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Protein

Thiol:disulfide interchange protein DsbC

Gene

dsbC

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Acts as a disulfide isomerase, interacting with incorrectly folded proteins to correct non-native disulfide bonds. DsbG and DsbC are part of a periplasmic reducing system that controls the level of cysteine sulfenylation, and provides reducing equivalents to rescue oxidatively damaged secreted proteins. Acts by transferring its disulfide bond to other proteins and is reduced in the process. DsbC is reoxidized by DsbD.1 Publication

GO - Molecular functioni

  • protein disulfide isomerase activity Source: EcoCyc
  • protein disulfide oxidoreductase activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Enzyme and pathway databases

BioCyciEcoCyc:DSBC-MONOMER.
ECOL316407:JW2861-MONOMER.
MetaCyc:DSBC-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Thiol:disulfide interchange protein DsbC
Gene namesi
Name:dsbC
Synonyms:xprA
Ordered Locus Names:b2893, JW2861
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11070. dsbC.

Subcellular locationi

  • Periplasm 1 Publication

GO - Cellular componenti

  • outer membrane-bounded periplasmic space Source: EcoCyc
  • periplasmic space Source: EcoliWiki
Complete GO annotation...

Keywords - Cellular componenti

Periplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi118 – 1181C → T or A: Loss of activity. 1 Publication
Mutagenesisi121 – 1211C → A: Partial loss of activity. 1 Publication
Mutagenesisi121 – 1211C → V: Loss of activity. 1 Publication
Mutagenesisi161 – 1611C → S: Destabilization of protein. 1 Publication
Mutagenesisi183 – 1831C → L: Destabilization of protein. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 20201 PublicationAdd
BLAST
Chaini21 – 236216Thiol:disulfide interchange protein DsbCPRO_0000034273Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi118 ↔ 121Redox-activePROSITE-ProRule annotation1 Publication
Disulfide bondi161 ↔ 1831 Publication

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiP0AEG6.
PRIDEiP0AEG6.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

BioGridi4261304. 486 interactions.
DIPiDIP-35818N.
IntActiP0AEG6. 9 interactions.
MINTiMINT-1288669.
STRINGi511145.b2893.

Structurei

Secondary structure

1
236
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi22 – 3110Combined sources
Beta strandi36 – 416Combined sources
Beta strandi47 – 526Combined sources
Beta strandi55 – 606Combined sources
Beta strandi65 – 695Combined sources
Beta strandi71 – 733Combined sources
Beta strandi75 – 784Combined sources
Helixi82 – 9211Combined sources
Helixi93 – 975Combined sources
Beta strandi98 – 1014Combined sources
Beta strandi108 – 1147Combined sources
Helixi119 – 1257Combined sources
Helixi128 – 1336Combined sources
Beta strandi136 – 1427Combined sources
Beta strandi148 – 1503Combined sources
Helixi151 – 16010Combined sources
Beta strandi162 – 1643Combined sources
Helixi165 – 1739Combined sources
Helixi187 – 19711Combined sources
Beta strandi201 – 2066Combined sources
Beta strandi212 – 2154Combined sources
Helixi219 – 23416Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EEJX-ray1.90A/B21-236[»]
1G0TX-ray2.60A/B21-236[»]
1JZDX-ray2.30A/B20-236[»]
1JZOX-ray1.92A/B21-236[»]
1TJDX-ray2.50A21-236[»]
2IYJX-ray2.00A/B19-91[»]
ProteinModelPortaliP0AEG6.
SMRiP0AEG6. Positions 21-236.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AEG6.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini36 – 231196ThioredoxinPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the thioredoxin family. DsbC subfamily.Curated
Contains 1 thioredoxin domain.PROSITE-ProRule annotation

Keywords - Domaini

Redox-active center, Signal

Phylogenomic databases

eggNOGiENOG4105T95. Bacteria.
COG1651. LUCA.
HOGENOMiHOG000222077.
InParanoidiP0AEG6.
KOiK03981.
OMAiVWCAKDP.
PhylomeDBiP0AEG6.

