ID   DSBC_DICD3              Reviewed;         238 AA.
AC   P39691; E0SLQ6;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Thiol:disulfide interchange protein DsbC;
DE   Flags: Precursor;
GN   Name=dsbC; OrderedLocusNames=Dda3937_02295;
OS   Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937)).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Dickeya.
OX   NCBI_TaxID=198628;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=3937;
RX   PubMed=8168497; DOI=10.1002/j.1460-2075.1994.tb06470.x;
RA   Shevchik V.E., Condemine G., Robert-Baudouy J.;
RT   "Characterization of DsbC, a periplasmic protein of Erwinia chrysanthemi
RT   and Escherichia coli with disulfide isomerase activity.";
RL   EMBO J. 13:2007-2012(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3937;
RX   PubMed=21217001; DOI=10.1128/jb.01513-10;
RA   Glasner J.D., Yang C.H., Reverchon S., Hugouvieux-Cotte-Pattat N.,
RA   Condemine G., Bohin J.P., Van Gijsegem F., Yang S., Franza T., Expert D.,
RA   Plunkett G. III, San Francisco M.J., Charkowski A.O., Py B., Bell K.,
RA   Rauscher L., Rodriguez-Palenzuela P., Toussaint A., Holeva M.C., He S.Y.,
RA   Douet V., Boccara M., Blanco C., Toth I., Anderson B.D., Biehl B.S.,
RA   Mau B., Flynn S.M., Barras F., Lindeberg M., Birch P.R., Tsuyumu S.,
RA   Shi X., Hibbing M., Yap M.N., Carpentier M., Dassa E., Umehara M.,
RA   Kim J.F., Rusch M., Soni P., Mayhew G.F., Fouts D.E., Gill S.R.,
RA   Blattner F.R., Keen N.T., Perna N.T.;
RT   "Genome sequence of the plant-pathogenic bacterium Dickeya dadantii 3937.";
RL   J. Bacteriol. 193:2076-2077(2011).
CC   -!- FUNCTION: Required for disulfide bond formation in some periplasmic
CC       proteins. Acts by transferring its disulfide bond to other proteins and
CC       is reduced in the process. DsbC is reoxidized by a yet uncharacterized
CC       protein. Also acts as a disulfide isomerase.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Periplasm.
CC   -!- SIMILARITY: Belongs to the thioredoxin family. DsbC subfamily.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X76687; CAA54108.1; -; Genomic_DNA.
DR   EMBL; CP002038; ADM96890.1; -; Genomic_DNA.
DR   PIR; S44444; S44444.
DR   RefSeq; WP_013316367.1; NC_014500.1.
DR   AlphaFoldDB; P39691; -.
DR   SMR; P39691; -.
DR   STRING; 198628.Dda3937_02295; -.
DR   EnsemblBacteria; ADM96890; ADM96890; Dda3937_02295.
DR   GeneID; 9732089; -.
DR   KEGG; ddd:Dda3937_02295; -.
DR   PATRIC; fig|198628.6.peg.693; -.
DR   eggNOG; COG1651; Bacteria.
DR   HOGENOM; CLU_083593_0_0_6; -.
DR   OMA; QMIVYKA; -.
DR   OrthoDB; 1678187at2; -.
DR   BioCyc; DDAD198628:DDA3937_RS03305-MON; -.
DR   Proteomes; UP000006859; Chromosome.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0015036; F:disulfide oxidoreductase activity; IEA:UniProt.
DR   CDD; cd03020; DsbA_DsbC_DsbG; 1.
DR   Gene3D; 3.10.450.70; -; 1.
DR   InterPro; IPR033954; DiS-bond_Isoase_DsbC/G.
DR   InterPro; IPR018950; DiS-bond_isomerase_DsbC/G_N.
DR   InterPro; IPR009094; DiS-bond_isomerase_DsbC/G_N_sf.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   Pfam; PF10411; DsbC_N; 1.
DR   Pfam; PF13098; Thioredoxin_2; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   SUPFAM; SSF54423; SSF54423; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Periplasm; Redox-active center; Reference proteome; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000250"
FT   CHAIN           22..238
FT                   /note="Thiol:disulfide interchange protein DsbC"
FT                   /id="PRO_0000034275"
FT   DOMAIN          61..232
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DISULFID        119..122
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ   SEQUENCE   238 AA;  25907 MW;  821012F0FC384A16 CRC64;
     MKKRVVLFSL LTLALSGVAR ADDAAIKQTL NRLGLQSAEV KDSPIGGMKT VLTENGVLYI
     TEDGKHLLQG PLYDVSGKTP VNVTNHILNE RLDALKDQMI VYKAPQEKHV ITVFTDITCG
     YCHKLHEQMK DYNALGITVR YLAYPRQGMN SQAAKDMQSI WCVADRNKAF DAAMKGDDVS
     PATCKTDIGA HYQLGVLFGV QGTPAIVLDD GTVVPGYQPP KEMMAMLDAH KASLKSGG