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
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 This image was kindly provided by SubtiList
Expression at a glance   PubMed

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

• Expression browser: acoC 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)