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P68569 (BDBA_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 51. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

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

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.

Ontologies

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

Inferred from electronic annotation. Source: InterPro

glycerol ether metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionelectron carrier activity

Inferred from electronic annotation. Source: InterPro

protein disulfide oxidoreductase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

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

Sequences

Sequence LengthMass (Da)Tools
P68569 [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

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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AL009126 Genomic DNA. Translation: CAB14064.1.
RefSeqNP_390029.1. NC_000964.3.

3D structure databases

ProteinModelPortalP68569.
SMRP68569. Positions 34-135.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000001186; EBBACP00000001186; EBBACG00000001184.
GeneID939129.
GenomeReviewsGene locus BSU21460 in contig AL009126_GR.
KEGGbsu:BSU21460.
NMPDRfig|224308.1.peg.2152.
PATRIC18976097. VBIBacSub10457_2239.

Organism-specific databases

GenoListBSU21460. [Micado]

Phylogenomic databases

GeneTreeEBGT00050000003329.
HOGENOMHBG344106.
OMAFYNDINL.
PhylomeDBP68569.
ProtClustDBCLSK514409.

Enzyme and pathway databases

BioCycBSUB:BSU21460-MONOMER.

Family and domain databases

InterProIPR005746. Thioredoxin.
IPR012336. Thioredoxin-like_fold.
IPR013766. Thioredoxin_domain.
[Graphical view]
Gene3DG3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
PANTHERPTHR10438. Trx. 1 hit.
PfamPF00085. Thioredoxin. 1 hit.
[Graphical view]
SUPFAMSSF52833. Thiordxn-like_fd. 1 hit.
PROSITEPS00194. THIOREDOXIN_1. False negative.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

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: January 25, 2012
This is version 51 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Bacillus subtilis

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

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents