ID   DSBA_ECO57              Reviewed;         208 AA.
AC   P0AEG5; P24991; Q46951; Q46952;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Thiol:disulfide interchange protein DsbA;
DE   Flags: Precursor;
GN   Name=dsbA; OrderedLocusNames=Z5392, ECs4783;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
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; AE005174; AAG59049.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB38206.1; -; Genomic_DNA.
DR   PIR; E86073; E86073.
DR   PIR; G91226; G91226.
DR   RefSeq; NP_312810.1; NC_002695.1.
DR   RefSeq; WP_000725337.1; NZ_SWKA01000005.1.
DR   AlphaFoldDB; P0AEG5; -.
DR   BMRB; P0AEG5; -.
DR   SMR; P0AEG5; -.
DR   STRING; 155864.EDL933_5175; -.
DR   EnsemblBacteria; AAG59049; AAG59049; Z5392.
DR   EnsemblBacteria; BAB38206; BAB38206; ECs_4783.
DR   GeneID; 66672234; -.
DR   GeneID; 915115; -.
DR   KEGG; ece:Z5392; -.
DR   KEGG; ecs:ECs_4783; -.
DR   PATRIC; fig|386585.9.peg.4992; -.
DR   eggNOG; COG1651; Bacteria.
DR   HOGENOM; CLU_088255_3_0_6; -.
DR   OMA; NAIHKQK; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; 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; Reference proteome; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000250"
FT   CHAIN           20..208
FT                   /note="Thiol:disulfide interchange protein DsbA"
FT                   /id="PRO_0000043367"
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;  23105 MW;  10527E876FCAEE55 CRC64;
     MKKIWLALAG LVLAFSASAA QYEDGKQYTT LEKPVAGAPQ VLEFFSFFCP HCYQFEEVLH
     ISDNVKKKLP EGVKMTKYHV NFMGGDLGKD LTQAWAVAMA LGVEDKVTVP LFEGVQKTQT
     IRSASDIRDV FINAGIKGEE YDAAWNSFVV KSLVAQQEKA AADVQLRGVP AMFVNGKYQL
     NPQGMDTSNM DVFVQQYADT VKYLSEKK