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Conserved domains on  [gi|942536340|ref|WP_055349110|]
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ABC transporter substrate-binding protein [Mycobacterium tuberculosis]

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 ...
 59-300 1.67e-38

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: 136.34  E-value: 1.67e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942536340   59 VVGAGYTEqdDLLAVDVVPIAVtdwfGDQPFAVWPWAAPKLggARPAVLNLDNGIQIDRIAALKPDLIVAINAGVDADTY 138
Cdd:pfam01497   2 ALSPAYTE--ILYALGATDSIV----GVDAYTRDPLKADAV--AAIVKVGAYGEINVERLAALKPDLVILSTGYLTDEAE 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942536340  139 QQLSAIAPTVAQsGGDAFFEPWKDQARSIGQAVFAADRMRSLIEAVDQKFAAVAQRHPRWRGKKALLLQGRLWQGNVVAT 218
Cdd:pfam01497  74 ELLSLIIPTVIF-ESSSTGESLKEQIKQLGELLGLEDEAEELVAEIDSALAAAKKAVPSLTRKPVLVFGGADGGGYVVAG 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942536340  219 LAGWRTDFLNDMGLVIADSIKPFavDQRGVIPRDHIKAvlDAADVLIWMT---ESPEDEKALLADPEIAASQATAQRRHI 295
Cdd:pfam01497 153 SNTYIGDLLRILGIENIAAELSG--SEYAPISFEAILS--SNPDVIIVSGrdsFTKTGPEFVAANPLWAGLPAVKNGRVY 228


                  ....*
gi 942536340  296 FTSKE 300
Cdd:pfam01497 229 TLPSD 233
 
Name Accession Description Interval E-value
Peripla_BP_2 pfam01497
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ...
 59-300 1.67e-38

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: 136.34  E-value: 1.67e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942536340   59 VVGAGYTEqdDLLAVDVVPIAVtdwfGDQPFAVWPWAAPKLggARPAVLNLDNGIQIDRIAALKPDLIVAINAGVDADTY 138
Cdd:pfam01497   2 ALSPAYTE--ILYALGATDSIV----GVDAYTRDPLKADAV--AAIVKVGAYGEINVERLAALKPDLVILSTGYLTDEAE 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942536340  139 QQLSAIAPTVAQsGGDAFFEPWKDQARSIGQAVFAADRMRSLIEAVDQKFAAVAQRHPRWRGKKALLLQGRLWQGNVVAT 218
Cdd:pfam01497  74 ELLSLIIPTVIF-ESSSTGESLKEQIKQLGELLGLEDEAEELVAEIDSALAAAKKAVPSLTRKPVLVFGGADGGGYVVAG 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942536340  219 LAGWRTDFLNDMGLVIADSIKPFavDQRGVIPRDHIKAvlDAADVLIWMT---ESPEDEKALLADPEIAASQATAQRRHI 295
Cdd:pfam01497 153 SNTYIGDLLRILGIENIAAELSG--SEYAPISFEAILS--SNPDVIIVSGrdsFTKTGPEFVAANPLWAGLPAVKNGRVY 228


                  ....*
gi 942536340  296 FTSKE 300
Cdd:pfam01497 229 TLPSD 233
FhuD cd01146
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial ...
 54-281 8.39e-36

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: 130.10  E-value: 8.39e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942536340  54 EPPKRVVGAGYTEQDDLLAVDVVPIAVTDWFGDQPFAVwpwaAPKLGGARPAVLNLDNGIQIDRIAALKPDLIVAINAGV 133
Cdd:cd01146    1 AKPQRIVALDWGALETLLALGVKPVGVADTAGYKPWIP----EPALPLEGVVDVGTRGQPNLEAIAALKPDLILGSASRH 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942536340 134 DADtYQQLSAIAPTVAQSGGDAFFEpWKDQARSIGQAVFAADRMRSLIEAVDQKFAAVAQRHPRWRGKKALLLQGRLWQG 213
Cdd:cd01146   77 DEI-YDQLSQIAPTVLLDSSPWLAE-WKENLRLIAKALGKEEEAEKLLAEYDQRLAELRQKLPDKGPKPVSVVRFSDAGS 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 942536340 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 3.67e-29

