ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P0AEG6


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name DSBC_ECOLI
Primary accession number P0AEG6
Secondary accession numbers P21892 Q2M9U8
Integrated into Swiss-Prot on December 6, 2005
Sequence was last modified on December 6, 2005 (Sequence version 1)
Annotations were last modified on    June 16, 2009 (Entry version 37)
Name and origin of the protein
Protein name Thiol:disulfide interchange protein dsbC [Precursor]
Synonyms None
Gene name
Name: dsbC
Synonyms: xprA
OrderedLocusNames: b2893, JW2861
From
Escherichia coli (strain K12) [TaxID: 83333] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12;
PubMed=1987126 [NCBI, ExPASy, EBI, Israel, Japan]
Lovett S.T., Kolodner R.D.;
"Nucleotide sequence of the Escherichia coli recJ chromosomal region and construction of recJ-overexpression plasmids.";
J. Bacteriol. 173:353-364(1991).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1474(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan]
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[4]
PROTEIN SEQUENCE OF 21-32.
STRAIN=K12 / EMG2;
DOI=10.1002/elps.1150180807; PubMed=9298646 [NCBI, ExPASy, EBI, Israel, Japan]
Link A.J., Robison K., Church G.M.;
"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12.";
Electrophoresis 18:1259-1313(1997).
[5]
CHARACTERIZATION, AND MUTAGENESIS.
PubMed=8168498 [NCBI, ExPASy, EBI, Israel, Japan]
Missiakas D., Georgopoulos C., Raina S.;
"The Escherichia coli dsbC (xprA) gene encodes a periplasmic protein involved in disulfide bond formation.";
EMBO J. 13:2013-2020(1994).
[6]
CHARACTERIZATION, MUTAGENESIS, AND SEQUENCE REVISION TO 219.
DOI=10.1021/bi00015a019; PubMed=7536035 [NCBI, ExPASy, EBI, Israel, Japan]
Zapun A., Missiakas D., Raina S., Creighton T.E.;
"Structural and functional characterization of DsbC, a protein involved in disulfide bond formation in Escherichia coli.";
Biochemistry 34:5075-5089(1995).
[7]
CHARACTERIZATION.
PubMed=8168497 [NCBI, ExPASy, EBI, Israel, Japan]
Shevchik V.E., Condemine G., Robert-Baudouy J.;
"Characterization of DsbC, a periplasmic protein of Erwinia chrysanthemi and Escherichia coli with disulfide isomerase activity.";
EMBO J. 13:2007-2012(1994).
[8]
CHARACTERIZATION.
DOI=10.1021/bi9707739; PubMed=9254601 [NCBI, ExPASy, EBI, Israel, Japan]
Joly J.C., Swartz J.R.;
"In vitro and in vivo redox states of the Escherichia coli periplasmic oxidoreductases DsbA and DsbC.";
Biochemistry 36:10067-10072(1997).
[9]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), AND DISULFIDE BONDS.
DOI=10.1038/73295; PubMed=10700276 [NCBI, ExPASy, EBI, Israel, Japan]
McCarthy A.A., Haebel P.W., Torronen A., Rybin V., Baker E.N., Metcalf P.;
"Crystal structure of the protein disulfide bond isomerase, DsbC, from Escherichia coli.";
Nat. Struct. Biol. 7:196-199(2000).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M54884; AAA62788.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U28375; AAA83074.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC75931.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAE76958.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR E65073; E65073.
RefSeq AP_003452.1; -.
NP_417369.1; -.
3D structure databases
PDB
1EEJ; X-ray; 1.90 A; A/B=21-236.[ExPASy / RCSB / EBI]
1G0T; X-ray; 2.60 A; A/B=21-236.[ExPASy / RCSB / EBI]
1JZD; X-ray; 2.30 A; A/B=18-236.[ExPASy / RCSB / EBI]
1JZO; X-ray; 1.92 A; A/B=21-236.[ExPASy / RCSB / EBI]
1TJD; X-ray; 2.50 A; A=21-236.[ExPASy / RCSB / EBI]
2IYJ; X-ray; 2.00 A; A/B=19-91.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1EEJ; -.
1G0T; -.
1JZD; -.
1JZO; -.
1TJD; -.
2IYJ; -.
ModBase P0AEG6.
Enzyme and pathway databases
BioCyc EcoCyc:DSBC-MON; -.
Organism-specific databases
EchoBASE EB1063; -.
EcoGene EG11070; dsbC.
Ontologies
GO
GO:0042597; Cellular component: periplasmic space (inferred from electronic annotation from UniProtKB-SubCell).
GO:0045454; Biological process: cell redox homeostasis (inferred from electronic annotation from InterPro).
QuickGo view.
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 of domain structure.
Gene3D G3DSA:3.10.450.70; Disulf_isomers_N; 1.
G3DSA:3.40.30.10; Thioredoxin_fold; 1.
Pfam PF10411; DsbC_N; 1.
Pfam graphical view of domain structure.
PROSITE PS00194; THIOREDOXIN_1; 1.
PS51352; THIOREDOXIN_2; 1.
PROSITE graphical view of domain structure (profiles).
Genome annotation databases
GeneID 947363; -.
GenomeReviews AP009048_GR; JW2861.
U00096_GR; b2893.
KEGG ecj:JW2861; -.
eco:b2893; -.
Phylogenomic databases
HOGENOM P0AEG6; -.
OMA P0AEG6; GLYEVKL.
Genome annotation databases
CMR P0AEG6; b2893.
Other
ProtoNet P0AEG6.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Complete proteome; Direct protein sequencing; Disulfide bond; Periplasm; Redox-active center; Signal.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    20  20      
CHAIN   21   236  216     Thiol:disulfide interchange protein dsbC. PRO_0000034273
DOMAIN   36   231  196     Thioredoxin. 
DISULFID   118   121        Redox-active. 
DISULFID   161   183         
MUTAGEN   118   118        C->T,A: Loss of activity. 
MUTAGEN   121   121        C->A: Partial loss of activity. 
MUTAGEN   121   121        C->V: Loss of activity. 
MUTAGEN   161   161        C->S: Destabilization of protein. 
MUTAGEN   183   183        C->L: Destabilization of protein. 
CONFLICT   219   219        Missing (in Ref. 1; AAA62788). 
HELIX   22    31  10      
STRAND   36    41  6      
STRAND   47    52  6      
STRAND   55    60  6      
STRAND   65    69  5      
STRAND   71    73  3      
STRAND   75    78  4      
HELIX   82    92  11      
HELIX   93    97  5      
STRAND   98   101  4      
STRAND   108   114  7      
HELIX   119   125  7      
HELIX   128   133  6      
STRAND   136   142  7      
STRAND   148   150  3      
HELIX   151   160  10      
STRAND   162   164  3      
HELIX   165   173  9      
HELIX   187   197  11      
STRAND   201   206  6      
STRAND   212   215  4      
HELIX   219   234  16      
Sequence information
Length: 236 AA [This is the length of the unprocessed precursor] Molecular weight: 25622 Da [This is the MW of the unprocessed precursor] CRC64: 69A834A666BAA6D6 [This is a checksum on the sequence]
        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 

P0AEG6 in FASTA format

View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ch flag SIB Switzerland Mirror sites: Australia  Brazil  Canada  China  Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!