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Conserved domains on  [gi|624389466|gb|KBT48303|]
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iron complex transporter substrate-binding protein [Mycobacterium tuberculosis 2233BH]

Protein Classification

TroA family protein( domain architecture ID 513)

TroA family protein; most TroA-like proteins are encoded by ABC-type operons and appear to function as periplasmic components of ABC transporters in metal ion uptake.

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TroA-like super family cl00262
Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function ...
 60-300 4.94e-39

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.


The actual alignment was detected with superfamily member pfam01497:

Pssm-ID: 469696 [Multi-domain]  Cd Length: 233  Bit Score: 137.88  E-value: 4.94e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624389466   60 VSAGYTEQDDLLAVDVVPIAVtdwfGDQPFAVWPWAAPKLggARPAVLNLDNGIQIDRIAALKPDLIVAINAGVDADTYQ 139
Cdd:pfam01497   1 AALSPAYTEILYALGATDSIV----GVDAYTRDPLKADAV--AAIVKVGAYGEINVERLAALKPDLVILSTGYLTDEAEE 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624389466  140 QLSAIAPTVAQsGGDAFFEPWKDQARSIGQAVFAADRMRSLIEAVDQKFAAVAQRHPRWRGKKALLLQGRLWQGNVVATL 219
Cdd:pfam01497  75 LLSLIIPTVIF-ESSSTGESLKEQIKQLGELLGLEDEAEELVAEIDSALAAAKKAVPSLTRKPVLVFGGADGGGYVVAGS 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624389466  220 AGWRTDFLNDMGLVIADSIKPFavDQRGVIPRDHIKAvlDAADVLIWMT---ESPEDEKALLADPEIAASQATAQRRHIF 296
Cdd:pfam01497 154 NTYIGDLLRILGIENIAAELSG--SEYAPISFEAILS--SNPDVIIVSGrdsFTKTGPEFVAANPLWAGLPAVKNGRVYT 229


                  ....
gi 624389466  297 TSKE 300
Cdd:pfam01497 230 LPSD 233
 
Name Accession Description Interval E-value
Peripla_BP_2 pfam01497
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ...
 60-300 4.94e-39

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: 137.88  E-value: 4.94e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624389466   60 VSAGYTEQDDLLAVDVVPIAVtdwfGDQPFAVWPWAAPKLggARPAVLNLDNGIQIDRIAALKPDLIVAINAGVDADTYQ 139
Cdd:pfam01497   1 AALSPAYTEILYALGATDSIV----GVDAYTRDPLKADAV--AAIVKVGAYGEINVERLAALKPDLVILSTGYLTDEAEE 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624389466  140 QLSAIAPTVAQsGGDAFFEPWKDQARSIGQAVFAADRMRSLIEAVDQKFAAVAQRHPRWRGKKALLLQGRLWQGNVVATL 219
Cdd:pfam01497  75 LLSLIIPTVIF-ESSSTGESLKEQIKQLGELLGLEDEAEELVAEIDSALAAAKKAVPSLTRKPVLVFGGADGGGYVVAGS 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624389466  220 AGWRTDFLNDMGLVIADSIKPFavDQRGVIPRDHIKAvlDAADVLIWMT---ESPEDEKALLADPEIAASQATAQRRHIF 296
Cdd:pfam01497 154 NTYIGDLLRILGIENIAAELSG--SEYAPISFEAILS--SNPDVIIVSGrdsFTKTGPEFVAANPLWAGLPAVKNGRVYT 229


                  ....
gi 624389466  297 TSKE 300
Cdd:pfam01497 230 LPSD 233
FhuD cd01146
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial ...
 54-281 7.67e-37

