BDBD_BACSU
ID BDBD_BACSU Reviewed; 222 AA.
AC O32218;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Disulfide bond formation protein D;
DE AltName: Full=Disulfide oxidoreductase D;
DE AltName: Full=Thiol-disulfide oxidoreductase D;
DE Flags: Precursor;
GN Name=bdbD; Synonyms=yvgV; OrderedLocusNames=BSU33480;
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 DISRUPTION PHENOTYPE, AND MUTAGENESIS OF HIS-129.
RC STRAIN=168 / BGSC1A1;
RX PubMed=11844773; DOI=10.1128/jb.184.5.1423-1429.2002;
RA Erlendsson L.S., Hederstedt L.;
RT "Mutations in the thiol-disulfide oxidoreductases BdbC and BdbD can
RT suppress cytochrome c deficiency of CcdA-defective Bacillus subtilis
RT cells.";
RL J. Bacteriol. 184:1423-1429(2002).
RN [3]
RP FUNCTION IN PRODUCTION OF COMGC.
RC STRAIN=168;
RX PubMed=11744713; DOI=10.1074/jbc.m111380200;
RA Meima R., Eschevins C., Fillinger S., Bolhuis A., Hamoen L.W., Dorenbos R.,
RA Quax W.J., van Dijl J.M., Provvedi R., Chen I., Dubnau D., Bron S.;
RT "The bdbDC operon of Bacillus subtilis encodes thiol-disulfide
RT oxidoreductases required for competence development.";
RL J. Biol. Chem. 277:6994-7001(2002).
RN [4]
RP SUBCELLULAR LOCATION.
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=20713508; DOI=10.1101/gad.1945010;
RA Lopez D., Kolter R.;
RT "Functional microdomains in bacterial membranes.";
RL Genes Dev. 24:1893-1902(2010).
RN [5]
RP SUBCELLULAR LOCATION.
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=22882210; DOI=10.1111/j.1365-2958.2012.08205.x;
RA Yepes A., Schneider J., Mielich B., Koch G., Garcia-Betancur J.C.,
RA Ramamurthi K.S., Vlamakis H., Lopez D.;
RT "The biofilm formation defect of a Bacillus subtilis flotillin-defective
RT mutant involves the protease FtsH.";
RL Mol. Microbiol. 86:457-471(2012).
CC -!- FUNCTION: Required for the stabilization, possibly via formation of a
CC disulfide bond, of the obligatory competence protein ComGC. May be
CC required for the stability of secreted proteins with disulfide bonds.
CC Not required for sporulation. {ECO:0000269|PubMed:11744713}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20713508,
CC ECO:0000269|PubMed:22882210}. Membrane raft
CC {ECO:0000269|PubMed:20713508, ECO:0000269|PubMed:22882210}.
CC Note=Present in detergent-resistant membrane (DRM) fractions that may
CC be equivalent to eukaryotic membrane rafts; these rafts include
CC proteins involved in signaling, molecule trafficking and protein
CC secretion. {ECO:0000269|PubMed:20713508, ECO:0000269|PubMed:22882210}.
CC -!- DEVELOPMENTAL STAGE: A late competence gene, expression is enhanced in
CC the presence of ComK.
CC -!- DISRUPTION PHENOTYPE: Cells partially restore cytochrome c oxidase
CC activity in a CcdA-deficient mutant, possibly because the bacteria can
CC no longer oxidize the 2 heme-binding thiol groups in apocytochrome c.
CC {ECO:0000269|PubMed:11844773}.
CC -!- SIMILARITY: Belongs to the thioredoxin family. DsbA subfamily.
CC {ECO:0000305}.
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DR EMBL; AL009126; CAB15353.1; -; Genomic_DNA.
DR PIR; C70041; C70041.
DR RefSeq; NP_391228.1; NC_000964.3.
DR RefSeq; WP_003228414.1; NZ_JNCM01000033.1.
DR PDB; 3EU3; X-ray; 1.50 A; A=30-222.
DR PDB; 3EU4; X-ray; 2.30 A; A=30-222.
DR PDB; 3GH9; X-ray; 1.69 A; A=30-222.
DR PDB; 3GHA; X-ray; 1.40 A; A=30-222.
DR PDBsum; 3EU3; -.
DR PDBsum; 3EU4; -.
DR PDBsum; 3GH9; -.
DR PDBsum; 3GHA; -.
DR AlphaFoldDB; O32218; -.
DR SMR; O32218; -.
DR STRING; 224308.BSU33480; -.
DR jPOST; O32218; -.
DR PaxDb; O32218; -.
DR PRIDE; O32218; -.
DR EnsemblBacteria; CAB15353; CAB15353; BSU_33480.
DR GeneID; 936031; -.
DR KEGG; bsu:BSU33480; -.
DR PATRIC; fig|224308.179.peg.3633; -.
DR eggNOG; COG1651; Bacteria.
DR InParanoid; O32218; -.
DR OMA; APEDRYF; -.
DR PhylomeDB; O32218; -.
DR BioCyc; BSUB:BSU33480-MON; -.
DR EvolutionaryTrace; O32218; -.
DR PRO; PR:O32218; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0030420; P:establishment of competence for transformation; IEA:UniProtKB-KW.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF13462; Thioredoxin_4; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Competence; Disulfide bond; Membrane;
KW Oxidoreductase; Redox-active center; Reference proteome; Signal.
FT SIGNAL 1..36
FT /evidence="ECO:0000255"
FT CHAIN 37..222
FT /note="Disulfide bond formation protein D"
FT /id="PRO_0000034272"
FT DOMAIN 37..220
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DISULFID 69..72
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT MUTAGEN 129
FT /note="H->P: Partially restores cytochrome c synthesis in a
FT CcdA-deficient mutant, possibly because the bacteria can no
FT longer oxidize the 2 heme-binding thiol groups in
FT apocytochrome c."
FT /evidence="ECO:0000269|PubMed:11844773"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:3GHA"
FT STRAND 58..65
FT /evidence="ECO:0007829|PDB:3GHA"
FT HELIX 70..78
FT /evidence="ECO:0007829|PDB:3GHA"
FT HELIX 80..86
FT /evidence="ECO:0007829|PDB:3GHA"
FT TURN 87..91
FT /evidence="ECO:0007829|PDB:3GHA"
FT STRAND 92..99
FT /evidence="ECO:0007829|PDB:3GHA"
FT HELIX 104..120
FT /evidence="ECO:0007829|PDB:3GHA"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:3GHA"
FT HELIX 125..135
FT /evidence="ECO:0007829|PDB:3GHA"
FT STRAND 138..141
FT /evidence="ECO:0007829|PDB:3GHA"
FT HELIX 146..156
FT /evidence="ECO:0007829|PDB:3GHA"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:3GHA"
FT HELIX 161..170
FT /evidence="ECO:0007829|PDB:3GHA"
FT TURN 171..173
FT /evidence="ECO:0007829|PDB:3GHA"
FT HELIX 174..186
FT /evidence="ECO:0007829|PDB:3GHA"
FT STRAND 194..197
FT /evidence="ECO:0007829|PDB:3GHA"
FT HELIX 208..221
FT /evidence="ECO:0007829|PDB:3GHA"
SQ SEQUENCE 222 AA; 24905 MW; B1C91CA1995FBBC7 CRC64;
MKKKQQSSAK FAVILTVVVV VLLAAIVIIN NKTEQGNDAV SGQPSIKGQP VLGKDDAPVT
VVEFGDYKCP SCKVFNSDIF PKIQKDFIDK GDVKFSFVNV MFHGKGSRLA ALASEEVWKE
DPDSFWDFHE KLFEKQPDTE QEWVTPGLLG DLAKSTTKIK PETLKENLDK ETFASQVEKD
SDLNQKMNIQ ATPTIYVNDK VIKNFADYDE IKETIEKELK GK