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


Pssm-ID: 443650 [Multi-domain]  Cd Length: 316  Bit Score: 113.86  E-value: 3.67e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942536340   1 MRQGCSRRGFLqvaeaaAATGLFAGCSSPKPPPGTPGGAA--VTITHLFGQTVIKEPPKRVVGAGYTEQDDLLAVDVVPI 78
Cdd:COG4594    1 MKKLLLLLILL------LALLLLAACGSSSSDSSSSEAAAgaRTVKHAMGETTIPGTPKRVVVLEWSFADALLALGVTPV 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942536340  79 AVTDwfgDQPFAVW-PWAAPKLG-----GARPAVlNLdngiqiDRIAALKPDLIVAiNAGVDADTYQQLSAIAPTVAqsg 152
Cdd:COG4594   75 GIAD---DNDYDRWvPYLRDLIKgvtsvGTRSQP-NL------EAIAALKPDLIIA-DKSRHEAIYDQLSKIAPTVL--- 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942536340 153 GDAFFEPWKD---QARSIGQAVFAADRMRSLIEAVDQKFAAVAQR-HPRWRGKKALLLQG-----RLWQGNvvaTLAGwr 223
Cdd:COG4594  141 FKSRNGDYQEnleSFKTIAKALGKEEEAEAVLADHDQRIAEAKAKlAAADKGKKVAVGQFradglRLYTPN---SFAG-- 215

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 942536340 224 tDFLNDMGLVIAdsIKPFAVDQRGVIPRDhiKAVLDA--ADVLIWMTES-PEDEKALLADP 281
Cdd:COG4594  216 -SVLAALGFENP--PKQSKDNGYGYSEVS--LEQLPAldPDVLFIATYDdPSILKEWKNNP 271
PRK10957 PRK10957
iron-enterobactin transporter periplasmic binding protein; Provisional
 16-194 2.50e-12

iron-enterobactin transporter periplasmic binding protein; Provisional


Pssm-ID: 236806 [Multi-domain]  Cd Length: 317  Bit Score: 66.54  E-value: 2.50e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942536340  16 AAAATGLFAGCSSPKPPPGTPGGaavTITHLFGQTVIKEPPKRVVGAGYTEQDDLLAVDVVPIA---------VTDwfgD 86
Cdd:PRK10957   7 LLLLGLLLSGIAAAQASAAGWPR---TVTDSRGSVTLESKPQRIVSTSVTLTGTLLAIDAPVIAsgattpntrVAD---D 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942536340  87 QPF-AVWPWAAPKLGGARPAVLNLDngiqIDRIAALKPDLIVAINAGVD--ADTYQQLSAIAPTVAQSGGDaffEPWKDQ 163
Cdd:PRK10957  81 QGFfRQWSDVAKERGVEVLYIGEPD----AEAVAAQMPDLIVISATGGDsaLALYDQLSAIAPTLVIDYDD---KSWQEL 153

                        170       180       190
                 ....*....|....*....|....*....|.
gi 942536340 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 ...
 59-300 1.67e-38

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: 136.34  E-value: 1.67e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942536340   59 VVGAGYTEqdDLLAVDVVPIAVtdwfGDQPFAVWPWAAPKLggARPAVLNLDNGIQIDRIAALKPDLIVAINAGVDADTY 138
Cdd:pfam01497   2 ALSPAYTE--ILYALGATDSIV----GVDAYTRDPLKADAV--AAIVKVGAYGEINVERLAALKPDLVILSTGYLTDEAE 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942536340  139 QQLSAIAPTVAQsGGDAFFEPWKDQARSIGQAVFAADRMRSLIEAVDQKFAAVAQRHPRWRGKKALLLQGRLWQGNVVAT 218
Cdd:pfam01497  74 ELLSLIIPTVIF-ESSSTGESLKEQIKQLGELLGLEDEAEELVAEIDSALAAAKKAVPSLTRKPVLVFGGADGGGYVVAG 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942536340  219 LAGWRTDFLNDMGLVIADSIKPFavDQRGVIPRDHIKAvlDAADVLIWMT---ESPEDEKALLADPEIAASQATAQRRHI 295
Cdd:pfam01497 153 SNTYIGDLLRILGIENIAAELSG--SEYAPISFEAILS--SNPDVIIVSGrdsFTKTGPEFVAANPLWAGLPAVKNGRVY 228


                  ....*
gi 942536340  296 FTSKE 300
Cdd:pfam01497 229 TLPSD 233
FhuD cd01146
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial ...
 54-281 8.39e-36

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: 130.10  E-value: 8.39e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942536340  54 EPPKRVVGAGYTEQDDLLAVDVVPIAVTDWFGDQPFAVwpwaAPKLGGARPAVLNLDNGIQIDRIAALKPDLIVAINAGV 133
Cdd:cd01146    1 AKPQRIVALDWGALETLLALGVKPVGVADTAGYKPWIP----EPALPLEGVVDVGTRGQPNLEAIAALKPDLILGSASRH 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942536340 134 DADtYQQLSAIAPTVAQSGGDAFFEpWKDQARSIGQAVFAADRMRSLIEAVDQKFAAVAQRHPRWRGKKALLLQGRLWQG 213
Cdd:cd01146   77 DEI-YDQLSQIAPTVLLDSSPWLAE-WKENLRLIAKALGKEEEAEKLLAEYDQRLAELRQKLPDKGPKPVSVVRFSDAGS 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 942536340 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 3.67e-29

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


Pssm-ID: 443650 [Multi-domain]  Cd Length: 316  Bit Score: 113.86  E-value: 3.67e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942536340   1 MRQGCSRRGFLqvaeaaAATGLFAGCSSPKPPPGTPGGAA--VTITHLFGQTVIKEPPKRVVGAGYTEQDDLLAVDVVPI 78
Cdd:COG4594    1 MKKLLLLLILL------LALLLLAACGSSSSDSSSSEAAAgaRTVKHAMGETTIPGTPKRVVVLEWSFADALLALGVTPV 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942536340  79 AVTDwfgDQPFAVW-PWAAPKLG-----GARPAVlNLdngiqiDRIAALKPDLIVAiNAGVDADTYQQLSAIAPTVAqsg 152
Cdd:COG4594   75 GIAD---DNDYDRWvPYLRDLIKgvtsvGTRSQP-NL------EAIAALKPDLIIA-DKSRHEAIYDQLSKIAPTVL--- 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942536340 153 GDAFFEPWKD---QARSIGQAVFAADRMRSLIEAVDQKFAAVAQR-HPRWRGKKALLLQG-----RLWQGNvvaTLAGwr 223
Cdd:COG4594  141 FKSRNGDYQEnleSFKTIAKALGKEEEAEAVLADHDQRIAEAKAKlAAADKGKKVAVGQFradglRLYTPN---SFAG-- 215

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 942536340 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 1.49e-24

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


Pssm-ID: 440379 [Multi-domain]  Cd Length: 264  Bit Score: 100.07  E-value: 1.49e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942536340  58 RVVGAGYTEQDDLLAVDVVP--IAVTDWfgdqPFAVWPWAA----PKLGGarpavlnlDNGIQIDRIAALKPDLIVAINA 131
Cdd:COG0614    2 RIVSLSPSATELLLALGAGDrlVGVSDW----GYCDYPELElkdlPVVGG--------TGEPNLEAILALKPDLVLASSS 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942536340 132 GVDADTYQQLSAI-APTVAQSGGDafFEPWKDQARSIGQAVFAADRMRSLIEAVDQKFAAVAQRHPRWRGKKALLLQGRL 210
Cdd:COG0614   70 GNDEEDYEQLEKIgIPVVVLDPRS--LEDLYESIRLLGELLGREERAEALIAEYEARLAAVRARLAGAEERPTVLYEIWS 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942536340 211 WQGNVVATLAGWRTDFLNDMGLV-IADSIKPFAVDqrgvIPRDHIkaVLDAADVLIWMTESPEDEKALLADPEIAASQAT 289
Cdd:COG0614  148 GDPLYTAGGGSFIGELLELAGGRnVAADLGGGYPE----VSLEQV--LALDPDVIILSGGGYDAETAEEALEALLADPGW 221


