTHNYRLWVSEPALPDSVIDVGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445938138  84 RTEPNLELLTEMKPSFMVWSAGYGPSSEMLARIAPGRGFNFSDGKQPLAMARKSLTEMADLLNLQSAAETHLAHYEDFIR 163
Cdd:PRK10576  81 RTEPNLELLTQMKPSLILWSAGYGPSPEKLARIAPGRGFAFSDGKKPLAVARKSLVELAQRLNLEAAAETHLAQFDDFIA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445938138 164 SMKPRFVKRGERPLLLTTLIDPRHMLVFGPNSLFQEILDEYGIPNAWQGETNFWGSTAVSIDRLAAYKDVDVLCFDHDNS 243
Cdd:PRK10576 161 SAKPRLAGRGQRPLLLTSLIDPRHALVFGPNSLFQEVLDELGIENAWQGETNFWGSTVVGIERLAAYKDADVICFDHGNS 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 445938138 244 KDMDALMATPLWQAMPFVRAGRFQRVPAVWFYGATLSAMHFVRVLDNAIGGK 295
Cdd:PRK10576 241 KDMQQLMATPLWQAMPFVRAGRFQRVPAVWFYGATLSAMHFVRVLDNALGGK 292
FhuD cd01146
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial ...
 34-285 1.50e-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: 228.71  E-value: 1.50e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445938138  34 DPNRIVALEWLPVELLLALGIVPYGVADTINYRLWVSEPPLP-DSVIDVGLRTEPNLELLTEMKPSFMVWSAGYGPSS-E 111
Cdd:cd01146    2 KPQRIVALDWGALETLLALGVKPVGVADTAGYKPWIPEPALPlEGVVDVGTRGQPNLEAIAALKPDLILGSASRHDEIyD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445938138 112 MLARIAPGRGFNFSDgkqPLAMARKSLTEMADLLNLQSAAETHLAHYEDFIRSMKPRFVKRGERPLLLTTLIDPRHMLVF 191
Cdd:cd01146   82 QLSQIAPTVLLDSSP---WLAEWKENLRLIAKALGKEEEAEKLLAEYDQRLAELRQKLPDKGPKPVSVVRFSDAGSIRLY 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445938138 192 GPNSLFQEILDEYGIPNAW-QGETNFWGSTAVSIDRLAAYkDVDVLCFDHD-NSKDMDALMATPLWQAMPFVRAGRFQRV 269
Cdd:cd01146  159 GPNSFAGSVLEDLGLQNPWaQETTNDSGFATISLERLAKA-DADVLFVFTYeDEELAQALQANPLWQNLPAVKNGRVYVV 237

                        250
                 ....*....|....*..
gi 445938138 270 PAV-WFYGATLSAMHFV 285
Cdd:cd01146  238 DDVwWFFGGGLSAARLL 254
FecB COG4594
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and ...
 34-296 1.88e-35

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


Pssm-ID: 443650 [Multi-domain]  Cd Length: 316  Bit Score: 129.66  E-value: 1.88e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445938138  34 DPNRIVALEWLPVELLLALGIVPYGVADTINYRLWVSEP-PLPDSVIDVGLRTEPNLELLTEMKP-----SFMVWSAGYg 107
Cdd:COG4594   51 TPKRVVVLEWSFADALLALGVTPVGIADDNDYDRWVPYLrDLIKGVTSVGTRSQPNLEAIAALKPdliiaDKSRHEAIY- 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445938138 108 pssEMLARIAPGRGFNFSDGkqPLAMARKSLTEMADLLNLQSAAETHLAHYEDFIRSMKPRFVKRGE-RPLLLTTLIDPr 186
Cdd:COG4594  130 ---DQLSKIAPTVLFKSRNG--DYQENLESFKTIAKALGKEEEAEAVLADHDQRIAEAKAKLAAADKgKKVAVGQFRAD- 203

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445938138 187 HMLVFGPNSLFQEILDEYGIPNAW-QGETNFWGSTAVSIDRLAAYkDVDVL-CFDHDNSKDMDALMATPLWQAMPFVRAG 264
Cdd:COG4594  204 GLRLYTPNSFAGSVLAALGFENPPkQSKDNGYGYSEVSLEQLPAL-DPDVLfIATYDDPSILKEWKNNPLWKNLKAVKNG 282

                        250       260       270
                 ....*....|....*....|....*....|....
gi 445938138 265 RFQRVP-AVW-FYGATLSAMHFVRVLDNAIGGKA 296
Cdd:COG4594  283 RVYEVDgDLWtRGRGPLAAELMADDLVEILLKKK 316
FepB COG0614
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ...
 37-292 2.18e-32

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


Pssm-ID: 440379 [Multi-domain]  Cd Length: 264  Bit Score: 120.49  E-value: 2.18e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445938138  37 RIVALEWLPVELLLALGIVPYGVAdtINYRLWVSEPPLP-DSVIDVGLRTEPNLELLTEMKPSFMV--WSAGYGPSSEML 113
Cdd:COG0614    2 RIVSLSPSATELLLALGAGDRLVG--VSDWGYCDYPELElKDLPVVGGTGEPNLEAILALKPDLVLasSSGNDEEDYEQL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445938138 114 ARI-APGRGFNFSdgkqPLAMARKSLTEMADLLNLQSAAETHLAHYEDFIRSMKPRFVKRGERPLLLTTLIDPRHMLVFG 192
Cdd:COG0614   80 EKIgIPVVVLDPR----SLEDLYESIRLLGELLGREERAEALIAEYEARLAAVRARLAGAEERPTVLYEIWSGDPLYTAG 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445938138 193 PNSLFQEILDEYGIPNAWQGETNFWGStaVSIDRLAAYkDVDVL------CFDHDNSKDMDALMATPLWQAMPFVRAGRF 266
Cdd:COG0614  156 GGSFIGELLELAGGRNVAADLGGGYPE--VSLEQVLAL-DPDVIilsgggYDAETAEEALEALLADPGWQSLPAVKNGRV 232

                        250       260
                 ....*....|....*....|....*.
gi 445938138 267 QRVPAVWFYGATLSAMHFVRVLDNAI 292
Cdd:COG0614  233 YVVPGDLLSRPGPRLLLALEDLAKAL 258
Peripla_BP_2 pfam01497
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ...
 39-271 2.85e-30

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: 114.00  E-value: 2.85e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445938138   39 VALEWLPVELLLALGIVPYGVADtINYRLWVSEPPLPDSVIDVGLRTEPNLELLTEMKPSFMVWSAGYGPSS--EMLARI 116
Cdd:pfam01497   1 AALSPAYTEILYALGATDSIVGV-DAYTRDPLKADAVAAIVKVGAYGEINVERLAALKPDLVILSTGYLTDEaeELLSLI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445938138  117 APGRGFNFSDGKQPLamaRKSLTEMADLLNLQSAAETHLAHYEDFIRSMKPRFVKRGERPLLLTTLIDPRHMLVFGPNSL 196
Cdd:pfam01497  80 IPTVIFESSSTGESL---KEQIKQLGELLGLEDEAEELVAEIDSALAAAKKAVPSLTRKPVLVFGGADGGGYVVAGSNTY 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 445938138  197 FQEILDEYGIPNaWQGETNFWGSTAVSIDRLAAYkDVDVL---CFDHDNSKDMDALMATPLWQAMPFVRAGRFQRVPA 271
Cdd:pfam01497 157 IGDLLRILGIEN-IAAELSGSEYAPISFEAILSS-NPDVIivsGRDSFTKTGPEFVAANPLWAGLPAVKNGRVYTLPS 232
FatB cd01140
Siderophore binding protein FatB. These proteins have been shown to function as ABC-type ...
 35-209 3.87e-15

