MurAB

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  • Description: UDP-N-acetylglucosamine 1-carboxyvinyltransferase

Gene name murAB
Synonyms murZ, lssF, rev-4
Essential no
Product UDP-N-acetylglucosamine 1-carboxyvinyltransferase
Function peptidoglycan precursor biosynthesis
Gene expression levels in SubtiExpress: murAB
Metabolic function and regulation of this protein in SubtiPathways:
Cell wall
MW, pI 45 kDa, 5.831
Gene length, protein length 1287 bp, 429 aa
Immediate neighbours glpX, ywjH
Sequences Protein DNA DNA_with_flanks
Genetic context
MurAB context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
MurAB expression.png




























Categories containing this gene/protein

cell wall synthesis, biosynthesis of cell wall components

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU37100

Phenotypes of a mutant

Database entries

  • DBTBS entry: no entry
  • SubtiList entry: [1]

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): MurAA

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • Structure: 3SG1 (from B. anthracis, 50% identity, 81% similarity)
  • KEGG entry: [2]

Additional information

Expression and regulation

  • Sigma factor:
  • Regulation: constitutive PubMed
  • Regulatory mechanism:
  • Additional information:

Biological materials

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

Labs working on this gene/protein

Your additional remarks

References

Matthieu Jules, Ludovic Le Chat, Stéphane Aymerich, Dominique Le Coq
The Bacillus subtilis ywjI (glpX) gene encodes a class II fructose-1,6-bisphosphatase, functionally equivalent to the class III Fbp enzyme.
J Bacteriol: 2009, 191(9);3168-71
[PubMed:19270101] [WorldCat.org] [DOI] (I p)