BDBA_BACSU
ID BDBA_BACSU Reviewed; 137 AA.
AC P68569; O31987; O64035;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=SPbeta prophage-derived disulfide bond formation protein A;
DE AltName: Full=Disulfide oxidoreductase A;
DE AltName: Full=Thiol-disulfide oxidoreductase A;
DE Flags: Precursor;
GN Name=bdbA; Synonyms=yolI; OrderedLocusNames=BSU21460;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [2]
RP IDENTIFICATION.
RC STRAIN=168;
RX PubMed=10455116; DOI=10.1074/jbc.274.35.24531;
RA Bolhuis A., Venema G., Quax W.J., Bron S., van Dijl J.M.;
RT "Functional analysis of paralogous thiol-disulfide oxidoreductases in
RT Bacillus subtilis.";
RL J. Biol. Chem. 274:24531-24538(1999).
RN [3]
RP HAS NO ROLE IN PRODUCTION OF SUBLANCIN 168.
RC STRAIN=168;
RX PubMed=11872755; DOI=10.1074/jbc.m201158200;
RA Dorenbos R., Stein T., Kabel J., Bruand C., Bolhuis A., Bron S., Quax W.J.,
RA Van Dijl J.M.;
RT "Thiol-disulfide oxidoreductases are essential for the production of the
RT lantibiotic sublancin 168.";
RL J. Biol. Chem. 277:16682-16688(2002).
CC -!- FUNCTION: Unknown; dispensable for production of the lantibiotic
CC sublancin 168 and for competence for DNA uptake.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the thioredoxin family. {ECO:0000305}.
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DR EMBL; AL009126; CAB14064.1; -; Genomic_DNA.
DR RefSeq; NP_390029.1; NC_000964.3.
DR RefSeq; WP_003230920.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; P68569; -.
DR SMR; P68569; -.
DR STRING; 224308.BSU21460; -.
DR PaxDb; P68569; -.
DR PRIDE; P68569; -.
DR EnsemblBacteria; CAB14064; CAB14064; BSU_21460.
DR GeneID; 939129; -.
DR KEGG; bsu:BSU21460; -.
DR PATRIC; fig|224308.179.peg.2343; -.
DR eggNOG; COG0526; Bacteria.
DR InParanoid; P68569; -.
DR OMA; KANWITA; -.
DR PhylomeDB; P68569; -.
DR BioCyc; BSUB:BSU21460-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IBA:GO_Central.
DR GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF00085; Thioredoxin; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Disulfide bond; Oxidoreductase; Redox-active center; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..137
FT /note="SPbeta prophage-derived disulfide bond formation
FT protein A"
FT /id="PRO_0000034282"
FT DOMAIN 26..136
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DISULFID 58..61
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ SEQUENCE 137 AA; 16182 MW; 13649E43C8C6D443 CRC64;
MKKWIVLFLV LIAAAISIFV YVSTGSEKPF YNDINLTQYQ KEVDSKKPKF IYVYETSCPP
CQEIKPELNE VIKKEKLKVQ ALNIEEKENY NTEFLDKYNL NKTPTILYYK DGKEKDRLEG
YRSASQIEKF FDKNGDR