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: 73.83  E-value: 3.87e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445938138  35 PNRIVALEWLPVELLLALGIVPYGVADTINyrlwvseppLP--------DSVIDVGLRTEPNLELLTEMKPSFMVWSAGY 106
Cdd:cd01140   12 PEKVVVFDVGALDTLDALGVKVVGVPKSST---------LPeylkkykdDKYANVGTLFEPDLEAIAALKPDLIIIGGRL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445938138 107 GPSSEMLARIAPGRGFnFSDGKQPLAMARKSLTEMADLLNLQSAAETHLAHYEDFIRSMKpRFVKRGERPLLLttLIDPR 186
Cdd:cd01140   83 AEKYDELKKIAPTIDL-GADLKNYLESVKQNIETLGKIFGKEEEAKELVAEIDASIAEAK-SAAKGKKKALVV--LVNGG 158

                        170       180
                 ....*....|....*....|...
gi 445938138 187 HMLVFGPNSLFQEILDEYGIPNA 209
Cdd:cd01140  159 KLSAFGPGSRFGWLHDLLGFEPA 181
TroA-like cd00636
Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function ...
 37-179 7.23e-14

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: 67.58  E-value: 7.23e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445938138  37 RIVALEWLPVELLLALG--IVPYGVADTINYRLWVSEPPlpDSVIDVGLRTEPNLELLTEMKPSFMVWSAGYGPSS-EML 113
Cdd:cd00636    2 RVVALDPGATELLLALGgdDKPVGVADPSGYPPEAKALL--EKVPDVGHGYEPNLEKIAALKPDLIIANGSGLEAWlDKL 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 445938138 114 ARIAPGRGFNFSDGKQPLAMARKSLTEMADLLNLQSAAETHLAHYEDFIRSMKPRFVKRGERPLLL 179
Cdd:cd00636   80 SKIAIPVVVVDEASELSLENIKESIRLIGKALGKEENAEELIAELDARLAELRAKLAKIPKKKVSL 145
FeuA cd01138
Periplasmic binding protein FeuA. These proteins have predicted to function as initial ...
 34-265 3.11e-11

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: 62.35  E-value: 3.11e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445938138  34 DPNRIVALEwLPVELLLALGIVPYGVADTINyrlwvsepPLPD-----SVIDVGLRTEPNLELLTEMKPSFMVWSAGYGP 108
Cdd:cd01138    8 KPKRIVALS-GETEGLALLGIKPVGAASIGG--------KNPYykkktLAKVVGIVDEPNLEKVLELKPDLIIVSSKQEE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445938138 109 SSEMLARIAPGRGFNfSDGKQPlamaRKSLTEMADLLNLQSAAETHLAHYEDFIRSMKPRFVKRGERPLLLTTLIDPRHM 188
Cdd:cd01138   79 NYEKLSKIAPTVPVS-YNSSDW----EEQLKEIGKLLNKEDEAEKWLADYKQKAKEAKEKIKKKLGNDKSVAVLRGRKQI 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445938138 189 LVFGPNSLFQEI----LDEYGIPNAWQGETNFWGSTAVSIDRLAAYkDVD-VLCFDHDNSKDMDALMATPLWQAMPFVRA 263
Cdd:cd01138  154 YVFGEDGRGGGPilyaDLGLKAPEKVKEIEDKPGYAAISLEVLPEF-DADyIFLLFFTGPEAKADFESLPIWKNLPAVKN 232


                 ..
gi 445938138 264 GR 265
Cdd:cd01138  233 NH 234
CeuA COG4607
ABC-type enterochelin transport system, periplasmic component [Inorganic ion transport and ...
 34-209 2.51e-08

