ID   DSBA_ECO27              Reviewed;         208 AA.
AC   P0A4L6; B7UNI3; P59589;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Thiol:disulfide interchange protein DsbA;
DE   Flags: Precursor;
GN   Name=dsbA; OrderedLocusNames=E2348C_4167;
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8878041; DOI=10.1046/j.1365-2958.1996.431403.x;
RA   Zhang H.Z., Donnenberg M.S.;
RT   "DsbA is required for stability of the type IV pilin of enteropathogenic
RT   Escherichia coli.";
RL   Mol. Microbiol. 21:787-797(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC;
RX   PubMed=18952797; DOI=10.1128/jb.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T., Henderson I.R.,
RA   Harris D., Asadulghani M., Kurokawa K., Dean P., Kenny B., Quail M.A.,
RA   Thurston S., Dougan G., Hayashi T., Parkhill J., Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(2009).
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; Z54203; CAA90910.1; -; Genomic_DNA.
DR   EMBL; FM180568; CAS11715.1; -; Genomic_DNA.
DR   RefSeq; WP_000725344.1; NC_011601.1.
DR   AlphaFoldDB; P0A4L6; -.
DR   BMRB; P0A4L6; -.
DR   SMR; P0A4L6; -.
DR   EnsemblBacteria; CAS11715; CAS11715; E2348C_4167.
DR   GeneID; 67417257; -.
DR   KEGG; ecg:E2348C_4167; -.
DR   HOGENOM; CLU_088255_3_0_6; -.
DR   OMA; NAIHKQK; -.
DR   Proteomes; UP000008205; 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..208
FT                   /note="Thiol:disulfide interchange protein DsbA"
FT                   /id="PRO_0000034253"
FT   DOMAIN          20..150
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   208 AA;  23119 MW;  01527E876ECAEE92 CRC64;
     MKKIWLALAG LVLAFSASAA QYEDGKQYTT LEKPVAGAPQ VLEFFSFFCP HCYQFEEVLH
     ISDNVKKKLP EGVKMTKYHV NFMGGDLGKE LTQAWAVAMA LGVEDKVTVP LFEGVQKTQT
     IRSASDIRDV FINAGIKGEE YDAAWNSFVV KSLVAQQEKA AADVQLRGVP AMFVNGKYQL
     NPQGMDTSNM DVFVQQYADT VKYLSEKK