Reviewed, UniProtKB/Swiss-Prot O32218 (BDBD_BACSU)

Names and origin

Protein names

Recommended name:
    Disulfide bond formation protein D
Alternative name(s):
    Disulfide oxidoreductase D
    Thiol-disulfide oxidoreductase D

Gene names

Name:	bdbD
Synonyms:	yvgV
Ordered Locus Names:	BSU33480

Organism

Bacillus subtilis [Complete proteome] [HAMAP]

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	222 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Required for the stabilization, possibly via formation of a disulfide bond, of the obligatory competence protein ComGC. May be required for the stability of secreted proteins with disulfide bonds. Not required for sporulation. Ref.3
Developmental stage	A late competence gene, expression is enhanced in the presence of comK.
Disruption phenotype	Cells partially restore cytochrome c oxidase activity in a ccdA-deficient mutant, possibly because the bacteria can no longer oxidize the 2 heme-binding thiol groups in apocytochrome c. Ref.2
Sequence similarities	Belongs to the thioredoxin family. DsbA subfamily. Contains 1 thioredoxin domain.

Ontologies

Keywords
Biological process	Competence
Domain	Redox-active center Signal
Molecular function	Oxidoreductase
PTM	Disulfide bond
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cell redox homeostasis Inferred from electronic annotation. Source: InterPro establishment of competence for transformation Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	outer membrane-bounded periplasmic space Inferred from electronic annotation. Source: InterPro
Molecular function	protein disulfide oxidoreductase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 36	36	Potential
	Chain	37 – 222	186	Disulfide bond formation protein D		PRO_0000034272
Regions
	Domain	37 – 220	184	Thioredoxin
Amino acid modifications
	Disulfide bond	69 ↔ 72		Redox-active Potential
Experimental info
	Mutagenesis	129	1	H → P: Partially restores cytochrome c synthesis in a ccdA-deficient mutant, possibly because the bacteria can no longer oxidize the 2 heme-binding thiol groups in apocytochrome c. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	O32218-1 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: B1C91CA1995FBBC7	FASTA	222	24,905
	10 20 30 40 50 60 MKKKQQSSAK FAVILTVVVV VLLAAIVIIN NKTEQGNDAV SGQPSIKGQP VLGKDDAPVT 70 80 90 100 110 120 VVEFGDYKCP SCKVFNSDIF PKIQKDFIDK GDVKFSFVNV MFHGKGSRLA ALASEEVWKE 130 140 150 160 170 180 DPDSFWDFHE KLFEKQPDTE QEWVTPGLLG DLAKSTTKIK PETLKENLDK ETFASQVEKD 190 200 210 220 SDLNQKMNIQ ATPTIYVNDK VIKNFADYDE IKETIEKELK GK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A. Nature 390:249-256(1997) [PubMed: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.
[2]	"Mutations in the thiol-disulfide oxidoreductases BdbC and BdbD can suppress cytochrome c deficiency of CcdA-defective Bacillus subtilis cells." Erlendsson L.S., Hederstedt L. J. Bacteriol. 184:1423-1429(2002) [PubMed: 11844773] [Abstract] Cited for: DISRUPTION PHENOTYPE, MUTAGENESIS OF HIS-129. Strain: 168 / BGSC1A1.
[3]	"The bdbDC operon of Bacillus subtilis encodes thiol-disulfide oxidoreductases required for competence development." Meima R., Eschevins C., Fillinger S., Bolhuis A., Hamoen L.W., Dorenbos R., Quax W.J., van Dijl J.M., Provvedi R., Chen I., Dubnau D., Bron S. J. Biol. Chem. 277:6994-7001(2002) [PubMed: 11744713] [Abstract] Cited for: FUNCTION IN PRODUCTION OF COMGC. Strain: 168.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AL009126 Genomic DNA. Translation: CAB15353.1.
PIR	C70041.
RefSeq	NP_391228.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	936031.
GenomeReviews	Gene locus BSU33480 in contig AL009126_GR.
KEGG	bsu:BSU33480.
NMPDR	fig|224308.1.peg.3354.
Organism-specific databases
SubtiList	BG14104. bdbD. [Micado]
CMR	Search...
Phylogenomic databases
HOGENOM	O32218.
OMA	O32218. PPKAHIP.
Enzyme and pathway databases
BioCyc	BSUB224308:BSU3345-MON.
Family and domain databases
InterPro	IPR001853. OxRdtase_DSBA. IPR017936. Thioredoxin-like. IPR017937. Thioredoxin_CS. IPR012335. Thioredoxin_fold. [Graphical view]
Gene3D	G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
Pfam	PF01323. DSBA. 1 hit. [Graphical view]
PROSITE	PS00194. THIOREDOXIN_1. False negative. PS51352. THIOREDOXIN_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

BDBD_BACSU

Accession

Primary (citable) accession number: O32218

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 19, 2003
Last sequence update:	January 1, 1998
Last modified:	June 16, 2009
This is version 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)