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 27-MAR-2024, entry version 100.
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; Bacillota; 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 KEGG; bce:BC0542; -.
DR PATRIC; fig|226900.8.peg.499; -.
DR HOGENOM; CLU_000288_47_1_9; -.
DR OrthoDB; 117402at2; -.
DR Proteomes; UP000001417; Chromosome.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR13887:SF55; DISULFIDE BOND FORMATION PROTEIN D; 1.
DR PANTHER; PTHR13887; GLUTATHIONE S-TRANSFERASE KAPPA; 1.
DR Pfam; PF13462; Thioredoxin_4; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 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
//
