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Reviewed, UniProtKB/Swiss-Prot P68569 (BDBA_BACSU)

Last modified June 16, 2009. Version 32. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    SPBc2 prophage-derived disulfide bond formation protein A
Alternative name(s):
    Disulfide oxidoreductase A
    Thiol-disulfide oxidoreductase A
Gene names
Name: bdbA
Synonyms: yolI
Ordered Locus Names: BSU21460
OrganismBacillus subtilis [Complete proteome] [HAMAP]
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

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Protein attributes

Sequence length137 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology.

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General annotation (Comments)

Function

Unknown; dispensable for production of the lantibiotic sublancin 168 and for competence for DNA uptake. Ref.3

Subcellular location

Secreted Potential.

Sequence similarities

Belongs to the thioredoxin family.

Contains 1 thioredoxin domain.

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Ontologies

Keywords
   Cellular componentSecreted
   DomainRedox-active center
Signal
   Molecular functionOxidoreductase
   PTMDisulfide bond
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processcell redox homeostasis

Inferred from electronic annotation. Source: InterPro

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionoxidoreductase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 Potential
Chain26 – 137112SPBc2 prophage-derived disulfide bond formation protein A
PRO_0000034282

Regions

Domain26 – 136111Thioredoxin

Amino acid modifications

Disulfide bond58 ↔ 61Redox-active Potential

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Sequences

Sequence LengthMass (Da)Tools
P68569-1 [UniParc].

Last modified December 7, 2004. Version 1.
Checksum: 13649E43C8C6D443

FASTA13716,182
        10         20         30         40         50         60 
MKKWIVLFLV LIAAAISIFV YVSTGSEKPF YNDINLTQYQ KEVDSKKPKF IYVYETSCPP 

        70         80         90        100        110        120 
CQEIKPELNE VIKKEKLKVQ ALNIEEKENY NTEFLDKYNL NKTPTILYYK DGKEKDRLEG 

       130 
YRSASQIEKF FDKNGDR

« Hide

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References

« Hide '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. expand/collapse author list , 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]"Functional analysis of paralogous thiol-disulfide oxidoreductases in Bacillus subtilis."
Bolhuis A., Venema G., Quax W.J., Bron S., van Dijl J.M.
J. Biol. Chem. 274:24531-24538(1999) [PubMed: 10455116] [Abstract]
Cited for: IDENTIFICATION.
Strain: 168.
[3]"Thiol-disulfide oxidoreductases are essential for the production of the lantibiotic sublancin 168."
Dorenbos R., Stein T., Kabel J., Bruand C., Bolhuis A., Bron S., Quax W.J., Van Dijl J.M.
J. Biol. Chem. 277:16682-16688(2002) [PubMed: 11872755] [Abstract]
Cited for: HAS NO ROLE IN PRODUCTION OF SUBLANCIN 168.
Strain: 168.

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Cross-references

Sequence databases

AL009126 Genomic DNA. Translation: CAB14064.1.
RefSeqNP_390029.1.

3D structure databases

HSSPHSSP built from PDB template 1T7P based on UniProtKB P00274.
ModBaseSearch...

Genome annotation databases

GeneID939129.
GenomeReviewsGene locus BSU21460 in contig AL009126_GR.
KEGGbsu:BSU21460.
NMPDRfig|224308.1.peg.2152.

Organism-specific databases

SubtiListBG13585. bdbA. [Micado]
CMRSearch...

Phylogenomic databases

HOGENOMP68569.
OMAP68569. ISTSENQ.

Enzyme and pathway databases

BioCycBSUB224308:BSU2147-MON.

Family and domain databases

InterProIPR017936. Thioredoxin-like.
IPR015467. Thioredoxin_core.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
IPR012335. Thioredoxin_fold.
[Graphical view]
Gene3DG3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
PANTHERPTHR10438. Trx. 1 hit.
PfamPF00085. Thioredoxin. 1 hit.
[Graphical view]
PROSITEPS00194. THIOREDOXIN_1. False negative.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameBDBA_BACSU
AccessionPrimary (citable) accession number: P68569
Secondary accession number(s): O31987, O64035
Entry history
Integrated into UniProtKB/Swiss-Prot: December 7, 2004
Last sequence update: December 7, 2004
Last modified: June 16, 2009
This is version 32 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents