ID   DSBA_PECCC              Reviewed;         207 AA.
AC   Q9RB10;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Thiol:disulfide interchange protein DsbA;
DE   Flags: Precursor;
GN   Name=dsbA;
OS   Pectobacterium carotovorum subsp. carotovorum (Erwinia carotovora subsp.
OS   carotovora).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=555;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=SCRI 193;
RX   PubMed=10463161; DOI=10.1099/13500872-145-8-1945;
RA   Vincent-Sealy L.V., Thomas J.D., Commander P., Salmond G.P.C.;
RT   "Erwinia carotovora DsbA mutants: evidence for a periplasmic-stress signal
RT   transduction system affecting transcription of genes encoding secreted
RT   proteins.";
RL   Microbiology 145:1945-1958(1999).
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}.
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DR   EMBL; AF146615; AAD47613.1; -; Genomic_DNA.
DR   RefSeq; WP_010298113.1; NZ_VBUA01000002.1.
DR   AlphaFoldDB; Q9RB10; -.
DR   SMR; Q9RB10; -.
DR   GeneID; 61350201; -.
DR   PATRIC; fig|555.16.peg.4018; -.
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:0000255"
FT   CHAIN           20..207
FT                   /note="Thiol:disulfide interchange protein DsbA"
FT                   /id="PRO_0000034258"
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;  23078 MW;  18BC5256E1EC414F CRC64;
     MKKLWFALIG VVLAFSASAA EFSDGKQYVE LDKPATQEPQ VLEFFSFYCP HCYQFEQVYH
     VPDAVKKALP EGTKMTRYHV DFLGPLGKNL TQAWAVAMAL GVEDKITPLM FDAVQKTQTV
     QKPEDIREVF VKAGVSAEEF DGALNSFVVK SLVAQQEKAA ADLQLRGVPA MFVNGKYMIK
     NDGLDTSSMD GYVKQYADVV KFLITKK