MurQ

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Revision as of 16:16, 19 April 2012 by Jstuelk (talk | contribs) (Expression and regulation)
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  • Description: similar to E. coli MurQ (etherase, cleaves lactate from N-acetylmuramic acid)

Gene name murQ
Synonyms ybbI
Essential no
Product putative etherase
Function cell wall turnover
Metabolic function and regulation of this protein in SubtiPathways:
Murein recycling
MW, pI 32 kDa, 5.404
Gene length, protein length 912 bp, 304 aa
Immediate neighbours murR, ybbJ
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
YbbI context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
MurQ expression.png
























Categories containing this gene/protein

cell wall degradation/ turnover, utilization of specific carbon sources, phosphoproteins

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU01700

Phenotypes of a mutant

Database entries

  • DBTBS entry: no entry
  • SubtiList entry: [1]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: N-acetylmuramic acid 6-phosphate + H2O = N-acetyl-D-glucosamine 6-phosphate + D-lactate (according to Swiss-Prot)
  • Protein family: SIS domain (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification: phosphorylation on Ser-2 PubMed
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • Structure:
  • KEGG entry: [2]
  • E.C. number:

Additional information

Expression and regulation

  • Sigma factor:
  • Regulation:
  • Regulatory mechanism:
  • 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

Silke Litzinger, Amanda Duckworth, Katja Nitzsche, Christian Risinger, Valentin Wittmann, Christoph Mayer
Muropeptide rescue in Bacillus subtilis involves sequential hydrolysis by beta-N-acetylglucosaminidase and N-acetylmuramyl-L-alanine amidase.
J Bacteriol: 2010, 192(12);3132-43
[PubMed:20400549] [WorldCat.org] [DOI] (I p)

Boris Macek, Ivan Mijakovic, Jesper V Olsen, Florian Gnad, Chanchal Kumar, Peter R Jensen, Matthias Mann
The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis.
Mol Cell Proteomics: 2007, 6(4);697-707
[PubMed:17218307] [WorldCat.org] [DOI] (P p)