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: 132.79  E-value: 7.67e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624389466  54 EPPKRVVSAGYTEQDDLLAVDVVPIAVTDWFGDQPFAVwpwaAPKLGGARPAVLNLDNGIQIDRIAALKPDLIVAINAGV 133
Cdd:cd01146    1 AKPQRIVALDWGALETLLALGVKPVGVADTAGYKPWIP----EPALPLEGVVDVGTRGQPNLEAIAALKPDLILGSASRH 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624389466 134 DADtYQQLSAIAPTVAQSGGDAFFEpWKDQARSIGQAVFAADRMRSLIEAVDQKFAAVAQRHPRWRGKKALLLQGRLWQG 213
Cdd:cd01146   77 DEI-YDQLSQIAPTVLLDSSPWLAE-WKENLRLIAKALGKEEEAEKLLAEYDQRLAELRQKLPDKGPKPVSVVRFSDAGS 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 624389466 214 NVVATLAGWRTDFLNDMGLVIADSIKPFAVDQRGVIPRDHIkAVLDaADVLIWMTESPED-EKALLADP 281
Cdd:cd01146  155 IRLYGPNSFAGSVLEDLGLQNPWAQETTNDSGFATISLERL-AKAD-ADVLFVFTYEDEElAQALQANP 221
FecB COG4594
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and ...
 1-281 8.43e-30

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


Pssm-ID: 443650 [Multi-domain]  Cd Length: 316  Bit Score: 115.40  E-value: 8.43e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624389466   1 MRQGCSRRGFLqvaeaaAATGLFAGCSSPKPPPGTPGGAA--VTITHLFGQTVIKEPPKRVVSAGYTEQDDLLAVDVVPI 78
Cdd:COG4594    1 MKKLLLLLILL------LALLLLAACGSSSSDSSSSEAAAgaRTVKHAMGETTIPGTPKRVVVLEWSFADALLALGVTPV 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624389466  79 AVTDwfgDQPFAVW-PWAAPKLG-----GARPAVlNLdngiqiDRIAALKPDLIVAiNAGVDADTYQQLSAIAPTVAqsg 152
Cdd:COG4594   75 GIAD---DNDYDRWvPYLRDLIKgvtsvGTRSQP-NL------EAIAALKPDLIIA-DKSRHEAIYDQLSKIAPTVL--- 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624389466 153 GDAFFEPWKD---QARSIGQAVFAADRMRSLIEAVDQKFAAVAQR-HPRWRGKKALLLQG-----RLWQGNvvaTLAGwr 223
Cdd:COG4594  141 FKSRNGDYQEnleSFKTIAKALGKEEEAEAVLADHDQRIAEAKAKlAAADKGKKVAVGQFradglRLYTPN---SFAG-- 215

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 624389466 224 tDFLNDMGLVIAdsIKPFAVDQRGVIPRDhiKAVLDA--ADVLIWMTES-PEDEKALLADP 281
Cdd:COG4594  216 -SVLAALGFENP--PKQSKDNGYGYSEVS--LEQLPAldPDVLFIATYDdPSILKEWKNNP 271
PRK10957 PRK10957
iron-enterobactin transporter periplasmic binding protein; Provisional
 16-194 2.02e-13

iron-enterobactin transporter periplasmic binding protein; Provisional


Pssm-ID: 236806 [Multi-domain]  Cd Length: 317  Bit Score: 69.62  E-value: 2.02e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624389466  16 AAAATGLFAGCSSPKPPPGTPGGaavTITHLFGQTVIKEPPKRVVSAGYTEQDDLLAVDVVPIA---------VTDwfgD 86
Cdd:PRK10957   7 LLLLGLLLSGIAAAQASAAGWPR---TVTDSRGSVTLESKPQRIVSTSVTLTGTLLAIDAPVIAsgattpntrVAD---D 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624389466  87 QPF-AVWPWAAPKLGGARPAVLNLDngiqIDRIAALKPDLIVAINAGVD--ADTYQQLSAIAPTVAQSGGDaffEPWKDQ 163
Cdd:PRK10957  81 QGFfRQWSDVAKERGVEVLYIGEPD----AEAVAAQMPDLIVISATGGDsaLALYDQLSAIAPTLVIDYDD---KSWQEL 153

                        170       180       190
                 ....*....|....*....|....*....|.
gi 624389466 164 ARSIGQAVFAADRMRSLIEAVDQKFAAVAQR 194
Cdd:PRK10957 154 ATQLGEATGLEKQAAAVIAQFDAQLAEVKAK 184
 
Name Accession Description Interval E-value
Peripla_BP_2 pfam01497
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ...
 60-300 4.94e-39

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: 137.88  E-value: 4.94e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624389466   60 VSAGYTEQDDLLAVDVVPIAVtdwfGDQPFAVWPWAAPKLggARPAVLNLDNGIQIDRIAALKPDLIVAINAGVDADTYQ 139
Cdd:pfam01497   1 AALSPAYTEILYALGATDSIV----GVDAYTRDPLKADAV--AAIVKVGAYGEINVERLAALKPDLVILSTGYLTDEAEE 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624389466  140 QLSAIAPTVAQsGGDAFFEPWKDQARSIGQAVFAADRMRSLIEAVDQKFAAVAQRHPRWRGKKALLLQGRLWQGNVVATL 219
Cdd:pfam01497  75 LLSLIIPTVIF-ESSSTGESLKEQIKQLGELLGLEDEAEELVAEIDSALAAAKKAVPSLTRKPVLVFGGADGGGYVVAGS 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624389466  220 AGWRTDFLNDMGLVIADSIKPFavDQRGVIPRDHIKAvlDAADVLIWMT---ESPEDEKALLADPEIAASQATAQRRHIF 296
Cdd:pfam01497 154 NTYIGDLLRILGIENIAAELSG--SEYAPISFEAILS--SNPDVIIVSGrdsFTKTGPEFVAANPLWAGLPAVKNGRVYT 229


                  ....
gi 624389466  297 TSKE 300
Cdd:pfam01497 230 LPSD 233
FhuD cd01146
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial ...
 54-281 7.67e-37

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: 132.79  E-value: 7.67e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624389466  54 EPPKRVVSAGYTEQDDLLAVDVVPIAVTDWFGDQPFAVwpwaAPKLGGARPAVLNLDNGIQIDRIAALKPDLIVAINAGV 133
Cdd:cd01146    1 AKPQRIVALDWGALETLLALGVKPVGVADTAGYKPWIP----EPALPLEGVVDVGTRGQPNLEAIAALKPDLILGSASRH 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624389466 134 DADtYQQLSAIAPTVAQSGGDAFFEpWKDQARSIGQAVFAADRMRSLIEAVDQKFAAVAQRHPRWRGKKALLLQGRLWQG 213
Cdd:cd01146   77 DEI-YDQLSQIAPTVLLDSSPWLAE-WKENLRLIAKALGKEEEAEKLLAEYDQRLAELRQKLPDKGPKPVSVVRFSDAGS 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 624389466 214 NVVATLAGWRTDFLNDMGLVIADSIKPFAVDQRGVIPRDHIkAVLDaADVLIWMTESPED-EKALLADP 281
Cdd:cd01146  155 IRLYGPNSFAGSVLEDLGLQNPWAQETTNDSGFATISLERL-AKAD-ADVLFVFTYEDEElAQALQANP 221
FecB COG4594
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and ...
 1-281 8.43e-30

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


Pssm-ID: 443650 [Multi-domain]  Cd Length: 316  Bit Score: 115.40  E-value: 8.43e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624389466   1 MRQGCSRRGFLqvaeaaAATGLFAGCSSPKPPPGTPGGAA--VTITHLFGQTVIKEPPKRVVSAGYTEQDDLLAVDVVPI 78
Cdd:COG4594    1 MKKLLLLLILL------LALLLLAACGSSSSDSSSSEAAAgaRTVKHAMGETTIPGTPKRVVVLEWSFADALLALGVTPV 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624389466  79 AVTDwfgDQPFAVW-PWAAPKLG-----GARPAVlNLdngiqiDRIAALKPDLIVAiNAGVDADTYQQLSAIAPTVAqsg 152
Cdd:COG4594   75 GIAD---DNDYDRWvPYLRDLIKgvtsvGTRSQP-NL------EAIAALKPDLIIA-DKSRHEAIYDQLSKIAPTVL--- 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624389466 153 GDAFFEPWKD---QARSIGQAVFAADRMRSLIEAVDQKFAAVAQR-HPRWRGKKALLLQG-----RLWQGNvvaTLAGwr 223
Cdd:COG4594  141 FKSRNGDYQEnleSFKTIAKALGKEEEAEAVLADHDQRIAEAKAKlAAADKGKKVAVGQFradglRLYTPN---SFAG-- 215

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 624389466 224 tDFLNDMGLVIAdsIKPFAVDQRGVIPRDhiKAVLDA--ADVLIWMTES-PEDEKALLADP 281
Cdd:COG4594  216 -SVLAALGFENP--PKQSKDNGYGYSEVS--LEQLPAldPDVLFIATYDdPSILKEWKNNP 271
FepB COG0614
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ...
 58-291 1.07e-25

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


Pssm-ID: 440379 [Multi-domain]  Cd Length: 264  Bit Score: 103.15  E-value: 1.07e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624389466  58 RVVSAGYTEQDDLLAVDVVP--IAVTDWfgdqPFAVWPWAA----PKLGGarpavlnlDNGIQIDRIAALKPDLIVAINA 131
Cdd:COG0614    2 RIVSLSPSATELLLALGAGDrlVGVSDW----GYCDYPELElkdlPVVGG--------TGEPNLEAILALKPDLVLASSS 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624389466 132 GVDADTYQQLSAI-APTVAQSGGDafFEPWKDQARSIGQAVFAADRMRSLIEAVDQKFAAVAQRHPRWRGKKALLLQGRL 210
Cdd:COG0614   70 GNDEEDYEQLEKIgIPVVVLDPRS--LEDLYESIRLLGELLGREERAEALIAEYEARLAAVRARLAGAEERPTVLYEIWS 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624389466 211 WQGNVVATLAGWRTDFLNDMGLV-IADSIKPFAVDqrgvIPRDHIkaVLDAADVLIWMTESPEDEKALLADPEIAASQAT 289
Cdd:COG0614  148 GDPLYTAGGGSFIGELLELAGGRnVAADLGGGYPE----VSLEQV--LALDPDVIILSGGGYDAETAEEALEALLADPGW 221


                 ..
gi 624389466 290 AQ 291
Cdd:COG0614  222 QS 223
CeuA COG4607
ABC-type enterochelin transport system, periplasmic component [Inorganic ion transport and ...
 10-206 1.55e-16

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


Pssm-ID: 443657 [Multi-domain]  Cd Length: 310  Bit Score: 78.68  E-value: 1.55e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624389466  10 FLQVAEAAAATGLFAGCSSPKPPPGTPGGAA-VTITHLFGQTVIKEPPKRVVSAGYTEQDDLLAVDVVPIAVtdwfgdqP 88
Cdd:COG4607    4 TLLAALALAAALALAACGSSSAAAASAAAAEtVTVEHALGTVEVPKNPKRVVVFDNGALDTLDALGVEVAGV-------P 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624389466  89 FAVWPWAAPKLggARPAVLNLDNGIQID--RIAALKPDLIvaINAGVDADTYQQLSAIAPTVAQS-GGDAFFEPWKDQAR 165
Cdd:COG4607   77 KGLLPDYLSKY--ADDKYANVGTLFEPDleAIAALKPDLI--IIGGRSAKKYDELSKIAPTIDLTvDGEDYLESLKRNTE 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 624389466 166 SIGQaVFAA-DRMRSLIEAVDQKFAAVAQRHPrwRGKKALLL 206
Cdd:COG4607  153 TLGE-IFGKeDEAEELVADLDAKIAALKAAAA--GKGTALIV 191
TroA-like cd00636
Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function ...
 57-208 4.31e-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: 4.31e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624389466  57 KRVVSAGYTEQDDLLAV--DVVPIAVTDWFGDQPFAVWPWAAPKLGGARpavlnldNGIQIDRIAALKPDLIVAiNAGVD 134
Cdd:cd00636    1 KRVVALDPGATELLLALggDDKPVGVADPSGYPPEAKALLEKVPDVGHG-------YEPNLEKIAALKPDLIIA-NGSGL 72

