ID   DSBA_DICD3              Reviewed;         207 AA.
AC   P52234; E0SDU7;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Thiol:disulfide interchange protein DsbA;
DE   Flags: Precursor;
GN   Name=dsbA; OrderedLocusNames=Dda3937_01111;
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=7476168; DOI=10.1111/j.1365-2958.1995.tb02435.x;
RA   Shevchike V.E., Bortoli-German I., Robert-Baudouy J., Robinet S.,
RA   Barras F., Condemine G.;
RT   "Differential effect of dsbA and dsbC mutations on extracellular enzyme
RT   secretion in Erwinia chrysanthemi.";
RL   Mol. Microbiol. 16:745-753(1995).
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 such as PhoA or OmpA. Acts by transferring its disulfide bond
CC       to other proteins and is reduced in the process. DsbA is reoxidized by
CC       DsbB. It is required for pilus biogenesis.
CC   -!- SUBCELLULAR LOCATION: Periplasm.
CC   -!- SIMILARITY: Belongs to the thioredoxin family. DsbA 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; X75900; CAA53508.1; -; Genomic_DNA.
DR   EMBL; CP002038; ADM96239.1; -; Genomic_DNA.
DR   PIR; S77725; S77725.
DR   RefSeq; WP_013315728.1; NC_014500.1.
DR   AlphaFoldDB; P52234; -.
DR   SMR; P52234; -.
DR   STRING; 198628.Dda3937_01111; -.
DR   PRIDE; P52234; -.
DR   EnsemblBacteria; ADM96239; ADM96239; Dda3937_01111.
DR   GeneID; 9731406; -.
DR   KEGG; ddd:Dda3937_01111; -.
DR   PATRIC; fig|198628.6.peg.17; -.
DR   eggNOG; COG1651; Bacteria.
DR   HOGENOM; CLU_088255_3_0_6; -.
DR   OMA; NAIHKQK; -.
DR   OrthoDB; 1805428at2; -.
DR   BioCyc; DDAD198628:DDA3937_RS00100-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; cd03019; DsbA_DsbA; 1.
DR   InterPro; IPR001853; DSBA-like_thioredoxin_dom.
DR   InterPro; IPR023205; DsbA/DsbL.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   Pfam; PF01323; DSBA; 1.
DR   PIRSF; PIRSF001488; Tdi_protein; 1.
DR   SUPFAM; SSF52833; SSF52833; 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..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..207
FT                   /note="Thiol:disulfide interchange protein DsbA"
FT                   /id="PRO_0000034259"
FT   DOMAIN          20..149
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DISULFID        49..52
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ   SEQUENCE   207 AA;  22838 MW;  73396DB822EAE94D CRC64;
     MKKLWLALAG MVLAFSASAA DFSDGKQYAT LDKPVPQSPQ VLEFFSFYCP HCYQFAQVYH
     IPDAIQKALP ADAKLTKYHV DFLGELGKEL TQAWAVAIAL GVEDKVSPLM FDAVQKTQTV
     KQPQDIRQVF VAAGVKAEDY DSALNSFVVK SLVAQQEKAA ADLQLRGVPA VFVNGKYMIK
     SDGLDTSSMD NYVKQYADVV KFLLSQK