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Conserved domains on  [gi|496082725|ref|WP_008807232|]
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MULTISPECIES: DsbA family protein [Klebsiella]

Protein Classification

DsbA family protein( domain architecture ID 16062126)

DsbA family protein such as Proteus mirabilis suppressor of copper sensitivity protein C ScaC (PmScsC), a homotrimeric disulfide isomerase that plays a role in copper tolerance

CATH:  3.40.30.10
Gene Ontology:  GO:0015036
PubMed:  9099998|10049365|15558583|12524212|12074972|30367780
SCOP:  3000031

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DsbA_Com1_like cd03023
DsbA family, Com1-like subfamily; composed of proteins similar to Com1, a 27-kDa outer ...
 94-257 2.38e-51

DsbA family, Com1-like subfamily; composed of proteins similar to Com1, a 27-kDa outer membrane-associated immunoreactive protein originally found in both acute and chronic disease strains of the pathogenic bacteria Coxiella burnetti. It contains a CXXC motif, assumed to be imbedded in a DsbA-like structure. Its homology to DsbA suggests that the protein is a protein disulfide oxidoreductase. The role of such a protein in pathogenesis is unknown.


:

Pssm-ID: 239321 [Multi-domain]  Cd Length: 154  Bit Score: 164.69  E-value: 2.38e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082725  94 GPANGKVTVIEFFDYQCVYCSRLAPVMEQVIKAHPQTRFAFKEWPIFGgrwESSLEAAKTGLQIYQQkGADAYLAYHNGI 173
Cdd:cd03023    1 GNPNGDVTIVEFFDYNCGYCKKLAPELEKLLKEDPDVRVVFKEFPILG---ESSVLAARVALAVWKN-GPGKYLEFHNAL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082725 174 YATGhneGKLTTADIQQQAKKAGFDAKKAT------DVEPVLQSINDLAQEIGLSGTPGVIVMpttgateasITVFPGLA 247
Cdd:cd03023   77 MATR---GRLNEESLLRIAKKAGLDEAKLKkdmddpEIEATIDKNRQLARALGITGTPAFIIG---------DTVIPGAV 144

                        170
                 ....*....|
gi 496082725 248 DQASLEAAIK 257
Cdd:cd03023  145 PADTLKEAID 154
ScsC_N pfam18312
Copper resistance protein ScsC N-terminal domain; This is the N-terminal domain found in ...
 35-68 1.72e-08

Copper resistance protein ScsC N-terminal domain; This is the N-terminal domain found in Copper resistance protein ScsS present in Proteus mirabilis. ScsC is a powerful disulfide isomerase that is able to refold and reactivate the scrambled disulfide form of the model substrate RNase A. The protein has a thioredoxin 4 domain (pfam13462) but, unlike other characterized proteins in this family, it is trimeric. The N-terminal domain is responsible for trimerization of ScsC which is needed for isomerase activity.


:

Pssm-ID: 465704  Cd Length: 34  Bit Score: 49.31  E-value: 1.72e-08
                          10        20        30
                  ....*....|....*....|....*....|....
gi 496082725   35 QEAKIGKIAADYLVAHPEVLLQASQKLQQIQAEQ 68
Cdd:pfam18312   1 QKAAIEAIVRDYLLENPEILVEALTALQKRQAAA 34
 
Name Accession Description Interval E-value
DsbA_Com1_like cd03023
DsbA family, Com1-like subfamily; composed of proteins similar to Com1, a 27-kDa outer ...
 94-257 2.38e-51

DsbA family, Com1-like subfamily; composed of proteins similar to Com1, a 27-kDa outer membrane-associated immunoreactive protein originally found in both acute and chronic disease strains of the pathogenic bacteria Coxiella burnetti. It contains a CXXC motif, assumed to be imbedded in a DsbA-like structure. Its homology to DsbA suggests that the protein is a protein disulfide oxidoreductase. The role of such a protein in pathogenesis is unknown.


Pssm-ID: 239321 [Multi-domain]  Cd Length: 154  Bit Score: 164.69  E-value: 2.38e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082725  94 GPANGKVTVIEFFDYQCVYCSRLAPVMEQVIKAHPQTRFAFKEWPIFGgrwESSLEAAKTGLQIYQQkGADAYLAYHNGI 173
Cdd:cd03023    1 GNPNGDVTIVEFFDYNCGYCKKLAPELEKLLKEDPDVRVVFKEFPILG---ESSVLAARVALAVWKN-GPGKYLEFHNAL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082725 174 YATGhneGKLTTADIQQQAKKAGFDAKKAT------DVEPVLQSINDLAQEIGLSGTPGVIVMpttgateasITVFPGLA 247
Cdd:cd03023   77 MATR---GRLNEESLLRIAKKAGLDEAKLKkdmddpEIEATIDKNRQLARALGITGTPAFIIG---------DTVIPGAV 144

                        170
                 ....*....|
gi 496082725 248 DQASLEAAIK 257
Cdd:cd03023  145 PADTLKEAID 154
DsbG COG1651
Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, ...
 99-259 4.66e-28

Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441257 [Multi-domain]  Cd Length: 152  Bit Score: 104.70  E-value: 4.66e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082725  99 KVTVIEFFDYQCVYCSRLAPVMEQVIKAHP--QTRFAFKEWPIFGgrwESSLEAAKTGLQIYQQkgaDAYLAYHNGIYAt 176
Cdd:COG1651    1 KVTVVEFFDYQCPYCARFHPELPELLKKYVdgKVRVVYRPFPLLH---PDSLRAARAALCAADQ---GKFWAFHDALFA- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082725 177 ghNEGKLTTADIQQQAKKAGFDAKKAT------DVEPVLQSINDLAQEIGLSGTPGVIVMPttgateasiTVFPGLADQA 250
Cdd:COG1651   74 --NQPALTDDDLREIAKEAGLDAAKFDaclnsgAVAAKVEADTALAQALGVTGTPTFVVNG---------KLVSGAVPYE 142


                 ....*....
gi 496082725 251 SLEAAIKKA 259
Cdd:COG1651  143 ELEAALDAA 151
Thioredoxin_4 pfam13462
Thioredoxin;
90-229 1.93e-10

Thioredoxin;


Pssm-ID: 433227 [Multi-domain]  Cd Length: 164  Bit Score: 58.12  E-value: 1.93e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082725   90 TPTYGPANGKVTVIEFFDYQCVYCSRLAPVMEQVIKAHPQT---RFAFKEWPIfgGRWESSLEAAKTgLQIYQQKGADAY 166
Cdd:pfam13462   4 DPVIGNPDAPVTVVEYADLRCPHCAKFHEEVLKLLEEYIDTgkvRFIIRDFPL--DGEGESLLAAMA-ARCAGDQSPEYF 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496082725  167 LAYHNGIYATGHNEGklTTADIQQQAK---KAGFDAKKATDVEPVLQSINDLAQEIGLSGTPGVIV 229
Cdd:pfam13462  81 LVIDKLLYSQQEEWA--QDLELAALAGlkdEEFEACLEEEDFLALVMADVKEARAAGINFTPTFII 144
ScsC_N pfam18312
Copper resistance protein ScsC N-terminal domain; This is the N-terminal domain found in ...
 35-68 1.72e-08

Copper resistance protein ScsC N-terminal domain; This is the N-terminal domain found in Copper resistance protein ScsS present in Proteus mirabilis. ScsC is a powerful disulfide isomerase that is able to refold and reactivate the scrambled disulfide form of the model substrate RNase A. The protein has a thioredoxin 4 domain (pfam13462) but, unlike other characterized proteins in this family, it is trimeric. The N-terminal domain is responsible for trimerization of ScsC which is needed for isomerase activity.


Pssm-ID: 465704  Cd Length: 34  Bit Score: 49.31  E-value: 1.72e-08
                          10        20        30
                  ....*....|....*....|....*....|....
gi 496082725   35 QEAKIGKIAADYLVAHPEVLLQASQKLQQIQAEQ 68
Cdd:pfam18312   1 QKAAIEAIVRDYLLENPEILVEALTALQKRQAAA 34
 
Name Accession Description Interval E-value
DsbA_Com1_like cd03023
DsbA family, Com1-like subfamily; composed of proteins similar to Com1, a 27-kDa outer ...
 94-257 2.38e-51

DsbA family, Com1-like subfamily; composed of proteins similar to Com1, a 27-kDa outer membrane-associated immunoreactive protein originally found in both acute and chronic disease strains of the pathogenic bacteria Coxiella burnetti. It contains a CXXC motif, assumed to be imbedded in a DsbA-like structure. Its homology to DsbA suggests that the protein is a protein disulfide oxidoreductase. The role of such a protein in pathogenesis is unknown.