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 624389466 135 ADTYQQLSAIA-PTVAQS-GGDAFFEPWKDQARSIGQAVFAADRMRSLIEAVDQKFAAVAQRHPRWRGKKALLLQG 208
Cdd:cd00636   73 EAWLDKLSKIAiPVVVVDeASELSLENIKESIRLIGKALGKEENAEELIAELDARLAELRAKLAKIPKKKVSLVVG 148
PRK10957 PRK10957
iron-enterobactin transporter periplasmic binding protein; Provisional
 16-194 2.02e-13

iron-enterobactin transporter periplasmic binding protein; Provisional


Pssm-ID: 236806 [Multi-domain]  Cd Length: 317  Bit Score: 69.62  E-value: 2.02e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624389466  16 AAAATGLFAGCSSPKPPPGTPGGaavTITHLFGQTVIKEPPKRVVSAGYTEQDDLLAVDVVPIA---------VTDwfgD 86
Cdd:PRK10957   7 LLLLGLLLSGIAAAQASAAGWPR---TVTDSRGSVTLESKPQRIVSTSVTLTGTLLAIDAPVIAsgattpntrVAD---D 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624389466  87 QPF-AVWPWAAPKLGGARPAVLNLDngiqIDRIAALKPDLIVAINAGVD--ADTYQQLSAIAPTVAQSGGDaffEPWKDQ 163
Cdd:PRK10957  81 QGFfRQWSDVAKERGVEVLYIGEPD----AEAVAAQMPDLIVISATGGDsaLALYDQLSAIAPTLVIDYDD---KSWQEL 153

                        170       180       190
                 ....*....|....*....|....*....|.
gi 624389466 164 ARSIGQAVFAADRMRSLIEAVDQKFAAVAQR 194
Cdd:PRK10957 154 ATQLGEATGLEKQAAAVIAQFDAQLAEVKAK 184
FeuA cd01138
Periplasmic binding protein FeuA. These proteins have predicted to function as initial ...
 48-191 1.80e-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: 60.43  E-value: 1.80e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624389466  48 GQTVIKEPPKRVVSAGYTEQDDLLaVDVVPIAVTDWFGDQPFAvwpwaapkLGGARPAVLNLDNGIQIDRIAALKPDLIV 127
Cdd:cd01138    1 GEVEIPAKPKRIVALSGETEGLAL-LGIKPVGAASIGGKNPYY--------KKKTLAKVVGIVDEPNLEKVLELKPDLII 71

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 624389466 128 AINAgvDADTYQQLSAIAPTVAQS--GGDaffepWKDQARSIGQAVFAADRMRSLIEAVDQKFAAV 191
Cdd:cd01138   72 VSSK--QEENYEKLSKIAPTVPVSynSSD-----WEEQLKEIGKLLNKEDEAEKWLADYKQKAKEA 130
fecB PRK11411
iron-dicitrate transporter substrate-binding subunit; Provisional
 39-204 6.30e-10

iron-dicitrate transporter substrate-binding subunit; Provisional


Pssm-ID: 183123 [Multi-domain]  Cd Length: 303  Bit Score: 59.30  E-value: 6.30e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624389466  39 AAVTITHLFGQTVIKEPPKRVVSAGYTEQDDLLAVDVVPIAVTDwfGDQPFAVWPWAAPKLG-----GARPAVlnldngi 113
Cdd:PRK11411  22 FAVTVQDEQGTFTLEKTPQRIVVLELSFVDALAAVGVSPVGVAD--DNDAKRILPEVRAHLKpwqsvGTRSQP------- 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624389466 114 QIDRIAALKPDLIVAiNAGVDADTYQQLSAIAPTVA-QSGGDAFFEPWkDQARSIGQAVFAADRMRSLIEAVDQKFAAVA 192
Cdd:PRK11411  93 SLEAIAALKPDLIIA-DSSRHAGVYIALQKIAPTLLlKSRNETYQENL-QSAAIIGEVLGKKREMQARIEQHKERMAQFA 170

                        170
                 ....*....|..
gi 624389466 193 QRHPrwRGKKAL 204
Cdd:PRK11411 171 SQLP--KGTRVA 180
YvrC cd01143
Periplasmic binding protein YvrC. These proteins are predicted to function as initial ...
 54-242 6.88e-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: 48.81  E-value: 6.88e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624389466  54 EPPKRVVS--AGYTE-------QDDLLAVDvvpiavtdwfgdqPFAVWPWAAPKLggarPAVLNLDNgIQIDRIAALKPD 124
Cdd:cd01143    1 KEPERIVSlsPSITEilfalgaGDKIVGVD-------------TYSNYPKEVRKK----PKVGSYSN-PNVEKIVALKPD 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624389466 125 LIVAInAGVDADTYQQLSAIAPTVAQSGGDAFFEPWKDQARSIGQAVFAADRMRSLIEAVDQKFAAVAQRHPRWRGKKAL 204
Cdd:cd01143   63 LVIVS-SSSLAELLEKLKDAGIPVVVLPAASSLDEIYDQIELIGKITGAEEEAEKLVKEMKQKIDKVKDKGKTIKKSKVY 141

