Difference between revisions of "MurG"

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Revision as of 08:59, 19 April 2012

  • Description: UDP-N-acetylglucosamine-N-acetylmuramyl-(pentapeptide)pyrophosphoryl-undecaprenol N-acetylglucosamine transferase

Gene name murG
Synonyms
Essential yes PubMed
Product UDP-N-acetylglucosamine-

N-acetylmuramyl-(pentapeptide)pyrophosphoryl-undecaprenol N-acetylglucosamine transferase

Function peptidoglycan precursor biosynthesis
Metabolic function and regulation of this protein in SubtiPathways:
Cell wall
MW, pI 39 kDa, 9.568
Gene length, protein length 1089 bp, 363 aa
Immediate neighbours spoVE, murB
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
MurG context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
MurG expression.png




























Categories containing this gene/protein

cell wall synthesis, biosynthesis of cell wall components, sporulation proteins, essential genes, membrane proteins

This gene is a member of the following regulons

SigE regulon, SpoIIID regulon

The gene

Basic information

  • Locus tag: BSU15220

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: UDP-N-acetylglucosamine + Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol = UDP + GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol (according to Swiss-Prot)
  • Protein family: MurG subfamily (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

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

Database entries

  • Structure: 1F0K (from Escherichia coli, 30% identity, 52% similarity) PubMed
  • KEGG entry: [3]

Additional information

Expression and regulation

  • Regulation:
    • expressed during vegatative growth, then switched off, and again expressed during sporulation in the mother cell (SigE) PubMed
  • 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

Katarína Muchová, Anthony J Wilkinson, Imrich Barák
Changes of lipid domains in Bacillus subtilis cells with disrupted cell wall peptidoglycan.
FEMS Microbiol Lett: 2011, 325(1);92-8
[PubMed:22092867] [WorldCat.org] [DOI] (I p)

Warawan Eiamphungporn, John D Helmann
The Bacillus subtilis sigma(M) regulon and its contribution to cell envelope stress responses.
Mol Microbiol: 2008, 67(4);830-48
[PubMed:18179421] [WorldCat.org] [DOI] (P p)

Ahmed Bouhss, Amy E Trunkfield, Timothy D H Bugg, Dominique Mengin-Lecreulx
The biosynthesis of peptidoglycan lipid-linked intermediates.
FEMS Microbiol Rev: 2008, 32(2);208-33
[PubMed:18081839] [WorldCat.org] [DOI] (P 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)

Patrick Eichenberger, Masaya Fujita, Shane T Jensen, Erin M Conlon, David Z Rudner, Stephanie T Wang, Caitlin Ferguson, Koki Haga, Tsutomu Sato, Jun S Liu, Richard Losick
The program of gene transcription for a single differentiating cell type during sporulation in Bacillus subtilis.
PLoS Biol: 2004, 2(10);e328
[PubMed:15383836] [WorldCat.org] [DOI] (I p)

A A Branstrom, S Midha, C B Longley, K Han, E R Baizman, H R Axelrod
Assay for identification of inhibitors for bacterial MraY translocase or MurG transferase.
Anal Biochem: 2000, 280(2);315-9
[PubMed:10790316] [WorldCat.org] [DOI] (P p)

G Theeragool, A Miyao, K Yamada, T Sato, Y Kobayashi
In vivo expression of the Bacillus subtilis spoVE gene.
J Bacteriol: 1993, 175(13);4071-80
[PubMed:8320223] [WorldCat.org] [DOI] (P p)

A O Henriques, H de Lencastre, P J Piggot
A Bacillus subtilis morphogene cluster that includes spoVE is homologous to the mra region of Escherichia coli.
Biochimie: 1992, 74(7-8);735-48
[PubMed:1391053] [WorldCat.org] [DOI] (P p)