AcoC

• Description: acetoin dehydrogenase E2 component (dihydrolipoamide acetyltransferase)
  
  

Gene name	acoC
Synonyms	yfjI
Essential	no
Product	acetoin dehydrogenase E2 component (dihydrolipoamide acetyltransferase)
Function	acetoin utilization
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 This image was kindly provided by SubtiList

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

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

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:

• Interactions:
  • (AcoA-AcoB)-AcoC-AcoL

• Localization: Membrane-proximal (Spotty) PubMed

Database entries

• Structure:

• UniProt: O31550

• KEGG entry: [3]

• E.C. number: 2.3.1.12

Expression and regulation

• Operon: acoA-acoB-acoC-acoL PubMed

• Sigma factor: SigL PubMed

• Regulation:
  • repressed by glucose (CcpA) PubMed
  • induced by acetoin (AcoR) PubMed
  • induced under anaerobic conditions (Fnr) PubMed

• Regulatory mechanism:
  • CcpA: transcription repression PubMed
  • AcoR: transcription activation (interaction with SigL-containing RNA polymerase) PubMed
  • Fnr: indirect positive regulation via NarG-NarH-NarJ-NarI PubMed

• 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

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

Jean-Christophe Meile, Ling Juan Wu, S Dusko Ehrlich, Jeff Errington, Philippe Noirot
Systematic localisation of proteins fused to the green fluorescent protein in Bacillus subtilis: identification of new proteins at the DNA replication factory.
Proteomics: 2006, 6(7);2135-46
[PubMed:16479537] [WorldCat.org] [DOI] (P p)

Heike Reents, Richard Münch, Thorben Dammeyer, Dieter Jahn, Elisabeth Härtig
The Fnr regulon of Bacillus subtilis.
J Bacteriol: 2006, 188(3);1103-12
[PubMed:16428414] [WorldCat.org] [DOI] (P p)

G Hambraeus, C von Wachenfeldt, L Hederstedt
Genome-wide survey of mRNA half-lives in Bacillus subtilis identifies extremely stable mRNAs.
Mol Genet Genomics: 2003, 269(5);706-14
[PubMed:12884008] [WorldCat.org] [DOI] (P p)

N O Ali, J Bignon, G Rapoport, M Debarbouille
Regulation of the acetoin catabolic pathway is controlled by sigma L in Bacillus subtilis.
J Bacteriol: 2001, 183(8);2497-504
[PubMed:11274109] [WorldCat.org] [DOI] (P p)

Y Miwa, A Nakata, A Ogiwara, M Yamamoto, Y Fujita
Evaluation and characterization of catabolite-responsive elements (cre) of Bacillus subtilis.
Nucleic Acids Res: 2000, 28(5);1206-10
[PubMed:10666464] [WorldCat.org] [DOI] (I p)

M Huang, F B Oppermann-Sanio, A Steinbüchel
Biochemical and molecular characterization of the Bacillus subtilis acetoin catabolic pathway.
J Bacteriol: 1999, 181(12);3837-41
[PubMed:10368162] [WorldCat.org] [DOI] (P p)