MurAA

• Description: UDP-N-acetylglucosamine 1-carboxyvinyltransferase
  
  

Gene name	murAA
Synonyms	murA
Essential	yes PubMed
Product	UDP-N-acetylglucosamine 1-carboxyvinyltransferase
Function	peptidoglycan precursor biosynthesis
Metabolic function and regulation of this protein in SubtiPathways: Cell wall
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 This image was kindly provided by SubtiList

The gene

Basic information

• Locus tag: BSU36760

Phenotypes of a mutant

essential PubMed

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

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:

• UniProt: P70965

• KEGG entry: [3]

• E.C. number: 2.5.1.7

Additional information

• subject to Clp-dependent proteolysis upon glucose starvation PubMed

MurAA is subject to ClpC-ClpP-dependent degradation PubMed

Expression and regulation

• Operon:

• Sigma factor:

• 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:

References

Jean van Heijenoort
Lipid intermediates in the biosynthesis of bacterial peptidoglycan.
Microbiol Mol Biol Rev: 2007, 71(4);620-35
[PubMed:18063720] [WorldCat.org] [DOI] (P p)

Holger Kock, Ulf Gerth, Michael Hecker
MurAA, catalysing the first committed step in peptidoglycan biosynthesis, is a target of Clp-dependent proteolysis in Bacillus subtilis.
Mol Microbiol: 2004, 51(4);1087-102
[PubMed:14763982] [WorldCat.org] [DOI] (P p)