Reviewed, UniProtKB/Swiss-Prot P0AEG6 (DSBC_ECOLI)

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) [Complete proteome] [HAMAP]

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	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 component	Periplasm
Domain	Redox-active center Signal
PTM	Disulfide bond
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	cell redox homeostasis Inferred from electronic annotation. Source: InterPro
Cellular component	periplasmic space Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 20

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.9

Disulfide bond

161 ↔ 183

Ref.9

Experimental info

Mutagenesis

118

1

C → T or A: Loss of activity.

Mutagenesis

121

1

C → A: Partial loss of activity.

Mutagenesis

121

1

C → V: Loss of activity.

Mutagenesis

161

1

C → S: Destabilization of protein.

Mutagenesis

183

1

C → L: Destabilization of protein.

Sequence conflict

219

1

Missing in AAA62788. Ref.1

Secondary structure

1

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236

Helix Strand Turn

Details...

Helix

22 – 31

10

Beta strand

36 – 41

6

Beta strand

47 – 52

6

Beta strand

55 – 60

6

Beta strand

65 – 69

5

Beta strand

71 – 73

3

Beta strand

75 – 78

4

Helix

82 – 92

11

Helix

93 – 97

5

Beta strand

98 – 101

4

Beta strand

108 – 114

7

Helix

119 – 125

7

Helix

128 – 133

6

Beta strand

136 – 142

7

Beta strand

148 – 150

3

Helix

151 – 160

10

Beta strand

162 – 164

3

Helix

165 – 173

9

Helix

187 – 197

11

Beta strand

201 – 206

6

Beta strand

212 – 215

4

Helix

219 – 234

16

Sequences

	Sequence		Length	Mass (Da)
	P0AEG6-1 [UniParc]. Last modified December 6, 2005. Version 1. Checksum: 69A834A666BAA6D6	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

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, 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

EMBLGenBankDDBJ

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

AP_003452.1.
NP_417369.1.

3D structure databases

PDBPDBe

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	[»]

ModBase

Search...

Genome annotation databases

GeneID

947363.

GenomeReviews

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

KEGG

ecj:JW2861.
eco:b2893.

Organism-specific databases

EchoBASE

EB1063.

EcoGene

EG11070. dsbC.

CMR

Search...

Phylogenomic databases

HOGENOM

P0AEG6.

OMA

P0AEG6. GLYEVKL.

Enzyme and pathway databases

BioCyc

EcoCyc:DSBC-MON.

Family and domain databases

InterPro

IPR018950. dS-bond_isomerase_DsbC/G_N.
IPR009094. dS-bond_isomerase_DsbC_N.
IPR017936. Thioredoxin-like.
IPR017937. Thioredoxin_CS.
IPR012335. Thioredoxin_fold.
[Graphical view]

Gene3D

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

Pfam

PF10411. DsbC_N. 1 hit.
[Graphical view]

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:	June 16, 2009
This is version 37 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)