ID   DSBA_SALTI              Reviewed;         207 AA.
AC   Q9X6N0;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 134.
DE   RecName: Full=Thiol:disulfide interchange protein DsbA;
DE   Flags: Precursor;
GN   Name=dsbA; OrderedLocusNames=STY3883, t3623;
OS   Salmonella typhi.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=90370;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=5866;
RA   Mendoza del Cueto M.T., Rotger R.;
RT   "DsbA-like oxidoreductase from Salmonella typhi.";
RL   Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CT18;
RX   PubMed=11677608; DOI=10.1038/35101607;
RA   Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA   Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA   Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA   Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA   Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA   Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA   Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA   Barrell B.G.;
RT   "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT   serovar Typhi CT18.";
RL   Nature 413:848-852(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700931 / Ty2;
RX   PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA   Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA   Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT   "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT   CT18.";
RL   J. Bacteriol. 185:2330-2337(2003).
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 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Periplasm.
CC   -!- SIMILARITY: Belongs to the thioredoxin family. DsbA subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AF141380; AAD31509.1; -; Genomic_DNA.
DR   EMBL; AL513382; CAD03102.1; -; Genomic_DNA.
DR   EMBL; AE014613; AAO71124.1; -; Genomic_DNA.
DR   RefSeq; NP_458051.1; NC_003198.1.
DR   RefSeq; WP_000725369.1; NZ_WSUR01000010.1.
DR   AlphaFoldDB; Q9X6N0; -.
DR   SMR; Q9X6N0; -.
DR   STRING; 220341.16504739; -.
DR   EnsemblBacteria; AAO71124; AAO71124; t3623.
DR   KEGG; stt:t3623; -.
DR   KEGG; sty:STY3883; -.
DR   PATRIC; fig|220341.7.peg.3964; -.
DR   eggNOG; COG1651; Bacteria.
DR   HOGENOM; CLU_088255_3_0_6; -.
DR   OMA; NAIHKQK; -.
DR   Proteomes; UP000000541; Chromosome.
DR   Proteomes; UP000002670; 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; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000250"
FT   CHAIN           20..207
FT                   /note="Thiol:disulfide interchange protein DsbA"
FT                   /id="PRO_0000034265"
FT   DOMAIN          20..158
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;  22910 MW;  85D668B745FD3BE3 CRC64;
     MKKIWLALAG MVLAFSASAA QISDGKQYIT LDKPVAGEPQ VLEFFSFYCP HCYQFEEVLH
     VSDNVKKKLP KGTKMTKYHV EFLGPLGKEL TQAWAVAMAL GVEDKVTVPL FEAVQKTQTV
     QSAADIRKVF VDAGVKGEDY DAAWNSFVVK SLVAQQEKAA ADLQLQGVPA MFVNGKYQIN
     PQGMDTSSMD VFVQQYADTV KYLVDKK