                 ..
gi 942536340 290 AQ 291
Cdd:COG0614  222 QS 223
CeuA COG4607
ABC-type enterochelin transport system, periplasmic component [Inorganic ion transport and ...
 10-206 4.93e-16

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


Pssm-ID: 443657 [Multi-domain]  Cd Length: 310  Bit Score: 77.14  E-value: 4.93e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942536340  10 FLQVAEAAAATGLFAGCSSPKPPPGTPGGAA-VTITHLFGQTVIKEPPKRVVGAGYTEQDDLLAVDVVPIAVtdwfgdqP 88
Cdd:COG4607    4 TLLAALALAAALALAACGSSSAAAASAAAAEtVTVEHALGTVEVPKNPKRVVVFDNGALDTLDALGVEVAGV-------P 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942536340  89 FAVWPWAAPKLggARPAVLNLDNGIQID--RIAALKPDLIvaINAGVDADTYQQLSAIAPTVAQS-GGDAFFEPWKDQAR 165
Cdd:COG4607   77 KGLLPDYLSKY--ADDKYANVGTLFEPDleAIAALKPDLI--IIGGRSAKKYDELSKIAPTIDLTvDGEDYLESLKRNTE 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 942536340 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 3.56e-13

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: 66.04  E-value: 3.56e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942536340  57 KRVV--GAGYTEQDDLLAVDVVPIAVTDWFGDQPFAVWPWAAPKLGGARpavlnldNGIQIDRIAALKPDLIVAiNAGVD 134
Cdd:cd00636    1 KRVValDPGATELLLALGGDDKPVGVADPSGYPPEAKALLEKVPDVGHG-------YEPNLEKIAALKPDLIIA-NGSGL 72

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 942536340 135 ADTYQQLSAIA-PTVAQS-GGDAFFEPWKDQARSIGQAVFAADRMRSLIEAVDQKFAAVAQRHPRWRGKKALLLQG 208
Cdd:cd00636   73 EAWLDKLSKIAiPVVVVDeASELSLENIKESIRLIGKALGKEENAEELIAELDARLAELRAKLAKIPKKKVSLVVG 148
PRK10957 PRK10957
iron-enterobactin transporter periplasmic binding protein; Provisional
 16-194 2.50e-12

iron-enterobactin transporter periplasmic binding protein; Provisional


Pssm-ID: 236806 [Multi-domain]  Cd Length: 317  Bit Score: 66.54  E-value: 2.50e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942536340  16 AAAATGLFAGCSSPKPPPGTPGGaavTITHLFGQTVIKEPPKRVVGAGYTEQDDLLAVDVVPIA---------VTDwfgD 86
Cdd:PRK10957   7 LLLLGLLLSGIAAAQASAAGWPR---TVTDSRGSVTLESKPQRIVSTSVTLTGTLLAIDAPVIAsgattpntrVAD---D 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942536340  87 QPF-AVWPWAAPKLGGARPAVLNLDngiqIDRIAALKPDLIVAINAGVD--ADTYQQLSAIAPTVAQSGGDaffEPWKDQ 163
Cdd:PRK10957  81 QGFfRQWSDVAKERGVEVLYIGEPD----AEAVAAQMPDLIVISATGGDsaLALYDQLSAIAPTLVIDYDD---KSWQEL 153

