Difference between revisions of "ClpC"

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(Labs working on this gene/protein)
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=Labs working on this gene/protein=
 
=Labs working on this gene/protein=
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[[Leendert Hamoen]], Newcastle University, UK [http://www.ncl.ac.uk/camb/staff/profile/l.hamoen homepage]
  
 
=Your additional remarks=
 
=Your additional remarks=

Revision as of 12:14, 28 April 2009

  • Description: ATP-dependent Clp protease, ATPase subunit

Gene name clpC
Synonyms mecB
Essential no
Product ATP-dependent Clp protease, ATPase subunit
Function protein degradation

positive regulator of autolysin (LytC and LytD) synthesis

MW, pI 89 kDa, 5.746
Gene length, protein length 2430 bp, 810 aa
Immediate neighbours mcsB, radA
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
ClpC context.gif
This image was kindly provided by SubtiList



The gene

Basic information

  • Coordinates:

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family:
  • Paralogous protein(s): ClpE

Extended information on the protein

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

Database entries

  • Structure:
  • Swiss prot entry:
  • KEGG entry: [3]
  • E.C. number:

Additional information

  • subject to Clp-dependent proteolysis upon glucose starvation PubMed

Expression and regulation

  • Operon:
  • Regulatory mechanism:
  • Additional information: subject to Clp-dependent proteolysis upon glucose starvation PubMed

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Leendert Hamoen, Newcastle University, UK homepage

Your additional remarks

References

  1. Petersohn et al. (2001) Global Analysis of the General Stress Response of Bacillus subtilis. J Bacteriol. 183: 5617-5631 PubMed
  2. Gerth et al. (2008) Clp-dependent proteolysis down-regulates central metabolic pathways in glucose-starved Bacillus subtilis. J Bacteriol 190:321-331 PubMed
  3. Kock H, Gerth U, Hecker M. (2004) MurAA, catalysing the first committed step in peptidoglycan biosynthesis, is a target of Clp-dependent proteolysis in Bacillus subtilis. Mol Microbiol, 51:1087-1102. PubMed
  4. Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed