AcoC

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  • Description: acetoin dehydrogenase E2 component (dihydrolipoamide acetyltransferase)

Gene name acoC
Synonyms yfjI
Essential no
Product acetoin dehydrogenase E2 component (dihydrolipoamide acetyltransferase)
Function acetoin utilization
Gene expression levels in SubtiExpress: acoC
Interactions involving this protein in SubtInteract: AcoC
Metabolic function and regulation of this protein in SubtiPathways:
Central C-metabolism
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
Expression at a glance   PubMed
AcoC expression.png




























Categories containing this gene/protein

utilization of specific carbon sources

This gene is a member of the following regulons

AcoR regulon, CcpA regulon, SigL regulon

The gene

Basic information

  • Locus tag: BSU08080

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: Acetyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-acetyldihydrolipoyl)lysine (according to Swiss-Prot)
  • 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:

Database entries

  • Structure:
  • KEGG entry: [3]

Additional information

Expression and regulation

  • Additional information:
    • the mRNA is very stable (half-life > 15 min) PubMed
    • the mRNA is substantially stabilized upon depletion of RNase Y PubMed

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

Lehnik-Habrink M, Schaffer M, Mäder U, Diethmaier C, Herzberg C, Stülke J  
RNA processing in Bacillus subtilis: identification of targets of the essential RNase Y. 
Mol Microbiol. 2011 81(6): 1459-1473. 
PubMed:21815947