Pssm-ID: 239321 [Multi-domain]  Cd Length: 154  Bit Score: 164.69  E-value: 2.38e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082725  94 GPANGKVTVIEFFDYQCVYCSRLAPVMEQVIKAHPQTRFAFKEWPIFGgrwESSLEAAKTGLQIYQQkGADAYLAYHNGI 173
Cdd:cd03023    1 GNPNGDVTIVEFFDYNCGYCKKLAPELEKLLKEDPDVRVVFKEFPILG---ESSVLAARVALAVWKN-GPGKYLEFHNAL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082725 174 YATGhneGKLTTADIQQQAKKAGFDAKKAT------DVEPVLQSINDLAQEIGLSGTPGVIVMpttgateasITVFPGLA 247
Cdd:cd03023   77 MATR---GRLNEESLLRIAKKAGLDEAKLKkdmddpEIEATIDKNRQLARALGITGTPAFIIG---------DTVIPGAV 144

                        170
                 ....*....|
gi 496082725 248 DQASLEAAIK 257
Cdd:cd03023  145 PADTLKEAID 154
DsbG COG1651
Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, ...
 99-259 4.66e-28

Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441257 [Multi-domain]  Cd Length: 152  Bit Score: 104.70  E-value: 4.66e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082725  99 KVTVIEFFDYQCVYCSRLAPVMEQVIKAHP--QTRFAFKEWPIFGgrwESSLEAAKTGLQIYQQkgaDAYLAYHNGIYAt 176
Cdd:COG1651    1 KVTVVEFFDYQCPYCARFHPELPELLKKYVdgKVRVVYRPFPLLH---PDSLRAARAALCAADQ---GKFWAFHDALFA- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082725 177 ghNEGKLTTADIQQQAKKAGFDAKKAT------DVEPVLQSINDLAQEIGLSGTPGVIVMPttgateasiTVFPGLADQA 250
Cdd:COG1651   74 --NQPALTDDDLREIAKEAGLDAAKFDaclnsgAVAAKVEADTALAQALGVTGTPTFVVNG---------KLVSGAVPYE 142


                 ....*....
gi 496082725 251 SLEAAIKKA 259
Cdd:COG1651  143 ELEAALDAA 151
Thioredoxin_4 pfam13462
Thioredoxin;
90-229 1.93e-10

Thioredoxin;


Pssm-ID: 433227 [Multi-domain]  Cd Length: 164  Bit Score: 58.12  E-value: 1.93e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082725   90 TPTYGPANGKVTVIEFFDYQCVYCSRLAPVMEQVIKAHPQT---RFAFKEWPIfgGRWESSLEAAKTgLQIYQQKGADAY 166
Cdd:pfam13462   4 DPVIGNPDAPVTVVEYADLRCPHCAKFHEEVLKLLEEYIDTgkvRFIIRDFPL--DGEGESLLAAMA-ARCAGDQSPEYF 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 496082725  167 LAYHNGIYATGHNEGklTTADIQQQAK---KAGFDAKKATDVEPVLQSINDLAQEIGLSGTPGVIV 229
Cdd:pfam13462  81 LVIDKLLYSQQEEWA--QDLELAALAGlkdEEFEACLEEEDFLALVMADVKEARAAGINFTPTFII 144
DsbA_DsbA cd03019
DsbA family, DsbA subfamily; DsbA is a monomeric thiol disulfide oxidoreductase protein ...
 95-229 1.25e-09

DsbA family, DsbA subfamily; DsbA is a monomeric thiol disulfide oxidoreductase protein containing a redox active CXXC motif imbedded in a TRX fold. It is involved in the oxidative protein folding pathway in prokaryotes, and is the strongest thiol oxidant known, due to the unusual stability of the thiolate anion form of the first cysteine in the CXXC motif. The highly unstable oxidized form of DsbA directly donates disulfide bonds to reduced proteins secreted into the bacterial periplasm. This rapid and unidirectional process helps to catalyze the folding of newly-synthesized polypeptides. To regain catalytic activity, reduced DsbA is then reoxidized by the membrane protein DsbB, which generates its disulfides from oxidized quinones, which in turn are reoxidized by the electron transport chain.


Pssm-ID: 239317 [Multi-domain]  Cd Length: 178  Bit Score: 56.14  E-value: 1.25e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082725  95 PANGKVTVIEFFDYQCVYCSRLAPVMEQVIKAHPQTrFAFKEWPI-FGGRWesSLEAAKtglqIY---QQKGADAylAYH 170
Cdd:cd03019   12 IPSGKPEVIEFFSYGCPHCYNFEPILEAWVKKLPKD-VKFEKVPVvFGGGE--GEPLAR----AFyaaEALGLED--KLH 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496082725 171 NGIYATGHNEGK--LTTADIQQQAKKAGFDAKKATD------VEPVLQSINDLAQEIGLSGTPGVIV 229
Cdd:cd03019   83 AALFEAIHEKRKrlLDPDDIRKIFLSQGVDKKKFDAaynsfsVKALVAKAEKLAKKYKITGVPAFVV 149
DsbA_family cd02972
DsbA family; consists of DsbA and DsbA-like proteins, including DsbC, DsbG, glutathione (GSH) ...
 102-229 8.97e-09