Family and domain databases

Gene3Di3.10.450.70. 1 hit.
3.40.30.10. 1 hit.
InterProiIPR018950. DiS-bond_isomerase_DsbC/G_N.
IPR009094. DiS-bond_isomerase_DsbC_N.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF10411. DsbC_N. 1 hit.
PF13098. Thioredoxin_2. 1 hit.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 1 hit.
SSF54423. SSF54423. 1 hit.
PROSITEiPS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0AEG6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKGFMLFTL LAAFSGFAQA DDAAIQQTLA KMGIKSSDIQ PAPVAGMKTV
60 70 80 90 100
LTNSGVLYIT DDGKHIIQGP MYDVSGTAPV NVTNKMLLKQ LNALEKEMIV
110 120 130 140 150
YKAPQEKHVI TVFTDITCGY CHKLHEQMAD YNALGITVRY LAFPRQGLDS
160 170 180 190 200
DAEKEMKAIW CAKDKNKAFD DVMAGKSVAP ASCDVDIADH YALGVQLGVS
210 220 230
GTPAVVLSNG TLVPGYQPPK EMKEFLDEHQ KMTSGK
Length:236
Mass (Da):25,622
Last modified:December 6, 2005 - v1
Checksum:i69A834A666BAA6D6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti219 – 2191Missing in AAA62788 (PubMed:1987126).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M54884 Genomic DNA. Translation: AAA62788.1.
U28375 Genomic DNA. Translation: AAA83074.1.
U00096 Genomic DNA. Translation: AAC75931.1.
AP009048 Genomic DNA. Translation: BAE76958.1.
PIRiE65073.
RefSeqiNP_417369.1. NC_000913.3.
WP_000715214.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75931; AAC75931; b2893.
BAE76958; BAE76958; BAE76958.
GeneIDi947363.
KEGGiecj:JW2861.
eco:b2893.
PATRICi32121198. VBIEscCol129921_2987.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M54884 Genomic DNA. Translation: AAA62788.1.
U28375 Genomic DNA. Translation: AAA83074.1.
U00096 Genomic DNA. Translation: AAC75931.1.
AP009048 Genomic DNA. Translation: BAE76958.1.
PIRiE65073.
RefSeqiNP_417369.1. NC_000913.3.
WP_000715214.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EEJX-ray1.90A/B21-236[»]
1G0TX-ray2.60A/B21-236[»]
1JZDX-ray2.30A/B20-236[»]
1JZOX-ray1.92A/B21-236[»]
1TJDX-ray2.50A21-236[»]
2IYJX-ray2.00A/B19-91[»]
ProteinModelPortaliP0AEG6.
SMRiP0AEG6. Positions 21-236.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261304. 486 interactions.
DIPiDIP-35818N.
IntActiP0AEG6. 9 interactions.
MINTiMINT-1288669.
STRINGi511145.b2893.

Proteomic databases

PaxDbiP0AEG6.
PRIDEiP0AEG6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75931; AAC75931; b2893.
BAE76958; BAE76958; BAE76958.
GeneIDi947363.
KEGGiecj:JW2861.
eco:b2893.
PATRICi32121198. VBIEscCol129921_2987.

Organism-specific databases

EchoBASEiEB1063.
EcoGeneiEG11070. dsbC.

Phylogenomic databases

eggNOGiENOG4105T95. Bacteria.
COG1651. LUCA.
HOGENOMiHOG000222077.
InParanoidiP0AEG6.
KOiK03981.
OMAiVWCAKDP.
PhylomeDBiP0AEG6.

Enzyme and pathway databases

BioCyciEcoCyc:DSBC-MONOMER.
ECOL316407:JW2861-MONOMER.
MetaCyc:DSBC-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0AEG6.
PROiP0AEG6.

Family and domain databases

Gene3Di3.10.450.70. 1 hit.
3.40.30.10. 1 hit.
InterProiIPR018950. DiS-bond_isomerase_DsbC/G_N.
IPR009094. DiS-bond_isomerase_DsbC_N.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF10411. DsbC_N. 1 hit.
PF13098. Thioredoxin_2. 1 hit.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 1 hit.
SSF54423. SSF54423. 1 hit.
PROSITEiPS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDSBC_ECOLI
AccessioniPrimary (citable) accession number: P0AEG6
Secondary accession number(s): P21892, Q2M9U8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: December 6, 2005
Last modified: September 7, 2016
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.