P0CI75 (BIRA_BACSU) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 23.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Bifunctional protein BirA Including the following 2 domains:
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| Gene names |
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| Organism | Bacillus subtilis (strain 168) [Reference proteome] [HAMAP] | ||||
| Taxonomic identifier | 224308 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › ![]() |
Protein attributes
| Sequence length | 325 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | BirA acts both as a biotin-operon repressor and as the enzyme that synthesizes the corepressor, acetyl-CoA:carbon-dioxide ligase. This protein also activates biotin to form biotinyl-5'-adenylate and transfers the biotin moiety to biotin-accepting proteins By similarity. |
| Catalytic activity | ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)] = AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]. |
| Sequence similarities | Belongs to the biotin--protein ligase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Transcription Transcription regulation |
| Ligand | ATP-binding Biotin DNA-binding Nucleotide-binding |
| Molecular function | Ligase Repressor |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | cellular protein modification process Inferred from electronic annotation. Source: InterPro regulation of transcription, DNA-dependentInferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependentInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular_function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW DNA bindingInferred from electronic annotation. Source: UniProtKB-KW biotin-[acetyl-CoA-carboxylase] ligase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 325 | 325 | Bifunctional protein BirA | PRO_0000064931 | |||||
Regions | |||||||||
| DNA binding | 23 – 42 | 20 | H-T-H motif Potential | ||||||
Experimental info | |||||||||
| Mutagenesis | 23 | 1 | G → S: Deregulation of biotin synthesis. Ref.1 | ||||||
| Mutagenesis | 38 | 1 | W → R: Deregulation of biotin synthesis. Ref.1 | ||||||
| Mutagenesis | 58 | 1 | G → E: Deregulation of biotin synthesis. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Cloning and characterization of the Bacillus subtilis birA gene encoding a repressor of the biotin operon." Bower S., Perkins J.P., Yocum R.R., Serror P., Sorokin A.V., Rahaim P., Howitt C.L., Prasad N., Ehrlich S.D., Pero J. J. Bacteriol. 177:2572-2575(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF GLY-23; TRP-38 AND GLY-58. Strain: 168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB 3610 / VKM B-501. |
| [2] | "Sequence analysis of the Bacillus subtilis chromosome region between the serA and kdg loci cloned in a yeast artificial chromosome." Sorokin A.V., Azevedo V., Zumstein E., Galleron N., Ehrlich S.D., Serror P. Microbiology 142:2005-2016(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB 3610 / VKM B-501. |
| [3] | "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. Danchin A.Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168. |
Cross-references
Sequence databases | |
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| EMBL GenBank DDBJ | L38424 Genomic DNA. Translation: AAA92879.1. Sequence problems. L47709 Genomic DNA. Translation: AAB38447.1. AL009126 Genomic DNA. Translation: CAB14160.1. |
| PIR | A69595. |
| RefSeq | NP_390125.1. NC_000964.3. |
3D structure databases | |
| ProteinModelPortal | P0CI75. |
| SMR | P0CI75. Positions 3-324. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | CAB14160; CAB14160; BSU22440. |
| GeneID | 939028. |
| KEGG | bsu:BSU22440. |
| PATRIC | 18976297. VBIBacSub10457_2339. |
Organism-specific databases | |
| GenoList | BSU22440. [Micado] |
Phylogenomic databases | |
| HOGENOM | HOG000041811. |
| KO | K03524. |
| OMA | AVWKHIE. |
Family and domain databases | |
| Gene3D | 1.10.10.10. 1 hit. |
| InterPro | IPR004408. Biotin_CoA_COase_ligase. IPR004409. Biotin_operon_repress_HTH. IPR003142. BPL_C. IPR004143. BPL_LipA_LipB. IPR013196. HTH_11. IPR011991. WHTH_DNA-bd_dom. [Graphical view] |
| PANTHER | PTHR12835. PTHR12835. 1 hit. |
| Pfam | PF02237. BPL_C. 1 hit. PF03099. BPL_LplA_LipB. 1 hit. PF08279. HTH_11. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR00121. birA_ligase. 1 hit. TIGR00122. birA_repr_reg. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | BIRA_BACSU | ||||||||
| Accession | Primary (citable) accession number: P0CI75 Secondary accession number(s): P42975 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic 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 |

Clusters with
