BDBB_BACSU
ID BDBB_BACSU Reviewed; 148 AA.
AC P68571; O31985; O64037;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=SPbeta prophage-derived disulfide bond formation protein B;
DE AltName: Full=Disulfide oxidoreductase B;
DE AltName: Full=Thiol-disulfide oxidoreductase B;
GN Name=bdbB; Synonyms=yolK; OrderedLocusNames=BSU21440;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9579063; DOI=10.1099/00221287-144-4-885;
RA Regamey A., Karamata D.;
RT "The N-acetylmuramoyl-L-alanine amidase encoded by the Bacillus subtilis
RT 168 prophage SP beta.";
RL Microbiology 144:885-893(1998).
RN [2]
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 [3]
RP IDENTIFICATION OF FUNCTION.
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 [4]
RP FUNCTION 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: Important but not absolutely essential for the production of
CC the lantibiotic sublancin 168, it may also be required for the
CC stability of other secreted proteins. Not required for competence for
CC DNA uptake. {ECO:0000269|PubMed:11872755}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the DsbB family. BdbC subfamily. {ECO:0000305}.
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DR EMBL; AF021803; AAC38303.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14062.1; -; Genomic_DNA.
DR RefSeq; NP_390027.1; NC_000964.3.
DR RefSeq; WP_009967541.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; P68571; -.
DR STRING; 224308.BSU21440; -.
DR PaxDb; P68571; -.
DR EnsemblBacteria; CAB14062; CAB14062; BSU_21440.
DR GeneID; 939128; -.
DR KEGG; bsu:BSU21440; -.
DR PATRIC; fig|224308.179.peg.2341; -.
DR eggNOG; COG1495; Bacteria.
DR OMA; WVNYFGF; -.
DR PhylomeDB; P68571; -.
DR BioCyc; BSUB:BSU21440-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR Gene3D; 1.20.1550.10; -; 1.
DR HAMAP; MF_00287; BdbC; 1.
DR InterPro; IPR003752; DiS_bond_form_DsbB/BdbC.
DR InterPro; IPR012187; Disulphide_bond_form_BdbC.
DR InterPro; IPR023380; DsbB-like_sf.
DR PANTHER; PTHR43469; PTHR43469; 1.
DR Pfam; PF02600; DsbB; 1.
DR PIRSF; PIRSF036659; BdbC; 1.
DR SUPFAM; SSF158442; SSF158442; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Chaperone; Disulfide bond; Electron transport; Membrane;
KW Oxidoreductase; Redox-active center; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..148
FT /note="SPbeta prophage-derived disulfide bond formation
FT protein B"
FT /id="PRO_0000059377"
FT TRANSMEM 7..26
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 41..60
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 67..84
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 111..135
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DISULFID 36..39
FT /note="Redox-active"
FT /evidence="ECO:0000250"
FT DISULFID 95..102
FT /note="Redox-active"
FT /evidence="ECO:0000250"
SQ SEQUENCE 148 AA; 17139 MW; 25676A3B9C9AF6DC CRC64;
MNTRYVKSFF LLLFFLSFFG TMASLFYSEI MHFKPCVLCW YQRIFLYPIP IILLIGLLKK
DLNSIFYVVF LSSIGLIIAF YHYIIQLTQS KSVVCEIGTN SCAKIEVEYL GFITLPLMSS
VCFALIFGIG LKLIIKSKKL KQNQHVYN
