ID   DSBA_SALEN              Reviewed;         207 AA.
AC   P0A2I0; O30848; O69191;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Thiol:disulfide interchange protein DsbA;
DE   Flags: Precursor;
GN   Name=dsbA;
OS   Salmonella enteritidis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=149539;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=82139;
RA   Mendoza-del-Cueto M.T., Rotger-Anglada R.;
RL   Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
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 {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the thioredoxin family. DsbA subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AF067152; AAC17906.1; -; Genomic_DNA.
DR   RefSeq; WP_000725364.1; NZ_WIAP01000016.1.
DR   AlphaFoldDB; P0A2I0; -.
DR   SMR; P0A2I0; -.
DR   PATRIC; fig|149539.316.peg.4079; -.
DR   OMA; NAIHKQK; -.
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_0000034264"
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;  22911 MW;  8260C50145FD3655 CRC64;
     MKKIWLALAG MVLAFSASAA QISDGKQYIT LDKPVAGEPQ VLEFFSFYCP HCYQFEEVLH
     VSDNVKKKLP EGTKMTKYHV EFLGPLGKEL TQAWAVAMAL GVEDKVTVPL FEAVQKTQTV
     QSAADIRKVF VDAGVKGEDY DAAWNSFVVK SLVAQQEKAA ADLQLQGVPA MFVNGKYQIN
     PQGMDTSSMD VFVQQYADTV KYLVDKK