Difference between revisions of "MurQ"

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{{SubtiWiki category|[[utilization of specific carbon sources]]}},
 
{{SubtiWiki category|[[utilization of specific carbon sources]]}},
 
{{SubtiWiki category|[[phosphoproteins]]}},
 
{{SubtiWiki category|[[phosphoproteins]]}},
{{SubtiWiki category|[[sporulation/ other]]}}
+
{{SubtiWiki category|[[Sporulation#Sporulation_proteins/_other|sporulation proteins]]}}
  
 
= This gene is a member of the following [[regulons]] =
 
= This gene is a member of the following [[regulons]] =

Revision as of 11:05, 24 April 2014

  • 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
Gene expression levels in SubtiExpress: murQ
Metabolic function and regulation of this protein in SubtiPathways:
murQ
MW, pI 32 kDa, 5.404
Gene length, protein length 912 bp, 304 aa
Immediate neighbours murR, ybbJ
Sequences Protein DNA DNA_with_flanks
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, sporulation proteins

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

Pierre Nicolas, Ulrike Mäder, Etienne Dervyn, Tatiana Rochat, Aurélie Leduc, Nathalie Pigeonneau, Elena Bidnenko, Elodie Marchadier, Mark Hoebeke, Stéphane Aymerich, Dörte Becher, Paola Bisicchia, Eric Botella, Olivier Delumeau, Geoff Doherty, Emma L Denham, Mark J Fogg, Vincent Fromion, Anne Goelzer, Annette Hansen, Elisabeth Härtig, Colin R Harwood, Georg Homuth, Hanne Jarmer, Matthieu Jules, Edda Klipp, Ludovic Le Chat, François Lecointe, Peter Lewis, Wolfram Liebermeister, Anika March, Ruben A T Mars, Priyanka Nannapaneni, David Noone, Susanne Pohl, Bernd Rinn, Frank Rügheimer, Praveen K Sappa, Franck Samson, Marc Schaffer, Benno Schwikowski, Leif Steil, Jörg Stülke, Thomas Wiegert, Kevin M Devine, Anthony J Wilkinson, Jan Maarten van Dijl, Michael Hecker, Uwe Völker, Philippe Bessières, Philippe Noirot
Condition-dependent transcriptome reveals high-level regulatory architecture in Bacillus subtilis.
Science: 2012, 335(6072);1103-6
[PubMed:22383849] [WorldCat.org] [DOI] (I p)

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)