ID   DSBA_HAEIN              Reviewed;         205 AA.
AC   P31810;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=Thiol:disulfide interchange protein DsbA;
DE   Flags: Precursor;
GN   Name=dsbA; Synonyms=por; OrderedLocusNames=HI_0846;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=1438213; DOI=10.1073/pnas.89.21.10252;
RA   Tomb J.-F.;
RT   "A periplasmic protein disulfide oxidoreductase is required for
RT   transformation of Haemophilus influenzae Rd.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:10252-10256(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
CC   -!- FUNCTION: Involved in disulfide-bond formation. Required for HI
CC       transformation. Acts by transferring its disulfide bond to other
CC       proteins.
CC   -!- SUBCELLULAR LOCATION: Periplasm.
CC   -!- SIMILARITY: Belongs to the thioredoxin family. DsbA subfamily.
CC       {ECO:0000305}.
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DR   EMBL; M94205; AAA24956.1; -; Genomic_DNA.
DR   EMBL; L42023; AAC22503.1; -; Genomic_DNA.
DR   PIR; B64098; B46411.
DR   RefSeq; NP_439006.1; NC_000907.1.
DR   RefSeq; WP_005693196.1; NC_000907.1.
DR   AlphaFoldDB; P31810; -.
DR   SMR; P31810; -.
DR   STRING; 71421.HI_0846; -.
DR   EnsemblBacteria; AAC22503; AAC22503; HI_0846.
DR   KEGG; hin:HI_0846; -.
DR   PATRIC; fig|71421.8.peg.887; -.
DR   eggNOG; COG1651; Bacteria.
DR   HOGENOM; CLU_088255_3_0_6; -.
DR   OMA; AVEFFWY; -.
DR   PhylomeDB; P31810; -.
DR   BioCyc; HINF71421:G1GJ1-886-MON; -.
DR   Proteomes; UP000000579; 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..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..205
FT                   /note="Thiol:disulfide interchange protein DsbA"
FT                   /id="PRO_0000034260"
FT   DOMAIN          23..201
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DISULFID        52..55
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ   SEQUENCE   205 AA;  22964 MW;  37469B216976969C CRC64;
     MKKVLLALGL GVSTLMSVNS FAADLQEGKQ YVQVSQQASQ QKEVIEFFSF YCPHCYAFEM
     EYKIPQQVVD ALPKDVKFKQ YHVNFLGHQS ENLTRAWALA MALGAESKVK SPLFEAAQKD
     ALKSMDDIRA IFLSNGITAE QFDGGINSFA VNGLVNKQVN AAEQFKVRGV PDFYVNGKFR
     VNPEGLNYDD FVKDYVQTVK GLLQK