Difference between revisions of "AcoC"

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Line 80: Line 80:
 
* '''Swiss prot entry:''' [http://www.uniprot.org/uniprot/O31550 O31550]
 
* '''Swiss prot entry:''' [http://www.uniprot.org/uniprot/O31550 O31550]
  
* '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu+BSU08080]
+
* '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu+BSU08080 BSU08080]
  
 
* '''E.C. number:''' [http://www.expasy.org/enzyme/2.3.1.12 2.3.1.12]
 
* '''E.C. number:''' [http://www.expasy.org/enzyme/2.3.1.12 2.3.1.12]

Revision as of 21:48, 13 May 2009

  • Description: acetoin dehydrogenase E2 component (dihydrolipoamide acetyltransferase)

Gene name acoC
Synonyms yfjI
Essential no
Product acetoin dehydrogenase E2 component (dihydrolipoamide acetyltransferase)
Function acetoin utilization
MW, pI 42 kDa, 6.524
Gene length, protein length 1194 bp, 398 aa
Immediate neighbours acoB, acoL
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
AcoC context.gif
This image was kindly provided by SubtiList



The gene

Basic information

  • Coordinates:

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family: lipoyl-binding domain (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:
  • Interactions:
  • Localization: Membrane-proximal (Spotty) PubMed

Database entries

  • Structure:

Additional information

Expression and regulation

  • Regulation: repressed by glucose (CcpA) , induced by acetoin (AcoR) PubMed
  • Regulatory mechanism: CcpA: transcription repression, AcoR: transcription activation (interaction with SigL-containing RNA polymerase) PubMed
  • Additional information:

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Michel Debarbouille, Pasteur Institute, Paris, France Homepage

Your additional remarks

References

  1. Meile et al. (2006) Systematic localisation of proteins fused to the green fluorescent protein in Bacillus subtilis: identification of new proteins at the DNA replication factory Proteomics 6: 2135-2146. PubMed
  2. Ali, N. O., Bignon, J., Rapoport, G., and Débarbouillé, M. (2001) Regulation of the acetoin catabolic pathway is controlled by sigma L in Bacillus subtilis. J. Bacteriol. 183, 2497-2504. PubMed
  3. Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed