Thiol:disulfide interchange protein DsbC precursor

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P0AEG6 (DSBC_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 60. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Thiol:disulfide interchange protein DsbC

Gene names

Name:	dsbC
Synonyms:	xprA
Ordered Locus Names:	b2893, JW2861

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	236 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Cellular component	Periplasm
Domain	Redox-active center Signal
PTM	Disulfide bond
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	cell redox homeostasis Inferred from electronic annotation. Source: InterPro protein folding Inferred from mutant phenotype Ref.5. Source: EcoliWiki
Molecular function	protein disulfide isomerase activity Inferred from direct assay Ref.5. Source: EcoCyc protein disulfide oxidoreductase activity Inferred from mutant phenotype Ref.9. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 20

Ref.4

Chain

21 – 236

216

Thiol:disulfide interchange protein DsbC

PRO_0000034273

Regions

Domain

36 – 231

196

Thioredoxin

Amino acid modifications

Disulfide bond

118 ↔ 121

Redox-active Ref.10

Disulfide bond

161 ↔ 183

Ref.10

Experimental info

Mutagenesis

118

C → T or A: Loss of activity. Ref.5

Mutagenesis

121

C → A: Partial loss of activity. Ref.5

Mutagenesis

121

C → V: Loss of activity. Ref.5

Mutagenesis

161

C → S: Destabilization of protein. Ref.5

Mutagenesis

183

C → L: Destabilization of protein. Ref.5

Sequence conflict

219

Missing in AAA62788. Ref.1

Secondary structure

236

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P0AEG6 [UniParc].

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

236

25,622

        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' referencesShow '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, 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: 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]	"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: 19965429] [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: 10700276] [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.

PIR

E65073.

RefSeq

NP_417369.1. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1EEJ	X-ray	1.90	A/B	21-236	[»]
1G0T	X-ray	2.60	A/B	21-236	[»]
1JZD	X-ray	2.30	A/B	18-236	[»]
1JZO	X-ray	1.92	A/B	21-236	[»]
1TJD	X-ray	2.50	A	21-236	[»]
2IYJ	X-ray	2.00	A/B	19-91	[»]

ProteinModelPortal

P0AEG6.

SMR

P0AEG6. Positions 21-236.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-35818N.

IntAct

P0AEG6. 9 interactions.

MINT

MINT-1288669.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBESCT00000001306; EBESCP00000001306; EBESCG00000001082.
EBESCT00000001307; EBESCP00000001307; EBESCG00000001082.
EBESCT00000017984; EBESCP00000017275; EBESCG00000017040.

GeneID

947363.

GenomeReviews

Gene locus JW2861 in contig AP009048_GR.
Gene locus b2893 in contig U00096_GR.

KEGG

ecj:JW2861.
eco:b2893.

PATRIC

32121198. VBIEscCol129921_2987.

Organism-specific databases

EchoBASE

EB1063.

EcoGene

EG11070. dsbC.

Phylogenomic databases

eggNOG

COG1651.

GeneTree

EBGT00050000010153.

HOGENOM

HBG469935.

OMA

GLYEVKL.

PhylomeDB

P0AEG6.

ProtClustDB

PRK10877.

Enzyme and pathway databases

BioCyc

EcoCyc:DSBC-MONOMER.
MetaCyc:DSBC-MONOMER.

Gene expression databases

Genevestigator

P0AEG6.

Family and domain databases

InterPro

IPR018950. DiS-bond_isomerase_DsbC/G_N.
IPR009094. DiS-bond_isomerase_DsbC_N.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
[Graphical view]

Gene3D

G3DSA:3.10.450.70. Disulf_isomers_N. 1 hit.
G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.

K03981.

Pfam

PF10411. DsbC_N. 1 hit.
[Graphical view]

SUPFAM

SSF54423. Disulfide_bond_isomerase_N. 1 hit.
SSF52833. Thiordxn-like_fd. 1 hit.

PROSITE

PS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

DSBC_ECOLI

Accession

Primary (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:	January 25, 2012
This is version 60 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic 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

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents