Difference between revisions of "AcoC"

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* '''Effectors of protein activity:'''
 
* '''Effectors of protein activity:'''
  
* '''Interactions:'''
+
* '''Interactions:''' ([[AcoA]]-[[AcoB]])-[[AcoC]]-[[AcoL]]
  
 
* '''Localization:''' Membrane-proximal (Spotty) [http://www.ncbi.nlm.nih.gov/sites/entrez/16479537 PubMed]
 
* '''Localization:''' Membrane-proximal (Spotty) [http://www.ncbi.nlm.nih.gov/sites/entrez/16479537 PubMed]
Line 100: Line 100:
 
* '''Regulatory mechanism:'''  
 
* '''Regulatory mechanism:'''  
 
** [[CcpA]]: transcription repression {{PubMed|10666464}}
 
** [[CcpA]]: transcription repression {{PubMed|10666464}}
** [[AcoR]]: transcription activation (interaction with [[SigL]]-containing RNA polymerase) [http://www.ncbi.nlm.nih.gov/sites/entrez/11274109  PubMed]
+
** [[AcoR]]: transcription activation (interaction with [[SigL]]-containing [[RNA polymerase]]) [http://www.ncbi.nlm.nih.gov/sites/entrez/11274109  PubMed]
 
** [[Fnr]]: indirect positive regulation via [[NarG]]-[[NarH]]-[[NarJ]]-[[NarI]] {{PubMed|16428414}}
 
** [[Fnr]]: indirect positive regulation via [[NarG]]-[[NarH]]-[[NarJ]]-[[NarI]] {{PubMed|16428414}}
  

Revision as of 18:00, 21 August 2010

  • Description: acetoin dehydrogenase E2 component (dihydrolipoamide acetyltransferase)

Gene name acoC
Synonyms yfjI
Essential no
Product acetoin dehydrogenase E2 component (dihydrolipoamide acetyltransferase)
Function acetoin utilization
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







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:
  • Localization: Membrane-proximal (Spotty) PubMed

Database entries

  • Structure:
  • KEGG entry: [3]

Additional information

Expression and regulation

  • Additional information:the mRNA is very stable (half-life > 15 min) 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

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)