MurB

• Description: UDP-N-acetylenolpyruvoylglucosamine reductase
  
  

Gene name	murB
Synonyms	ylxC
Essential	yes PubMed
Product	UDP-N-acetylenolpyruvoylglucosamine reductase
Function	peptidoglycan precursor biosynthesis
Gene expression levels in SubtiExpress: murB
Metabolic function and regulation of this protein in SubtiPathways: Cell wall
MW, pI	32 kDa, 6.087
Gene length, protein length	909 bp, 303 aa
Immediate neighbours	murG, divIB
Get the DNA and protein sequences (Barbe et al., 2009)
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, cell envelope stress proteins (controlled by SigM, V, W, X, Y), essential genes

This gene is a member of the following regulons

SigE regulon, SigM regulon, SpoIIID regulon

The gene

Basic information

• Locus tag: BSU15230

Phenotypes of a mutant

essential PubMed

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: UDP-N-acetylmuramate + NADP⁺ = UDP-N-acetyl-3-O-(1-carboxyvinyl)-D-glucosamine + NADPH (according to Swiss-Prot)

• Protein family: FAD-binding PCMH-type domain (according to Swiss-Prot)

• Paralogous protein(s):

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: 2GQU (from Thermus caldophilus, 38% identity, 55% similarity) PubMed

• UniProt: P18579

• KEGG entry: [3]

• E.C. number: 1.1.1.158

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: murB PubMed

• Sigma factor:
  • spoVE: SigE PubMed
  • murG: SigMPubMed

• 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:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

Labs working on this gene/protein

Adriano Henriques, Lisbon, Portugal homepage

References

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)

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)

Gonçalo Real, Adriano O Henriques
Localization of the Bacillus subtilis murB gene within the dcw cluster is important for growth and sporulation.
J Bacteriol: 2006, 188(5);1721-32
[PubMed:16484183] [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)

S L Rowland, J Errington, R G Wake
The Bacillus subtilis cell-division 135-137 degrees region contains an essential orf with significant similarity to murB and a dispensable sbp gene.
Gene: 1995, 164(1);113-6
[PubMed:7590298] [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)