                        170       180       190
                 ....*....|....*....|....*....|.
gi 942536340 164 ARSIGQAVFAADRMRSLIEAVDQKFAAVAQR 194
Cdd:PRK10957 154 ATQLGEATGLEKQAAAVIAQFDAQLAEVKAK 184
FeuA cd01138
Periplasmic binding protein FeuA. These proteins have predicted to function as initial ...
 48-191 4.97e-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: 58.88  E-value: 4.97e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942536340  48 GQTVIKEPPKRVVGAGYTEQDDLLaVDVVPIAVTDWFGDQPFAvwpwaapkLGGARPAVLNLDNGIQIDRIAALKPDLIV 127
Cdd:cd01138    1 GEVEIPAKPKRIVALSGETEGLAL-LGIKPVGAASIGGKNPYY--------KKKTLAKVVGIVDEPNLEKVLELKPDLII 71

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 942536340 128 AINAgvDADTYQQLSAIAPTVAQS--GGDaffepWKDQARSIGQAVFAADRMRSLIEAVDQKFAAV 191
Cdd:cd01138   72 VSSK--QEENYEKLSKIAPTVPVSynSSD-----WEEQLKEIGKLLNKEDEAEKWLADYKQKAKEA 130
fecB PRK11411
iron-dicitrate transporter substrate-binding subunit; Provisional
 39-204 7.93e-10

iron-dicitrate transporter substrate-binding subunit; Provisional


Pssm-ID: 183123 [Multi-domain]  Cd Length: 303  Bit Score: 58.92  E-value: 7.93e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942536340  39 AAVTITHLFGQTVIKEPPKRVVGAGYTEQDDLLAVDVVPIAVTDwfGDQPFAVWPWAAPKLG-----GARPAVlnldngi 113
Cdd:PRK11411  22 FAVTVQDEQGTFTLEKTPQRIVVLELSFVDALAAVGVSPVGVAD--DNDAKRILPEVRAHLKpwqsvGTRSQP------- 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942536340 114 QIDRIAALKPDLIVAiNAGVDADTYQQLSAIAPTVA-QSGGDAFFEPWkDQARSIGQAVFAADRMRSLIEAVDQKFAAVA 192
Cdd:PRK11411  93 SLEAIAALKPDLIIA-DSSRHAGVYIALQKIAPTLLlKSRNETYQENL-QSAAIIGEVLGKKREMQARIEQHKERMAQFA 170

                        170
                 ....*....|..
gi 942536340 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 1.32e-06

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: 48.04  E-value: 1.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942536340  54 EPPKRVV-------------GAGyteqDDLLAVDvvpiavtdwfgdqPFAVWPWAAPKLggarPAVLNLDNgIQIDRIAA 120
Cdd:cd01143    1 KEPERIVslspsiteilfalGAG----DKIVGVD-------------TYSNYPKEVRKK----PKVGSYSN-PNVEKIVA 58

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942536340 121 LKPDLIVAInAGVDADTYQQLSAIAPTVAQSGGDAFFEPWKDQARSIGQAVFAADRMRSLIEAVDQKFAAVAQRHPRWRG 200
Cdd:cd01143   59 LKPDLVIVS-SSSLAELLEKLKDAGIPVVVLPAASSLDEIYDQIELIGKITGAEEEAEKLVKEMKQKIDKVKDKGKTIKK 137

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 942536340 201 KKALLL--QGRLWQgnvvatlAGWRTdFLNDMgLVIADSIKPFA 242
Cdd:cd01143  138 SKVYIEvsLGGPYT-------AGKNT-FINEL-IRLAGAKNIAA 172
FatB cd01140
Siderophore binding protein FatB. These proteins have been shown to function as ABC-type ...
 45-191 1.77e-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: 1.77e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942536340  45 HLFGQTVIKEPPKRVVGAGYTEQDDLLAVDVVPIAVTDwFGDQPFAVwpwaaPKLGGARPAVLNLDNGIQIDRIAALKPD 124
Cdd:cd01140    1 HALGETKVPKNPEKVVVFDVGALDTLDALGVKVVGVPK-SSTLPEYL-----KKYKDDKYANVGTLFEPDLEAIAALKPD 74

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 942536340 125 LIvaINAGVDADTYQQLSAIAPTVAQS-GGDAFFEPWKDQARSIGQAVFAADRMRSLIEAVDQKFAAV 191
Cdd:cd01140   75 LI--IIGGRLAEKYDELKKIAPTIDLGaDLKNYLESVKQNIETLGKIFGKEEEAKELVAEIDASIAEA 140
ChuT COG4558
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism] ...
 48-295 1.25e-05

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


Pssm-ID: 443619 [Multi-domain]  Cd Length: 285  Bit Score: 45.95  E-value: 1.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942536340  48 GQTVIKEPPKRVV--GAGYTE-------QDDLLAVDVvpiavtdwfgdqpFAVWPWAA---PKLGGARpavlnldnGIQI 115
Cdd:COG4558   19 GASVAAAAAERIVslGGSVTEivyalgaGDRLVGVDT-------------TSTYPAAAkalPDVGYMR--------QLSA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942536340 116 DRIAALKPDLIVAINAGVDADTYQQLSAIAPTVAQSGGDAFFEPWKDQARSIGQAVFAADRMRSLIEAVDQKFAAVAQRH 195
Cdd:COG4558   78 EGILSLKPTLVLASEGAGPPEVLDQLRAAGVPVVVVPAAPSLEGVLAKIRAVAAALGVPEAGEALAARLEADLAALAARV 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942536340 196 PRW-RGKKALLLQGRlwqGNVVATLAGWRT---DFLNDMGLV-IADSIKPF-AVDQRGViprdhIKAvldAADVLIWMT- 268
Cdd:COG4558  158 AAIgKPPRVLFLLSR---GGGRPMVAGRGTaadALIRLAGGVnAAAGFEGYkPLSAEAL-----IAA---APDVILVMTr 226

                        250       260
                 ....*....|....*....|....*....
gi 942536340 269 --ESPEDEKALLADPEIAASQATAQRRHI 295
Cdd:COG4558  227 glESLGGVDGLLALPGLAQTPAGKNKRIV 255
BtuF cd01144
Cobalamin binding protein BtuF. These proteins have been shown to function as initial ...
 78-226 6.91e-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: 6.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942536340  78 IAVTDWfgdqpfAVWPWAAPKLggarPAVLNlDNGIQIDRIAALKPDLIVAINAGVDADTYQQLSAIAPTVAQSGGDAFF 157
Cdd:cd01144   24 VGVTDY------CDYPPEAKKL----PRVGG-FYQLDLERVLALKPDLVIAWDDCNVCAVVDQLRAAGIPVLVSEPQTLD 92

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 942536340 158 EPWKDQARsIGQAVFAADRMRSLIEAVDQKFAAVAQRHPRWRGKKALLLQ--------GRLWQGNVVAtLAGWRTDF 226
Cdd:cd01144   93 DILADIRR-LGTLAGRPARAEELAEALRRRLAALRKQYASKPPPRVFYQEwidplmtaGGDWVPELIA-LAGGVNVF 167
TroA_e cd01142
Periplasmic binding protein TroA_e. These proteins are predicted to function as initial ...
 39-194 1.17e-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: 43.11  E-value: 1.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 942536340  39 AAVTITHLFGQTV-IKEPPKRVVGAGYTEQDDLLAVDVVPIAVTDWFGDQPFAVWPWAAPKLGGArpAVLNLDNGIQIDR 117
Cdd:cd01142    6 ATRTITDMAGRKVtIPDEVKRIAALWGAGNAVVAALGGGKLIVATTSTVQQEPWLYRLAPSLENV--ATGGTGNDVNIEE 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 942536340 118 IAALKPDLIVAINAGVDaDTYQQLSAIAPTVAQSggDAFFEPWKDQARSIGQAVFAADRMRSLIEAVDQKFAAVAQR 194
Cdd:cd01142   84 LLALKPDVVIVWSTDGK-EAGKAVLRLLNALSLR--DAELEEVKLTIALLGELLGRQEKAEALVAYFDDNLAYVAAR 157
 
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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