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Conserved domains on  [gi|15829410|ref|NP_308183|]
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iron(3+)-hydroxamate import ABC transporter periplasmic binding protein [Escherichia coli O157:H7 str. Sakai]

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: 576.58  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829410    4 LPLISRRRLLTAMALSPLLWQMNTAHAAAIDPNRIVALEWLPVELLLALGIVPYGVADTINYRLWVSEPPLPESVIDVGL 83
Cdd:PRK10576   1 LPDISRRRLLTAMALSPLLWQMNTAAAAAIDPNRIVALEWLPVELLLALGVTPYGVADTHNYRLWVSEPALPDSVIDVGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829410   84 RTEPNLELLTEMKPSFMVWSAGYGPSPEMLARIAPGRGFNFSDGKQPLAMARKSLTEMADLLNLQSAAETHLAQYEDFIR 163
Cdd:PRK10576  81 RTEPNLELLTQMKPSLILWSAGYGPSPEKLARIAPGRGFAFSDGKKPLAVARKSLVELAQRLNLEAAAETHLAQFDDFIA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829410  164 SMNPRFVKRGARPLLLTTLIDPRHMLVFGPNSLFQEILDEYGIPNAWQGETNFWGSTAVSIDRLAAYKDVDVLCFDHDNS 243
Cdd:PRK10576 161 SAKPRLAGRGQRPLLLTSLIDPRHALVFGPNSLFQEVLDELGIENAWQGETNFWGSTVVGIERLAAYKDADVICFDHGNS 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 15829410  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: 576.58  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829410    4 LPLISRRRLLTAMALSPLLWQMNTAHAAAIDPNRIVALEWLPVELLLALGIVPYGVADTINYRLWVSEPPLPESVIDVGL 83
Cdd:PRK10576   1 LPDISRRRLLTAMALSPLLWQMNTAAAAAIDPNRIVALEWLPVELLLALGVTPYGVADTHNYRLWVSEPALPDSVIDVGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829410   84 RTEPNLELLTEMKPSFMVWSAGYGPSPEMLARIAPGRGFNFSDGKQPLAMARKSLTEMADLLNLQSAAETHLAQYEDFIR 163
Cdd:PRK10576  81 RTEPNLELLTQMKPSLILWSAGYGPSPEKLARIAPGRGFAFSDGKKPLAVARKSLVELAQRLNLEAAAETHLAQFDDFIA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829410  164 SMNPRFVKRGARPLLLTTLIDPRHMLVFGPNSLFQEILDEYGIPNAWQGETNFWGSTAVSIDRLAAYKDVDVLCFDHDNS 243
Cdd:PRK10576 161 SAKPRLAGRGQRPLLLTSLIDPRHALVFGPNSLFQEVLDELGIENAWQGETNFWGSTVVGIERLAAYKDADVICFDHGNS 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 15829410  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 1.60e-73

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: 226.40  E-value: 1.60e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829410  34 DPNRIVALEWLPVELLLALGIVPYGVADTINYRLWVSEPPLP-ESVIDVGLRTEPNLELLTEMKPSFMVWSAGYGP-SPE 111
Cdd:cd01146   2 KPQRIVALDWGALETLLALGVKPVGVADTAGYKPWIPEPALPlEGVVDVGTRGQPNLEAIAALKPDLILGSASRHDeIYD 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829410 112 MLARIAPGRGFNFSDgkqPLAMARKSLTEMADLLNLQSAAETHLAQYEDFIRSMNPRFVKRGARPLLLTTLIDPRHMLVF 191
Cdd:cd01146  82 QLSQIAPTVLLDSSP---WLAEWKENLRLIAKALGKEEEAEKLLAEYDQRLAELRQKLPDKGPKPVSVVRFSDAGSIRLY 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829410 192 GPNSLFQEILDEYGIPNAW-QGETNFWGSTAVSIDRLAAYkDVDVLCFDHD-NSKDMDALMATPLWQAMPFVRAGRFQRV 269
Cdd:cd01146 159 GPNSFAGSVLEDLGLQNPWaQETTNDSGFATISLERLAKA-DADVLFVFTYeDEELAQALQANPLWQNLPAVKNGRVYVV 237

                       250
                ....*....|....*..
gi 15829410 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 1.72e-34

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


Pssm-ID: 443650 [Multi-domain]  Cd Length: 316  Bit Score: 127.34  E-value: 1.72e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829410  34 DPNRIVALEWLPVELLLALGIVPYGVADTINYRLWVSEP-PLPESVIDVGLRTEPNLELLTEMKP-----SFMVWSAGYg 107
Cdd:COG4594  51 TPKRVVVLEWSFADALLALGVTPVGIADDNDYDRWVPYLrDLIKGVTSVGTRSQPNLEAIAALKPdliiaDKSRHEAIY- 129

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829410 108 pspEMLARIAPGRGFNFSDGkqPLAMARKSLTEMADLLNLQSAAETHLAQYEDFIRSMNPRFVKRGA-RPLLLTTLIDPr 186
Cdd:COG4594 130 ---DQLSKIAPTVLFKSRNG--DYQENLESFKTIAKALGKEEEAEAVLADHDQRIAEAKAKLAAADKgKKVAVGQFRAD- 203

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829410 187 HMLVFGPNSLFQEILDEYGIPNAW-QGETNFWGSTAVSIDRLAAYkDVDVL-CFDHDNSKDMDALMATPLWQAMPFVRAG 264
Cdd:COG4594 204 GLRLYTPNSFAGSVLAALGFENPPkQSKDNGYGYSEVSLEQLPAL-DPDVLfIATYDDPSILKEWKNNPLWKNLKAVKNG 282

                       250       260       270
                ....*....|....*....|....*....|....
gi 15829410 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 1.08e-29

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: 112.46  E-value: 1.08e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829410    39 VALEWLPVELLLALGIVPYGVADtINYRLWVSEPPLPESVIDVGLRTEPNLELLTEMKPSFMVWSAGYGPSP--EMLARI 116
Cdd:pfam01497   1 AALSPAYTEILYALGATDSIVGV-DAYTRDPLKADAVAAIVKVGAYGEINVERLAALKPDLVILSTGYLTDEaeELLSLI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829410   117 APGRGFNFSDGKQPLamaRKSLTEMADLLNLQSAAETHLAQYEDFIRSMNPRFVKRGARPLLLTTLIDPRHMLVFGPNSL 196
Cdd:pfam01497  80 IPTVIFESSSTGESL---KEQIKQLGELLGLEDEAEELVAEIDSALAAAKKAVPSLTRKPVLVFGGADGGGYVVAGSNTY 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15829410   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: 576.58  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829410    4 LPLISRRRLLTAMALSPLLWQMNTAHAAAIDPNRIVALEWLPVELLLALGIVPYGVADTINYRLWVSEPPLPESVIDVGL 83
Cdd:PRK10576   1 LPDISRRRLLTAMALSPLLWQMNTAAAAAIDPNRIVALEWLPVELLLALGVTPYGVADTHNYRLWVSEPALPDSVIDVGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829410   84 RTEPNLELLTEMKPSFMVWSAGYGPSPEMLARIAPGRGFNFSDGKQPLAMARKSLTEMADLLNLQSAAETHLAQYEDFIR 163
Cdd:PRK10576  81 RTEPNLELLTQMKPSLILWSAGYGPSPEKLARIAPGRGFAFSDGKKPLAVARKSLVELAQRLNLEAAAETHLAQFDDFIA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829410  164 SMNPRFVKRGARPLLLTTLIDPRHMLVFGPNSLFQEILDEYGIPNAWQGETNFWGSTAVSIDRLAAYKDVDVLCFDHDNS 243
Cdd:PRK10576 161 SAKPRLAGRGQRPLLLTSLIDPRHALVFGPNSLFQEVLDELGIENAWQGETNFWGSTVVGIERLAAYKDADVICFDHGNS 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 15829410  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 1.60e-73

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: 226.40  E-value: 1.60e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829410  34 DPNRIVALEWLPVELLLALGIVPYGVADTINYRLWVSEPPLP-ESVIDVGLRTEPNLELLTEMKPSFMVWSAGYGP-SPE 111
Cdd:cd01146   2 KPQRIVALDWGALETLLALGVKPVGVADTAGYKPWIPEPALPlEGVVDVGTRGQPNLEAIAALKPDLILGSASRHDeIYD 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829410 112 MLARIAPGRGFNFSDgkqPLAMARKSLTEMADLLNLQSAAETHLAQYEDFIRSMNPRFVKRGARPLLLTTLIDPRHMLVF 191
Cdd:cd01146  82 QLSQIAPTVLLDSSP---WLAEWKENLRLIAKALGKEEEAEKLLAEYDQRLAELRQKLPDKGPKPVSVVRFSDAGSIRLY 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829410 192 GPNSLFQEILDEYGIPNAW-QGETNFWGSTAVSIDRLAAYkDVDVLCFDHD-NSKDMDALMATPLWQAMPFVRAGRFQRV 269
Cdd:cd01146 159 GPNSFAGSVLEDLGLQNPWaQETTNDSGFATISLERLAKA-DADVLFVFTYeDEELAQALQANPLWQNLPAVKNGRVYVV 237

                       250
                ....*....|....*..
gi 15829410 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 1.72e-34

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


Pssm-ID: 443650 [Multi-domain]  Cd Length: 316  Bit Score: 127.34  E-value: 1.72e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829410  34 DPNRIVALEWLPVELLLALGIVPYGVADTINYRLWVSEP-PLPESVIDVGLRTEPNLELLTEMKP-----SFMVWSAGYg 107
Cdd:COG4594  51 TPKRVVVLEWSFADALLALGVTPVGIADDNDYDRWVPYLrDLIKGVTSVGTRSQPNLEAIAALKPdliiaDKSRHEAIY- 129

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829410 108 pspEMLARIAPGRGFNFSDGkqPLAMARKSLTEMADLLNLQSAAETHLAQYEDFIRSMNPRFVKRGA-RPLLLTTLIDPr 186
Cdd:COG4594 130 ---DQLSKIAPTVLFKSRNG--DYQENLESFKTIAKALGKEEEAEAVLADHDQRIAEAKAKLAAADKgKKVAVGQFRAD- 203

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829410 187 HMLVFGPNSLFQEILDEYGIPNAW-QGETNFWGSTAVSIDRLAAYkDVDVL-CFDHDNSKDMDALMATPLWQAMPFVRAG 264
Cdd:COG4594 204 GLRLYTPNSFAGSVLAALGFENPPkQSKDNGYGYSEVSLEQLPAL-DPDVLfIATYDDPSILKEWKNNPLWKNLKAVKNG 282

                       250       260       270
                ....*....|....*....|....*....|....
gi 15829410 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 1.21e-31

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


Pssm-ID: 440379 [Multi-domain]  Cd Length: 264  Bit Score: 118.18  E-value: 1.21e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829410  37 RIVALEWLPVELLLALGIVPYGVAdtINYRLWVSEPPLP-ESVIDVGLRTEPNLELLTEMKPSFMV--WSAGYGPSPEML 113
Cdd:COG0614   2 RIVSLSPSATELLLALGAGDRLVG--VSDWGYCDYPELElKDLPVVGGTGEPNLEAILALKPDLVLasSSGNDEEDYEQL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829410 114 ARI-APGRGFNFSdgkqPLAMARKSLTEMADLLNLQSAAETHLAQYEDFIRSMNPRFVKRGARPLLLTTLIDPRHMLVFG 192
Cdd:COG0614  80 EKIgIPVVVLDPR----SLEDLYESIRLLGELLGREERAEALIAEYEARLAAVRARLAGAEERPTVLYEIWSGDPLYTAG 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829410 193 PNSLFQEILDEYGIPNAWQGETNFWGStaVSIDRLAAYkDVDVL------CFDHDNSKDMDALMATPLWQAMPFVRAGRF 266
Cdd:COG0614 156 GGSFIGELLELAGGRNVAADLGGGYPE--VSLEQVLAL-DPDVIilsgggYDAETAEEALEALLADPGWQSLPAVKNGRV 232

                       250       260
                ....*....|....*....|....*.
gi 15829410 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 1.08e-29

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: 112.46  E-value: 1.08e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829410    39 VALEWLPVELLLALGIVPYGVADtINYRLWVSEPPLPESVIDVGLRTEPNLELLTEMKPSFMVWSAGYGPSP--EMLARI 116
Cdd:pfam01497   1 AALSPAYTEILYALGATDSIVGV-DAYTRDPLKADAVAAIVKVGAYGEINVERLAALKPDLVILSTGYLTDEaeELLSLI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829410   117 APGRGFNFSDGKQPLamaRKSLTEMADLLNLQSAAETHLAQYEDFIRSMNPRFVKRGARPLLLTTLIDPRHMLVFGPNSL 196
Cdd:pfam01497  80 IPTVIFESSSTGESL---KEQIKQLGELLGLEDEAEELVAEIDSALAAAKKAVPSLTRKPVLVFGGADGGGYVVAGSNTY 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15829410   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 2.02e-14