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 624389466 205 LL--QGRLWQgnvvatlAGWRTdFLNDMgLVIADSIKPFA 242
Cdd:cd01143  142 IEvsLGGPYT-------AGKNT-FINEL-IRLAGAKNIAA 172
ChuT COG4558
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism] ...
 48-295 1.53e-06

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


Pssm-ID: 443619 [Multi-domain]  Cd Length: 285  Bit Score: 49.03  E-value: 1.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624389466  48 GQTVIKEPPKRVVSAG--YTE-------QDDLLAVDVvpiavtdwfgdqpFAVWPWAA---PKLGGARpavlnldnGIQI 115
Cdd:COG4558   19 GASVAAAAAERIVSLGgsVTEivyalgaGDRLVGVDT-------------TSTYPAAAkalPDVGYMR--------QLSA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624389466 116 DRIAALKPDLIVAINAGVDADTYQQLSAIAPTVAQSGGDAFFEPWKDQARSIGQAVFAADRMRSLIEAVDQKFAAVAQRH 195
Cdd:COG4558   78 EGILSLKPTLVLASEGAGPPEVLDQLRAAGVPVVVVPAAPSLEGVLAKIRAVAAALGVPEAGEALAARLEADLAALAARV 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624389466 196 PRW-RGKKALLLQGRlwqGNVVATLAGWRT---DFLNDMGLV-IADSIKPF-AVDQRGViprdhIKAvldAADVLIWMT- 268
Cdd:COG4558  158 AAIgKPPRVLFLLSR---GGGRPMVAGRGTaadALIRLAGGVnAAAGFEGYkPLSAEAL-----IAA---APDVILVMTr 226

                        250       260
                 ....*....|....*....|....*....
gi 624389466 269 --ESPEDEKALLADPEIAASQATAQRRHI 295
Cdd:COG4558  227 glESLGGVDGLLALPGLAQTPAGKNKRIV 255
FatB cd01140
Siderophore binding protein FatB. These proteins have been shown to function as ABC-type ...
 45-191 1.83e-06

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: 48.41  E-value: 1.83e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624389466  45 HLFGQTVIKEPPKRVVSAGYTEQDDLLAVDVVPIAVTDwFGDQPFAVwpwaaPKLGGARPAVLNLDNGIQIDRIAALKPD 124
Cdd:cd01140    1 HALGETKVPKNPEKVVVFDVGALDTLDALGVKVVGVPK-SSTLPEYL-----KKYKDDKYANVGTLFEPDLEAIAALKPD 74

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 624389466 125 LIvaINAGVDADTYQQLSAIAPTVAQS-GGDAFFEPWKDQARSIGQAVFAADRMRSLIEAVDQKFAAV 191
Cdd:cd01140   75 LI--IIGGRLAEKYDELKKIAPTIDLGaDLKNYLESVKQNIETLGKIFGKEEEAKELVAEIDASIAEA 140
TroA_e cd01142
Periplasmic binding protein TroA_e. These proteins are predicted to function as initial ...
 39-194 2.68e-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: 45.04  E-value: 2.68e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624389466  39 AAVTITHLFGQTV-IKEPPKRVVSAGYTEQDDLLAVDVVPIAVTDWFGDQPFAVWPWAAPKLGGArpAVLNLDNGIQIDR 117
Cdd:cd01142    6 ATRTITDMAGRKVtIPDEVKRIAALWGAGNAVVAALGGGKLIVATTSTVQQEPWLYRLAPSLENV--ATGGTGNDVNIEE 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 624389466 118 IAALKPDLIVAINAGVDaDTYQQLSAIAPTVAQSggDAFFEPWKDQARSIGQAVFAADRMRSLIEAVDQKFAAVAQR 194
Cdd:cd01142   84 LLALKPDVVIVWSTDGK-EAGKAVLRLLNALSLR--DAELEEVKLTIALLGELLGRQEKAEALVAYFDDNLAYVAAR 157
BtuF cd01144
Cobalamin binding protein BtuF. These proteins have been shown to function as initial ...
 78-226 7.04e-05

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: 43.44  E-value: 7.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624389466  78 IAVTDWfgdqpfAVWPWAAPKLggarPAVLNlDNGIQIDRIAALKPDLIVAINAGVDADTYQQLSAIAPTVAQSGGDAFF 157
Cdd:cd01144   24 VGVTDY------CDYPPEAKKL----PRVGG-FYQLDLERVLALKPDLVIAWDDCNVCAVVDQLRAAGIPVLVSEPQTLD 92

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 624389466 158 EPWKDQARsIGQAVFAADRMRSLIEAVDQKFAAVAQRHPRWRGKKALLLQ--------GRLWQGNVVAtLAGWRTDF 226
Cdd:cd01144   93 DILADIRR-LGTLAGRPARAEELAEALRRRLAALRKQYASKPPPRVFYQEwidplmtaGGDWVPELIA-LAGGVNVF 167
TroA_d cd01141
Periplasmic binding protein TroA_d. These proteins are predicted to function as initial ...
 51-197 4.35e-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: 37.79  E-value: 4.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624389466  51 VIKEPPKRVVSAGYTEQDDLLAVDVVP--IAVTDWFGDqpfavwpWAAPKLGGARPAVLNLDNGIQIDRIAALKPDLIV- 127
Cdd:cd01141    3 TIKVPPKRIVVLSPTHVDLLLALDKADkiVGVSASAYD-------LNTPAVKERIDIQVGPTGSLNVELIVALKPDLVIl 75

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 624389466 128 -AINAGVDA-DTYQQLSAIAPTVAQSGgdaffEPWKD----QARSIGQAVFAADRMRSLIEAVDQKFAAVAQRHPR 197
Cdd:cd01141   76 yGGFQAQTIlDKLEQLGIPVLYVNEYP-----SPLGRaewiKFAAAFYGVGKEDKADEAFAQIAGRYRDLAKKVSN 146
HutB cd01149
Hemin binding protein HutB. These proteins have been shown to function as initial receptors ...
 56-293 4.68e-03

Hemin binding protein HutB. These proteins have been shown to function as initial receptors in ABC transport of hemin and hemoproteins in many eubacterial species. They belong to the TroA superfamily of periplasmic metal binding proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind the metal ion in the cleft between these domains.


Pssm-ID: 238569 [Multi-domain]  Cd Length: 235  Bit Score: 38.02  E-value: 4.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624389466  56 PKRVVSAG--YTE-------QDDLLAVDVVpiavtdwfgdqpfAVWPWAAPKLggarPAV-----LNLDNgiqidrIAAL 121
Cdd:cd01149    1 PERIVSLGgsVTEivyalgaGDRLVGVDST-------------STYPEAAAKL----PDVgymrqLSAEG------VLSL 57

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624389466 122 KPDLIVAINAGVDADTYQQLSAIAPTVAQSGGDAFFEPWKDQARSIGQAVFAADRMRSLIEAVDQKFAAVAQRHPRW-RG 200
Cdd:cd01149   58 KPTLVIASDEAGPPEALDQLRAAGVPVVTVPSTPTLDGLLTKIRQVAQALGVPEKGEALAQEVRQRLAALRKTVAAHkKP 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624389466 201 KKALLLqgrLWQGNVVATLAGWRTD---FLNDMGLV-IADSIKPF-AVDQRGVIprdhikavlDAADVLIWMT----ESP 271
Cdd:cd01149  138 PRVLFL---LSHGGGAAMAAGRNTAadaIIALAGAVnAAAGFRGYkPLSAEALI---------AAQPDVILVMsrglDAV 205

                        250       260
                 ....*....|....*....|..
gi 624389466 272 EDEKALLADPEIAASQATAQRR 293
Cdd:cd01149  206 GGVDGLLKLPGLAQTPAGRNKR 227
 
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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