(data stored in ACNUC10821 zone)

SWISSPROT: C8U2W9_ECO10

ID   C8U2W9_ECO10            Unreviewed;       248 AA.
AC   C8U2W9;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 50.
DE   RecName: Full=Thiol:disulfide interchange protein {ECO:0000256|RuleBase:RU364038};
GN   Name=dsbG {ECO:0000313|EMBL:BAI29477.1};
GN   OrderedLocusNames=ECO103_0613 {ECO:0000313|EMBL:BAI29477.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI29477.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI29477.1, ECO:0000313|Proteomes:UP000000959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12009 / EHEC {ECO:0000313|Proteomes:UP000000959};
RX   PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA   Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K.,
RA   Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M.,
RA   Hayashi T.;
RT   "Comparative genomics reveal the mechanism of the parallel evolution
RT   of O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009).
CC   -!- FUNCTION: Required for disulfide bond formation in some
CC       periplasmic proteins. Acts by transferring its disulfide bond to
CC       other proteins and is reduced in the process.
CC       {ECO:0000256|RuleBase:RU364038}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|RuleBase:RU364038}.
CC   -!- SIMILARITY: Belongs to the thioredoxin family. DsbC subfamily.
CC       {ECO:0000256|RuleBase:RU364038}.
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DR   EMBL; AP010958; BAI29477.1; -; Genomic_DNA.
DR   RefSeq; WP_000913832.1; NC_013353.1.
DR   EnsemblBacteria; BAI29477; BAI29477; ECO103_0613.
DR   KEGG; eoh:ECO103_0613; -.
DR   HOGENOM; HOG000117889; -.
DR   KO; K03805; -.
DR   OMA; CPYCNMF; -.
DR   BioCyc; ECOL585395:ECO103_RS03195-MONOMER; -.
DR   Proteomes; UP000000959; Chromosome.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR   CDD; cd03020; DsbA_DsbC_DsbG; 1.
DR   Gene3D; 3.10.450.70; -; 1.
DR   InterPro; IPR033954; DiS-bond_Isoase_DsbC/G.
DR   InterPro; IPR009094; DiS-bond_isomerase_DsbC/G_N_sf.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   Pfam; PF13098; Thioredoxin_2; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   SUPFAM; SSF54423; SSF54423; 1.
PE   3: Inferred from homology;
DR   PRODOM; C8U2W9.
DR   SWISS-2DPAGE; C8U2W9.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
KW   Isomerase {ECO:0000313|EMBL:BAI29477.1};
KW   Periplasm {ECO:0000256|RuleBase:RU364038};
KW   Redox-active center {ECO:0000256|RuleBase:RU364038};
KW   Signal {ECO:0000256|RuleBase:RU364038}.
FT   SIGNAL        1     17       {ECO:0000256|RuleBase:RU364038}.
FT   CHAIN        18    248       Thiol:disulfide interchange protein.
FT                                {ECO:0000256|RuleBase:RU364038}.
FT                                /FTId=PRO_5010007646.
FT   DOMAIN      115    241       Thioredoxin-like_fold. {ECO:0000259|Pfam:
FT                                PF13098}.
SQ   SEQUENCE   248 AA;  27484 MW;  3F8D0C387143E36B CRC64;
     MLKKILLLAL LPAIAFAEEL PSPVKAIEKQ GITIIKTFDA PGGMKGYLGK YQDMGVTIYL
     TPDGKHAISG YMYNEKGENL SNTLIEKEIY APAGREMWQR MEQSHWLLDG KKDAPVIVYV
     FADPFCPYCK QFWQQARPWV DSGKVQLRTL LVGVIKPESP ATAAAILASK DPAKTWQEYE
     SSGGKLKLNV PANVSTEQMK VLSANEKLMD DLGANVTPAI YYMSKENTLQ QAVGLPDQKT
     LNIIMGNK
//

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