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: 71.52  E-value: 2.02e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829410  35 PNRIVALEWLPVELLLALGIVPYGVADTINyrlwvseppLPES--------VIDVGLRTEPNLELLTEMKPSFMVWSAGY 106
Cdd:cd01140  12 PEKVVVFDVGALDTLDALGVKVVGVPKSST---------LPEYlkkykddkYANVGTLFEPDLEAIAALKPDLIIIGGRL 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829410 107 GPSPEMLARIAPGRGFnFSDGKQPLAMARKSLTEMADLLNLQSAAETHLAQYEDFIRSMNpRFVKRGARPLLLttLIDPR 186
Cdd:cd01140  83 AEKYDELKKIAPTIDL-GADLKNYLESVKQNIETLGKIFGKEEEAKELVAEIDASIAEAK-SAAKGKKKALVV--LVNGG 158

                       170       180
                ....*....|....*....|...
gi 15829410 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 3.01e-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: 68.74  E-value: 3.01e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829410  37 RIVALEWLPVELLLALG--IVPYGVADTINYRLWVSEPPlpESVIDVGLRTEPNLELLTEMKPSFMVWSAGYGPS-PEML 113
Cdd:cd00636   2 RVVALDPGATELLLALGgdDKPVGVADPSGYPPEAKALL--EKVPDVGHGYEPNLEKIAALKPDLIIANGSGLEAwLDKL 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15829410 114 ARIAPGRGFNFSDGKQPLAMARKSLTEMADLLNLQSAAETHLAQYEDFIRSMNPRFVKRGARPLLL 179
Cdd:cd00636  80 SKIAIPVVVVDEASELSLENIKESIRLIGKALGKEENAEELIAELDARLAELRAKLAKIPKKKVSL 145
FeuA cd01138
Periplasmic binding protein FeuA. These proteins have predicted to function as initial ...
 34-265 1.49e-10

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: 60.04  E-value: 1.49e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829410  34 DPNRIVALEwLPVELLLALGIVPYGVADtinyrlWVSEPPL---PESVIDVGLRTEPNLELLTEMKPSFMVWSAGYGPSP 110
Cdd:cd01138   8 KPKRIVALS-GETEGLALLGIKPVGAAS------IGGKNPYykkKTLAKVVGIVDEPNLEKVLELKPDLIIVSSKQEENY 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829410 111 EMLARIAPGRGFNfSDGKQPlamaRKSLTEMADLLNLQSAAETHLAQYEDFIRSMNPRFVKRGARPLLLTTLIDPRHMLV 190
Cdd:cd01138  81 EKLSKIAPTVPVS-YNSSDW----EEQLKEIGKLLNKEDEAEKWLADYKQKAKEAKEKIKKKLGNDKSVAVLRGRKQIYV 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829410 191 FGPNSLFQEI----LDEYGIPNAWQGETNFWGSTAVSIDRLAAYkDVD-VLCFDHDNSKDMDALMATPLWQAMPFVRAGR 265
Cdd:cd01138 156 FGEDGRGGGPilyaDLGLKAPEKVKEIEDKPGYAAISLEVLPEF-DADyIFLLFFTGPEAKADFESLPIWKNLPAVKNNH 234
fecB PRK11411
iron-dicitrate transporter substrate-binding subunit; Provisional
 10-272 2.99e-07

iron-dicitrate transporter substrate-binding subunit; Provisional


Pssm-ID: 183123 [Multi-domain]  Cd Length: 303  Bit Score: 50.83  E-value: 2.99e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829410   10 RRLLTAMALSpLLWQMNTAHAAAID-------------PNRIVALEWLPVELLLALGIVPYGVADTIN-YRLwvseppLP 75
Cdd:PRK11411   2 LAFIRLLFAG-LLLLSGSSHAFAVTvqdeqgtftlektPQRIVVLELSFVDALAAVGVSPVGVADDNDaKRI------LP 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829410   76 EsVID-------VGLRTEPNLELLTEMKPSFMV-----WSAGYgpspEMLARIAP-----GRGFNFsdgKQPLAMARKsl 138
Cdd:PRK11411  75 E-VRAhlkpwqsVGTRSQPSLEAIAALKPDLIIadssrHAGVY----IALQKIAPtlllkSRNETY---QENLQSAAI-- 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829410  139 teMADLLNLQSAAETHLAQYEDFIRSMNPRFVKrGARPLLLTTLIDprHMLVFGPNSLFQEILDEYGI--PNAWQGETNF 216
Cdd:PRK11411 145 --IGEVLGKKREMQARIEQHKERMAQFASQLPK-GTRVAFGTSREQ--QFNLHSPESYTGSVLAALGLnvPKAPMNGAAM 219

