ID   DSBA_PSEAB              Reviewed;         211 AA.
AC   Q02DM0; P95460;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Thiol:disulfide interchange protein DsbA;
DE   Flags: Precursor;
GN   Name=dsbA; OrderedLocusNames=PA14_72450;
OS   Pseudomonas aeruginosa (strain UCBPP-PA14).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10051655; DOI=10.1073/pnas.96.5.2408;
RA   Tan M.-W., Rahme L.G., Sternberg J.A., Tompkins R.G., Ausubel F.M.;
RT   "Pseudomonas aeruginosa killing of Caenorhabditis elegans used to identify
RT   P. aeruginosa virulence factors.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:2408-2413(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCBPP-PA14;
RX   PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA   Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA   Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L., Grills G.,
RA   Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT   "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT   combinatorial.";
RL   Genome Biol. 7:R90.1-R90.14(2006).
CC   -!- FUNCTION: Involved in disulfide-bond formation. Acts by transferring
CC       its disulfide bond to other proteins (By similarity). {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; AF116282; AAD22452.1; -; Genomic_DNA.
DR   EMBL; CP000438; ABJ14875.1; -; Genomic_DNA.
DR   RefSeq; WP_003096976.1; NZ_CP034244.1.
DR   AlphaFoldDB; Q02DM0; -.
DR   BMRB; Q02DM0; -.
DR   SMR; Q02DM0; -.
DR   PRIDE; Q02DM0; -.
DR   EnsemblBacteria; ABJ14875; ABJ14875; PA14_72450.
DR   KEGG; pau:PA14_72450; -.
DR   HOGENOM; CLU_088255_1_0_6; -.
DR   OMA; EVVEFFW; -.
DR   BioCyc; PAER208963:G1G74-6095-MON; -.
DR   Proteomes; UP000000653; 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..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..211
FT                   /note="Thiol:disulfide interchange protein DsbA"
FT                   /id="PRO_0000271730"
FT   DOMAIN          23..203
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DISULFID        56..59
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   CONFLICT        209
FT                   /note="Missing (in Ref. 1)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   211 AA;  23375 MW;  A994F93CC8E8C9F6 CRC64;
     MRNLILTAML AMASLFGMAA QADDYTAGKE YVELSSPVPV SQPGKIEVVE LFWYGCPHCY
     AFEPTIVPWS EKLPADVHFV RLPALFGGIW NVHGQMFLTL ESMGVEHDVH NAVFEAIHKE
     HKKLATPEEM ADFLAGKGVD KEKFLSTYNS FAIKGQMEKA KKLAMAYQVT GVPTMVVNGK
     YRFDIGSAGG PEETLKLADY LIEKERAAAK K