ID   DSBA_BUCAI              Reviewed;         212 AA.
AC   P57505;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 1.
DT   27-MAR-2024, entry version 103.
DE   RecName: Full=Thiol:disulfide interchange protein DsbA;
DE   Flags: Precursor;
GN   Name=dsbA; OrderedLocusNames=BU430;
OS   Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS   pisum symbiotic bacterium).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=107806;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=APS;
RX   PubMed=10993077; DOI=10.1038/35024074;
RA   Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT   "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT   sp. APS.";
RL   Nature 407:81-86(2000).
CC   -!- FUNCTION: Involved in disulfide-bond formation. Acts by transferring
CC       its disulfide bond to other proteins (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the thioredoxin family. DsbA subfamily.
CC       {ECO:0000305}.
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DR   EMBL; BA000003; BAB13128.1; -; Genomic_DNA.
DR   RefSeq; NP_240242.1; NC_002528.1.
DR   RefSeq; WP_009874383.1; NC_002528.1.
DR   AlphaFoldDB; P57505; -.
DR   SMR; P57505; -.
DR   STRING; 563178.BUAP5A_423; -.
DR   EnsemblBacteria; BAB13128; BAB13128; BAB13128.
DR   KEGG; buc:BU430; -.
DR   PATRIC; fig|107806.10.peg.439; -.
DR   eggNOG; COG1651; Bacteria.
DR   HOGENOM; CLU_088255_3_0_6; -.
DR   Proteomes; UP000001806; Chromosome.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   CDD; cd03019; DsbA_DsbA; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 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   PANTHER; PTHR35891; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBA; 1.
DR   PANTHER; PTHR35891:SF2; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBA; 1.
DR   Pfam; PF01323; DSBA; 1.
DR   PIRSF; PIRSF001488; Tdi_protein; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Redox-active center; Reference proteome; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..212
FT                   /note="Thiol:disulfide interchange protein DsbA"
FT                   /id="PRO_0000034248"
FT   DISULFID        49..52
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   212 AA;  25159 MW;  42DC3FD02DC2331D CRC64;
     MKKILIILCI LILSCNVFSC EFKNGREYTE KHKVISNIPS IIEFFSFFCP YCYEFEKTYD
     TQYLIEKKIK KNINIQKYHV SFLGGKLGYV LTKSWIIAQQ MGIEKKIVLP IFKGIQETYT
     INNLDDIKKI FKEKAGVSES KFNSFWNSLT IKILISKQEE DIRKYNLKNI PTMLINEKYV
     IDYSKIEEIF KDSFAEKYTK LIQFLINKKE KI
//