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


Pssm-ID: 443657 [Multi-domain]  Cd Length: 310  Bit Score: 54.03  E-value: 2.51e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445938138  34 DPNRIVALEWLPVELLLALGIVPYGVADTInyrlwvseppLP--------DSVIDVGLRTEPNLELLTEMKPSFMVWSAG 105
Cdd:COG4607   50 NPKRVVVFDNGALDTLDALGVEVAGVPKGL----------LPdylskyadDKYANVGTLFEPDLEAIAALKPDLIIIGGR 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445938138 106 YGPSSEMLARIAP----GRgfnfsDGKQPLAMARKSLTEMADLLNLQSAAETHLAHYEDFIRSMKPRfVKRGERPL-LLT 180
Cdd:COG4607  120 SAKKYDELSKIAPtidlTV-----DGEDYLESLKRNTETLGEIFGKEDEAEELVADLDAKIAALKAA-AAGKGTALiVLT 193

                        170       180
                 ....*....|....*....|....*....
gi 445938138 181 TliDPRhMLVFGPNSLFQEILDEYGIPNA 209
Cdd:COG4607  194 N--GGK-ISAYGPGSRFGPIHDVLGFKPA 219
fecB PRK11411
iron-dicitrate transporter substrate-binding subunit; Provisional
 10-272 5.08e-07

iron-dicitrate transporter substrate-binding subunit; Provisional


Pssm-ID: 183123 [Multi-domain]  Cd Length: 303  Bit Score: 50.06  E-value: 5.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445938138  10 RRLLTAMALSpLLWQMNTAHAAAID-------------PNRIVALEWLPVELLLALGIVPYGVADTIN-YRL-------- 67
Cdd:PRK11411   2 LAFIRLLFAG-LLLLSGSSHAFAVTvqdeqgtftlektPQRIVVLELSFVDALAAVGVSPVGVADDNDaKRIlpevrahl 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445938138  68 --WVSepplpdsvidVGLRTEPNLELLTEMKPSFMV-----WSAGYgpssEMLARIAP-----GRGFNFsdgKQPLAMAR 135
Cdd:PRK11411  81 kpWQS----------VGTRSQPSLEAIAALKPDLIIadssrHAGVY----IALQKIAPtlllkSRNETY---QENLQSAA 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445938138 136 KslteMADLLNLQSAAETHLAHYEDFIRSMKPRFVKrGERPLLLTTLIDprHMLVFGPNSLFQEILDEYGI--PNAWQGE 213
Cdd:PRK11411 144 I----IGEVLGKKREMQARIEQHKERMAQFASQLPK-GTRVAFGTSREQ--QFNLHSPESYTGSVLAALGLnvPKAPMNG 216

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 445938138 214 TNFwgsTAVSIDRLAAyKDVDVLCFDH--DNSKdMDALMATPLWQAMPFVRAgrfQRVPAV 272
Cdd:PRK11411 217 AAM---PSISLEQLLA-LNPDWLLVAHyrQESI-VKRWQQDPLWQMLTAAKK---QQVASV 269
TroA_e cd01142
Periplasmic binding protein TroA_e. These proteins are predicted to function as initial ...
 34-275 3.44e-05

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: 44.65  E-value: 3.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445938138  34 DPNRIVALEWLPVELLLALGIVPYGVADTinyRLWVSEP------PLPDSVIDVGLRTEPNLELLTEMKPSfMVWSAGYG 107
Cdd:cd01142   23 EVKRIAALWGAGNAVVAALGGGKLIVATT---STVQQEPwlyrlaPSLENVATGGTGNDVNIEELLALKPD-VVIVWSTD 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445938138 108 PSSEMLARIAPGRGFNFSDGKqpLAMARKSLTEMADLLNLQSAAETHLAHYEDFIRSMKPRF--VKRGERPLLLTTLIDP 185
Cdd:cd01142   99 GKEAGKAVLRLLNALSLRDAE--LEEVKLTIALLGELLGRQEKAEALVAYFDDNLAYVAARTkkLPDSERPRVYYAGPDP 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445938138 186 rhMLVFGPNSLFQEILDEYGIPNAwQGETNFWGSTAVSIDRLAAYkDVDVLCFDHDNSKdmDALMATPLWQAMPFVRAGR 265
Cdd:cd01142  177 --LTTDGTGSITNSWIDLAGGINV-ASEATKKGSGEVSLEQLLKW-NPDVIIVGNADTK--AAILADPRWQNLRAVKNGR 250

                        250
                 ....*....|
gi 445938138 266 FQRVPAVWFY 275
Cdd:cd01142  251 VYVNPEGAFW 260
YvrC cd01143
Periplasmic binding protein YvrC. These proteins are predicted to function as initial ...
 35-216 4.48e-04

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: 40.34  E-value: 4.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445938138  35 PNRIVALewLP--VELLLALG----IVpyGVADTINYrlwvsePP-LPDSVIdVGLRTEPNLELLTEMKPSFMVWSAGYG 107
Cdd:cd01143    3 PERIVSL--SPsiTEILFALGagdkIV--GVDTYSNY------PKeVRKKPK-VGSYSNPNVEKIVALKPDLVIVSSSSL 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445938138 108 PSS-EMLARiapgRGFN--FSDGKQPLAMARKSLTEMADLLNLQSAAEThlahyedFIRSMKPRFVKRGERPLLLTT--- 181
Cdd:cd01143   72 AELlEKLKD----AGIPvvVLPAASSLDEIYDQIELIGKITGAEEEAEK-------LVKEMKQKIDKVKDKGKTIKKskv 140

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 445938138 182 --LIDPRHMLVFGPNSLFQEILDEYGIPNAWQGETNF 216
Cdd:cd01143  141 yiEVSLGGPYTAGKNTFINELIRLAGAKNIAADSGGW 177
BtuF cd01144
Cobalamin binding protein BtuF. These proteins have been shown to function as initial ...
 37-275 1.27e-03

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: 39.59  E-value: 1.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445938138  37 RIVALewLP--VELLLALGIVP--YGVADTINYrlwvsePPLPDSVIDVGLRTEPNLELLTEMKPSFMV-WSAGYGPSse 111
Cdd:cd01144    2 RIVSL--APsaTELLYALGLGDqlVGVTDYCDY------PPEAKKLPRVGGFYQLDLERVLALKPDLVIaWDDCNVCA-- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445938138 112 mLARIAPGRGFN-FSDGKQPLAMARKSLTEMADLLNLQSAAETHLAHYEDFIRSMKPRFVKRGERPLLLTTLIDPrhmlV 190
Cdd:cd01144   72 -VVDQLRAAGIPvLVSEPQTLDDILADIRRLGTLAGRPARAEELAEALRRRLAALRKQYASKPPPRVFYQEWIDP----L 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445938138 191 FGPNS-LFQEILDEYGIPN--AWQGEtnfwGSTAVSIDRLAAyKDVDVLCF-DHDNSKDMDALMATPLWQAMPFVRAGRF 266
Cdd:cd01144  147 MTAGGdWVPELIALAGGVNvfADAGE----RSPQVSWEDVLA-ANPDVIVLsPCGFGFTPAILRKEPAWQALPAVRNGRV 221


                 ....*....
gi 445938138 267 QRVPAVWFY 275
Cdd:cd01144  222 YAVDGNWYF 230
TroA_d cd01141
Periplasmic binding protein TroA_d. These proteins are predicted to function as initial ...
 33-112 5.98e-03

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: 37.02  E-value: 5.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445938138  33 IDPNRIVALEWLPVELLLALGivpygVADTI----NYRLWVSEPPLPDSV-IDVGLRTEPNLELLTEMKPSFMVWSAGYG 107
Cdd:cd01141    6 VPPKRIVVLSPTHVDLLLALD-----KADKIvgvsASAYDLNTPAVKERIdIQVGPTGSLNVELIVALKPDLVILYGGFQ 80


                 ....*
gi 445938138 108 PSSEM 112
Cdd:cd01141   81 AQTIL 85
 
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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