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 15829410  217 wgsTAVSIDRLAAyKDVDVLCFDH--DNSKdMDALMATPLWQAMPFVRAgrfQRVPAV 272
Cdd:PRK11411 220 ---PSISLEQLLA-LNPDWLLVAHyrQESI-VKRWQQDPLWQMLTAAKK---QQVASV 269
CeuA COG4607
ABC-type enterochelin transport system, periplasmic component [Inorganic ion transport and ...
 34-209 3.45e-07

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


Pssm-ID: 443657 [Multi-domain]  Cd Length: 310  Bit Score: 50.56  E-value: 3.45e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829410  34 DPNRIVALEWLPVELLLALGIVPYGVADTInyrlwvseppLP--------ESVIDVGLRTEPNLELLTEMKPSFMVWSAG 105
Cdd:COG4607  50 NPKRVVVFDNGALDTLDALGVEVAGVPKGL----------LPdylskyadDKYANVGTLFEPDLEAIAALKPDLIIIGGR 119

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829410 106 YGPSPEMLARIAP----GRgfnfsDGKQPLAMARKSLTEMADLLNLQSAAETHLAQYEDFIRSMNPRfVKRGARPL-LLT 180
Cdd:COG4607 120 SAKKYDELSKIAPtidlTV-----DGEDYLESLKRNTETLGEIFGKEDEAEELVADLDAKIAALKAA-AAGKGTALiVLT 193

                       170       180
                ....*....|....*....|....*....
gi 15829410 181 TliDPRhMLVFGPNSLFQEILDEYGIPNA 209
Cdd:COG4607 194 N--GGK-ISAYGPGSRFGPIHDVLGFKPA 219
TroA_e cd01142
Periplasmic binding protein TroA_e. These proteins are predicted to function as initial ...
 34-275 1.27e-04

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: 42.73  E-value: 1.27e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829410  34 DPNRIVALEWLPVELLLALGIVPYGVADTinyRLWVSEPPLPES------VIDVGLRTEPNLELLTEMKPSfMVWSAGYg 107
Cdd:cd01142  23 EVKRIAALWGAGNAVVAALGGGKLIVATT---STVQQEPWLYRLapslenVATGGTGNDVNIEELLALKPD-VVIVWST- 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829410 108 PSPEMLARIAPGRGFNFSDgkqplAMARKSLTEMADLLNLQSAAETHLAQYEDFIRSMNPRFVKRGA------RPLLLTT 181
Cdd:cd01142  98 DGKEAGKAVLRLLNALSLR-----DAELEEVKLTIALLGELLGRQEKAEALVAYFDDNLAYVAARTKklpdseRPRVYYA 172

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829410 182 LIDPrhMLVFGPNSLFQEILDEYGIPNAwQGETNFWGSTAVSIDRLAAYkDVDVLCFDHDNSKdmDALMATPLWQAMPFV 261
Cdd:cd01142 173 GPDP--LTTDGTGSITNSWIDLAGGINV-ASEATKKGSGEVSLEQLLKW-NPDVIIVGNADTK--AAILADPRWQNLRAV 246

                       250
                ....*....|....
gi 15829410 262 RAGRFQRVPAVWFY 275
Cdd:cd01142 247 KNGRVYVNPEGAFW 260
YvrC cd01143
Periplasmic binding protein YvrC. These proteins are predicted to function as initial ...
 35-216 1.48e-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: 41.88  E-value: 1.48e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829410  35 PNRIVALewLP--VELLLALG----IVpyGVADTINYrlwvsePPLPESVIDVGLRTEPNLELLTEMKPSFMVWSAGYGP 108
Cdd:cd01143   3 PERIVSL--SPsiTEILFALGagdkIV--GVDTYSNY------PKEVRKKPKVGSYSNPNVEKIVALKPDLVIVSSSSLA 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829410 109 SP-EMLARiapgRGFN--FSDGKQPLAMARKSLTEMADLLNLQSAAEThlaqyedFIRSMNPRFVKRGARPLLLTT---- 181
Cdd:cd01143  73 ELlEKLKD----AGIPvvVLPAASSLDEIYDQIELIGKITGAEEEAEK-------LVKEMKQKIDKVKDKGKTIKKskvy 141

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 15829410 182 -LIDPRHMLVFGPNSLFQEILDEYGIPNAWQGETNF 216
Cdd:cd01143 142 iEVSLGGPYTAGKNTFINELIRLAGAKNIAADSGGW 177
 
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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