MurG

• 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
Gene expression levels in SubtiExpress: murG
Metabolic function and regulation of this protein in SubtiPathways: murG
MW, pI	39 kDa, 9.568
Gene length, protein length	1089 bp, 363 aa
Immediate neighbours	spoVE, murB
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, 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

• BsubCyc: BSU15220

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:
  • converts lipid I to lipid II by attaching GlcNAc to the bactoprenol carrier-conjugated UDP-N-acetylmuramic acid (UDP-MurNAc) pentapeptide molecule
  • 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:

• Cofactors:

• Effectors of protein activity:

• Interactions:

• Localization:
  • peripheral membrane protein PubMed

Database entries

• BsubCyc: BSU15220

• Structure: 1F0K (from Escherichia coli, 30% identity, 52% similarity) PubMed

• UniProt: P37585

• KEGG entry: [3]

• E.C. number: 2.4.1.227

Expression and regulation

• Operon:
  • murE-mraY-murD-spoVE-murG-murB-divIB-ylxW-ylxX-sbp PubMed
  • spoVE-murG-murB-divIB-ylxW-ylxX-sbp PubMed
  • murG-murB-divIB-ylxW-ylxX-sbp PubMed

• Expression browser: murG PubMed

• Sigma factor:
  • spoVE: SigE PubMed
  • within murG: SigM PubMed

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

• Regulatory mechanism:
  • SpoIIID: transcription repression PubMed

• Additional information:
  • number of protein molecules per cell (minimal medium with glucose and ammonium): 82 PubMed
  • number of protein molecules per cell (complex medium with amino acids, without glucose): 627 PubMed

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• FLAG-tag construct:
  • GP2002 murG-3xFLAG ermC (based on pGP1087), available in Jörg Stülke's lab

• Antibody:

References

Michaela Wenzel, Alina Iulia Chiriac, Andreas Otto, Dagmar Zweytick, Caroline May, Catherine Schumacher, Ronald Gust, H Bauke Albada, Maya Penkova, Ute Krämer, Ralf Erdmann, Nils Metzler-Nolte, Suzana K Straus, Erhard Bremer, Dörte Becher, Heike Brötz-Oesterhelt, Hans-Georg Sahl, Julia Elisabeth Bandow
Small cationic antimicrobial peptides delocalize peripheral membrane proteins.
Proc Natl Acad Sci U S A: 2014, 111(14);E1409-18
[PubMed:24706874] [WorldCat.org] [DOI] (I p)

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)