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
Gene expression levels in SubtiExpress: murAA
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
Sequences	Protein DNA DNA_with_flanks
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

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

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): 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)

• UniProt: P70965

• KEGG entry: [3]

• E.C. number: 2.5.1.7

Additional information

• MurAA is subject to ClpC-ClpP-dependent degradation upon glucose starvation PubMed

Expression and regulation

• Operon: murAA PubMed

• Expression browser: murAA PubMed

• Sigma factor:

• Regulation:

• Regulatory mechanism:

• Additional information: subject to Clp-dependent proteolysis upon glucose starvation PubMed

Biological materials

• Mutant:

• Expression vector:
  • pRSETA-murAA, Expression of His(6)-MurAA, avalable in Ulf Gerth's lab PubMed

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody: avalable in Ulf Gerth's lab PubMed

References

Original publications

Sean G Jackson, Fuzhong Zhang, Paul Chindemi, Murray S Junop, Paul J Berti
Evidence of kinetic control of ligand binding and staged product release in MurA (enolpyruvyl UDP-GlcNAc synthase)-catalyzed reactions .
Biochemistry: 2009, 48(49);11715-23
[PubMed:19899805] [WorldCat.org] [DOI] (I p)

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)

T Skarzynski, D H Kim, W J Lees, C T Walsh, K Duncan
Stereochemical course of enzymatic enolpyruvyl transfer and catalytic conformation of the active site revealed by the crystal structure of the fluorinated analogue of the reaction tetrahedral intermediate bound to the active site of the C115A mutant of MurA.
Biochemistry: 1998, 37(8);2572-7
[PubMed:9485407] [WorldCat.org] [DOI] (P p)

T Skarzynski, A Mistry, A Wonacott, S E Hutchinson, V A Kelly, K Duncan
Structure of UDP-N-acetylglucosamine enolpyruvyl transferase, an enzyme essential for the synthesis of bacterial peptidoglycan, complexed with substrate UDP-N-acetylglucosamine and the drug fosfomycin.
Structure: 1996, 4(12);1465-74
[PubMed:8994972] [WorldCat.org] [DOI] (P p)