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P0AEG6 (DSBC_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Thiol:disulfide interchange protein DsbC
Gene names
Name:dsbC
Synonyms:xprA
Ordered Locus Names:b2893, JW2861
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length236 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.9

Subunit structure

Homodimer.

Subcellular location

Periplasm Ref.5.

Sequence similarities

Belongs to the thioredoxin family. DsbC subfamily.

Contains 1 thioredoxin domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Ref.4
Chain21 – 236216Thiol:disulfide interchange protein DsbC
PRO_0000034273

Regions

Domain36 – 231196Thioredoxin

Amino acid modifications

Disulfide bond118 ↔ 121Redox-active Ref.10
Disulfide bond161 ↔ 183 Ref.10

Experimental info

Mutagenesis1181C → T or A: Loss of activity. Ref.5
Mutagenesis1211C → A: Partial loss of activity. Ref.5
Mutagenesis1211C → V: Loss of activity. Ref.5
Mutagenesis1611C → S: Destabilization of protein. Ref.5
Mutagenesis1831C → L: Destabilization of protein. Ref.5
Sequence conflict2191Missing in AAA62788. Ref.1

Secondary structure

......................................... 236
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0AEG6 [UniParc].

Last modified December 6, 2005. Version 1.
Checksum: 69A834A666BAA6D6

FASTA23625,622
        10         20         30         40         50         60 
MKKGFMLFTL LAAFSGFAQA DDAAIQQTLA KMGIKSSDIQ PAPVAGMKTV LTNSGVLYIT 

        70         80         90        100        110        120 
DDGKHIIQGP MYDVSGTAPV NVTNKMLLKQ LNALEKEMIV YKAPQEKHVI TVFTDITCGY 

       130        140        150        160        170        180 
CHKLHEQMAD YNALGITVRY LAFPRQGLDS DAEKEMKAIW CAKDKNKAFD DVMAGKSVAP 

       190        200        210        220        230 
ASCDVDIADH YALGVQLGVS GTPAVVLSNG TLVPGYQPPK EMKEFLDEHQ KMTSGK 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence of the Escherichia coli recJ chromosomal region and construction of recJ-overexpression plasmids."
Lovett S.T., Kolodner R.D.
J. Bacteriol. 173:353-364(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[2]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[3]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
Link A.J., Robison K., Church G.M.
Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 21-32.
Strain: K12 / EMG2.
[5]"The Escherichia coli dsbC (xprA) gene encodes a periplasmic protein involved in disulfide bond formation."
Missiakas D., Georgopoulos C., Raina S.
EMBO J. 13:2013-2020(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-118; CYS-121; CYS-161 AND CYS-183.
[6]"Structural and functional characterization of DsbC, a protein involved in disulfide bond formation in Escherichia coli."
Zapun A., Missiakas D., Raina S., Creighton T.E.
Biochemistry 34:5075-5089(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION, MUTAGENESIS, SEQUENCE REVISION TO 219.
[7]"Characterization of DsbC, a periplasmic protein of Erwinia chrysanthemi and Escherichia coli with disulfide isomerase activity."
Shevchik V.E., Condemine G., Robert-Baudouy J.
EMBO J. 13:2007-2012(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[8]"In vitro and in vivo redox states of the Escherichia coli periplasmic oxidoreductases DsbA and DsbC."
Joly J.C., Swartz J.R.
Biochemistry 36:10067-10072(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[9]"A periplasmic reducing system protects single cysteine residues from oxidation."
Depuydt M., Leonard S.E., Vertommen D., Denoncin K., Morsomme P., Wahni K., Messens J., Carroll K.S., Collet J.F.
Science 326:1109-1111(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
Strain: K12 / MC1000 / ATCC 39531.
[10]"Crystal structure of the protein disulfide bond isomerase, DsbC, from Escherichia coli."
McCarthy A.A., Haebel P.W., Torronen A., Rybin V., Baker E.N., Metcalf P.
Nat. Struct. Biol. 7:196-199(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), DISULFIDE BONDS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M54884 Genomic DNA. Translation: AAA62788.1.
U28375 Genomic DNA. Translation: AAA83074.1.
U00096 Genomic DNA. Translation: AAC75931.1.
AP009048 Genomic DNA. Translation: BAE76958.1.
PIRE65073.
RefSeqNP_417369.1. NC_000913.2.
YP_491094.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP0AEG6.
SMRP0AEG6. Positions 21-236.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-35818N.
IntActP0AEG6. 9 interactions.
MINTMINT-1288669.
STRING511145.b2893.

Proteomic databases

PaxDbP0AEG6.
PRIDEP0AEG6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC75931; AAC75931; b2893.
BAE76958; BAE76958; BAE76958.
GeneID12932310.
947363.
KEGGecj:Y75_p2825.
eco:b2893.
PATRIC32121198. VBIEscCol129921_2987.

Organism-specific databases

EchoBASEEB1063.
EcoGeneEG11070. dsbC.

Phylogenomic databases

eggNOGCOG1651.
HOGENOMHOG000222077.
KOK03981.
OMAGLYEVKL.
ProtClustDBPRK10877.

Enzyme and pathway databases

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

Gene expression databases

GenevestigatorP0AEG6.

Family and domain databases

Gene3D3.10.450.70. 1 hit.
3.40.30.10. 1 hit.
InterProIPR018950. DiS-bond_isomerase_DsbC/G_N.
IPR009094. DiS-bond_isomerase_DsbC_N.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
[Graphical view]
PfamPF10411. DsbC_N. 1 hit.
PF13098. Thioredoxin_2. 1 hit.
[Graphical view]
SUPFAMSSF54423. Disulfide_bond_isomerase_N. 1 hit.
SSF52833. Thiordxn-like_fd. 1 hit.
PROSITEPS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0AEG6.

Entry information

Entry nameDSBC_ECOLI
AccessionPrimary (citable) accession number: P0AEG6
Secondary accession number(s): P21892, Q2M9U8
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: December 6, 2005
Last modified: May 1, 2013
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families