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BDBD_BACCR
ID   BDBD_BACCR              Reviewed;         216 AA.
AC   Q81I73;
DT   19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 94.
DE   RecName: Full=Probable disulfide bond formation protein D;
DE   AltName: Full=Disulfide oxidoreductase D;
DE   AltName: Full=Thiol-disulfide oxidoreductase D;
DE   Flags: Precursor;
GN   Name=bdbD; OrderedLocusNames=BC_0542;
OS   Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC
OS   15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=226900;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373
RC   / NCTC 2599 / NRRL B-3711;
RX   PubMed=12721630; DOI=10.1038/nature01582;
RA   Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V.,
RA   Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M.,
RA   Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G.,
RA   Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.;
RT   "Genome sequence of Bacillus cereus and comparative analysis with Bacillus
RT   anthracis.";
RL   Nature 423:87-91(2003).
CC   -!- FUNCTION: May be required for disulfide bond formation in some
CC       proteins. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the thioredoxin family. DsbA subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AE016877; AAP07563.1; -; Genomic_DNA.
DR   RefSeq; NP_830362.1; NC_004722.1.
DR   RefSeq; WP_000841307.1; NZ_CP034551.1.
DR   AlphaFoldDB; Q81I73; -.
DR   SMR; Q81I73; -.
DR   STRING; 226900.BC_0542; -.
DR   EnsemblBacteria; AAP07563; AAP07563; BC_0542.
DR   GeneID; 67505239; -.
DR   KEGG; bce:BC0542; -.
DR   PATRIC; fig|226900.8.peg.499; -.
DR   HOGENOM; CLU_000288_47_1_9; -.
DR   OMA; APEDRYF; -.
DR   Proteomes; UP000001417; Chromosome.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   Pfam; PF13462; Thioredoxin_4; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Oxidoreductase; Redox-active center; Reference proteome;
KW   Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..216
FT                   /note="Probable disulfide bond formation protein D"
FT                   /id="PRO_0000034271"
FT   DISULFID        65..68
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   216 AA;  24577 MW;  C943285CE9217B13 CRC64;
     MKSNKLMALG IVFSIAVLIV IGTIAYSIIN DKKDKGNEMF AYSTQQSLGK DDAPVKVVEF
     GDFKCPACRT WDVTVLPRLK EEYIDKGKVQ LYFINFPFIG KDSDLGAAAG EAIYKQDKDS
     FWIFYDEIYQ NQKKDTEEWI TEDLLLSIVK EKLPKVDVEQ FKKDLHSKDI KEKVSKDSDR
     AQKLKVQGAP SVYVNGNLAN PDFDSMKKAI DKELKK
 
 
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