Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P0AEG6 (DSBC_ECOLI)

Last modified June 16, 2009. Version 37. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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) [Complete 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

Required for disulfide bond formation in some periplasmic proteins. Acts by transferring its disulfide bond to other proteins and is reduced in the process. DsbC is reoxidized by a yet uncharacterized protein. Also acts as a disulfide isomerase.

Subunit structure

Homodimer.

Subcellular location

Periplasm.

Sequence similarities

Belongs to the thioredoxin family. DsbC subfamily.

Contains 1 thioredoxin domain.

Ontologies

Keywords
   Cellular componentPeriplasm
   DomainRedox-active center
Signal
   PTMDisulfide bond
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological processcell redox homeostasis

Inferred from electronic annotation. Source: InterPro

   Cellular componentperiplasmic space

Inferred from electronic annotation. Source: UniProtKB-SubCell

Complete GO annotation...

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.9
Disulfide bond161 ↔ 183 Ref.9

Experimental info

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

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P0AEG6-1 [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: 1987126] [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: 9278503] [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: 16738553] [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: 9298646] [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: 8168498] [Abstract]
Cited for: CHARACTERIZATION, MUTAGENESIS.
[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: 7536035] [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: 8168497] [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: 9254601] [Abstract]
Cited for: CHARACTERIZATION.
[9]"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: 10700276] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), DISULFIDE BONDS.
+Additional computationally mapped references.

Cross-references

Sequence databases

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.
RefSeqAP_003452.1.
NP_417369.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1EEJX-ray1.90A/B21-236[»]
1G0TX-ray2.60A/B21-236[»]
1JZDX-ray2.30A/B18-236[»]
1JZOX-ray1.92A/B21-236[»]
1TJDX-ray2.50A21-236[»]
2IYJX-ray2.00A/B19-91[»]
ModBaseSearch...

Genome annotation databases

GeneID947363.
GenomeReviewsGene locus JW2861 in contig AP009048_GR.
Gene locus b2893 in contig U00096_GR.
KEGGecj:JW2861.
eco:b2893.

Organism-specific databases

EchoBASEEB1063.
EcoGeneEG11070. dsbC.
CMRSearch...

Phylogenomic databases

HOGENOMP0AEG6.
OMAP0AEG6. GLYEVKL.

Enzyme and pathway databases

BioCycEcoCyc:DSBC-MON.

Family and domain databases

InterProIPR018950. dS-bond_isomerase_DsbC/G_N.
IPR009094. dS-bond_isomerase_DsbC_N.
IPR017936. Thioredoxin-like.
IPR017937. Thioredoxin_CS.
IPR012335. Thioredoxin_fold.
[Graphical view]
Gene3DG3DSA:3.10.450.70. Disulf_isomers_N. 1 hit.
G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
PfamPF10411. DsbC_N. 1 hit.
[Graphical view]
PROSITEPS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

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: June 16, 2009
This is version 37 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents