Difference between revisions of "AcoC"

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Revision as of 12:47, 16 May 2013

  • 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
Sequences Protein DNA DNA_with_flanks
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