DsbA family; consists of DsbA and DsbA-like proteins, including DsbC, DsbG, glutathione (GSH) S-transferase kappa (GSTK), 2-hydroxychromene-2-carboxylate (HCCA) isomerase, an oxidoreductase (FrnE) presumed to be involved in frenolicin biosynthesis, a 27-kDa outer membrane protein, and similar proteins. Members of this family contain a redox active CXXC motif (except GSTK and HCCA isomerase) imbedded in a TRX fold, and an alpha helical insert of about 75 residues (shorter in DsbC and DsbG) relative to TRX. DsbA is involved in the oxidative protein folding pathway in prokaryotes, catalyzing disulfide bond formation of proteins secreted into the bacterial periplasm. DsbC and DsbG function as protein disulfide isomerases and chaperones to correct non-native disulfide bonds formed by DsbA and prevent aggregation of incorrectly folded proteins.


Pssm-ID: 239270 [Multi-domain]  Cd Length: 98  Bit Score: 51.64  E-value: 8.97e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082725 102 VIEFFDYQCVYCSRLAPVMEQVIKAHPQT-RFAFKEWPIFGGRWESSLEAAKTGLQIYQQkgaDAYLAYHNGIYATghne 180
Cdd:cd02972    1 IVEFFDPLCPYCYLFEPELEKLLYADDGGvRVVYRPFPLLGGMPPNSLAAARAALAAAAQ---GKFEALHEALADT---- 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 496082725 181 gklttadiqqqakkagfdakkatdvepvlqsinDLAQEIGLSGTPGVIV 229
Cdd:cd02972   74 ---------------------------------ALARALGVTGTPTFVV 89
ScsC_N pfam18312
Copper resistance protein ScsC N-terminal domain; This is the N-terminal domain found in ...
 35-68 1.72e-08

Copper resistance protein ScsC N-terminal domain; This is the N-terminal domain found in Copper resistance protein ScsS present in Proteus mirabilis. ScsC is a powerful disulfide isomerase that is able to refold and reactivate the scrambled disulfide form of the model substrate RNase A. The protein has a thioredoxin 4 domain (pfam13462) but, unlike other characterized proteins in this family, it is trimeric. The N-terminal domain is responsible for trimerization of ScsC which is needed for isomerase activity.


Pssm-ID: 465704  Cd Length: 34  Bit Score: 49.31  E-value: 1.72e-08
                          10        20        30
                  ....*....|....*....|....*....|....
gi 496082725   35 QEAKIGKIAADYLVAHPEVLLQASQKLQQIQAEQ 68
Cdd:pfam18312   1 QKAAIEAIVRDYLLENPEILVEALTALQKRQAAA 34
DSBA pfam01323
DSBA-like thioredoxin domain; This family contains a diverse set of proteins with a ...
 101-229 1.78e-07

DSBA-like thioredoxin domain; This family contains a diverse set of proteins with a thioredoxin-like structure pfam00085. This family also includes 2-hydroxychromene-2-carboxylate (HCCA) isomerase enzymes catalyze one step in prokaryotic polyaromatic hydrocarbon (PAH) catabolic pathways. This family also contains members with functions other than HCCA isomerization, such as Kappa family GSTs, whose similarity to HCCA isomerases was not previously recognized. The sequence Swiss:O07298 has been annotated as a dioxygenase but is almost certainly an HCCA isomerase enzyme. Similarly, the sequence Swiss:Q9ZI67 has been annotated as a dehydrogenase, but is most probably also an HCCA isomerase enzyme. In addition, the Rhizobium leguminosarum Swiss:Q52782 protein has been annotated as a putative glycerol-3-phosphate transfer protein, but is also most likely to be an HCCA isomerase enzyme.


Pssm-ID: 426200 [Multi-domain]  Cd Length: 191  Bit Score: 50.12  E-value: 1.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082725  101 TVIEFFDYQCVYCSRLAPVMEQVIKAHPQTRFAFKEWPIFGG-----------------------RWE-----------S 146
Cdd:pfam01323   1 TVDEFFDFLCPFCYLAKERLEKLAARYGDVKVVYRPFPLAGAkkignvgpsnlpvklkymmadleRWAalygiplrfpaN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082725  147 SLEAAKTGLQIY-----QQKGADAYLAYHNGIYATGHNEGklTTADIQQQAKKAGFDAKKATDV--EPVLQSI----NDL 215
Cdd:pfam01323  81 FLGNSTRANRLAlaagaEGLAEKVVRELFNALWGEGAAIT--DDSVLREVAEKAGLDAEEFDEFldSPAVKEAvrenTAA 158

                         170
                  ....*....|....
gi 496082725  216 AQEIGLSGTPGVIV 229
Cdd:pfam01323 159 AISLGVFGVPTFVV 172
 
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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