MurAA

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  • Description: UDP-N-acetylglucosamine 1-carboxyvinyltransferase

Gene name murAA
Synonyms murA
Essential yes PubMed
Product UDP-N-acetylglucosamine 1-carboxyvinyltransferase
Function peptidoglycan precursor biosynthesis
MW, pI 46 kDa, 5.45
Gene length, protein length 1308 bp, 436 aa
Immediate neighbours spoIID, ywmB
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
MurAA context.gif
This image was kindly provided by SubtiList



The gene

Basic information

  • Locus tag:

Phenotypes of a mutant

essential PubMed

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: Phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-D-glucosamine (according to Swiss-Prot)
  • Protein family: MurA subfamily (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:
  • Interactions:
  • Localization: cytoplasm (according to Swiss-Prot)

Database entries

  • Structure:

Additional information

  • subject to Clp-dependent proteolysis upon glucose starvation PubMed

MurAA is subject to ClpC-ClpP-dependent degradation PubMed

Expression and regulation

  • Operon:
  • Regulation:
  • Regulatory mechanism:
  • Additional information: subject to Clp-dependent proteolysis upon glucose starvation PubMed

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

  1. Gerth et al. (2008) Clp-dependent proteolysis down-regulates central metabolic pathways in glucose-starved Bacillus subtilis. J Bacteriol 190:321-331 PubMed
  2. Kock H, Gerth U, Hecker M. (2004) MurAA, catalysing the first committed step in peptidoglycan biosynthesis, is a target of Clp-dependent proteolysis in Bacillus subtilis. Mol Microbiol, 51:1087-1102. PubMed
  3. Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed