ID   DSBA_BURCE              Reviewed;         212 AA.
AC   Q9RHV8;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Thiol:disulfide interchange protein DsbA;
DE   Flags: Precursor;
GN   Name=dsbA;
OS   Burkholderia cepacia (Pseudomonas cepacia).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=KF1;
RX   PubMed=10711598; DOI=10.1111/j.1348-0421.2000.tb01244.x;
RA   Hayashi S., Abe M., Kimoto M., Furukawa S., Nakazawa T.;
RT   "The DsbA-DsbB disulfide bond formation system of Burkholderia cepacia is
RT   involved in the production of protease and alkaline phosphatase, motility,
RT   metal resistance, and multi-drug resistance.";
RL   Microbiol. Immunol. 44:41-50(2000).
CC   -!- FUNCTION: Involved in disulfide-bond formation. Acts by transferring
CC       its disulfide bond to other proteins. Involved in the production of
CC       protease and alkaline phosphatase, motility, metal resistance, and
CC       multi-drug resistance.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the thioredoxin family. DsbA subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AB012578; BAA89224.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9RHV8; -.
DR   SMR; Q9RHV8; -.
DR   STRING; 292.DM42_2150; -.
DR   eggNOG; COG1651; Bacteria.
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; IPR023205; DsbA/DsbL.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   Pfam; PF13462; Thioredoxin_4; 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..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..212
FT                   /note="Thiol:disulfide interchange protein DsbA"
FT                   /id="PRO_0000034251"
FT   DISULFID        58..61
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ   SEQUENCE   212 AA;  23233 MW;  4984916096593143 CRC64;
     MKKLLSTLLL SLGLAAGLAQ ASPAAPASGK DFEVMKSPQP VSAPAGKVEV IEFFWYGCPH
     CYEFEPTIEA WVKKQGNNID FKRVPVAFRD DFLPHSKLFY AVSALGISEK VTPAIFNAIH
     KQKNYLLTPQ AQADFLATQG VDKKKFMDAY NSFSVQGEVN QSAKLLKDYA IDGVPTVVVQ
     GKYKTGPAYT NSIPGTAQVL DFLVKQVQDK KL