Difference between revisions of "MurAA"

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(Database entries)
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=== Database entries ===
 
=== Database entries ===
  
* '''Structure:''' [http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1UAE 1UAE] (from ''Escherichia coli'', 48% identity, 64% similarity) {{PubMed|8994972}}
+
* '''Structure:''' [http://www.pdb.org/pdb/explore/explore.do?structureId=3SG1 3SG1] (from ''B. anthracis'', 79% identity, 94% similarity)  
  
 
* '''UniProt:''' [http://www.uniprot.org/uniprot/P70965 P70965]
 
* '''UniProt:''' [http://www.uniprot.org/uniprot/P70965 P70965]

Revision as of 20:31, 29 June 2011

  • 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
MurAA context.gif
This image was kindly provided by SubtiList







Categories containing this gene/protein

cell wall synthesis, biosynthesis of cell wall components, essential genes

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU36760

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): MurAB

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: 3SG1 (from B. anthracis, 79% identity, 94% similarity)
  • KEGG entry: [3]

Additional information

Expression and regulation

  • 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

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)