ClpC

• 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 This image was kindly provided by SubtiList

The gene

Basic information

• Coordinates:

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

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: YpbH-ClpC, McsB-ClpC, ClpC-MecA, ClpC-ClpP

• Localization: cytoplasmic polar clusters, excluded from the nucleoid, induced clustering upon heatshock, colocalization with ClpP

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:

• Sigma factor: SigB PubMed

• Regulation: induced by stress (SigB) PubMed

• Regulatory mechanism:

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

Biological materials

• Mutant: clpC::tet available from the Hamoen Lab Subtiwiki

• Expression vector:

• lacZ fusion:

• GFP fusion: C-terminal GFP fusions (single copy, also as CFP and YFP variants) available from the Hamoen Lab Subtiwiki

• two-hybrid system:

• Antibody:

Labs working on this gene/protein

Leendert Hamoen, Newcastle University, UK homepage

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. Kirstein, J., Strahl, H., Molière, N., Hamoen, LW., Turgay K. (2008) Localization of general and regulatory proteolysis in Bacillus subtilis cells. Mol Microbiol. 70:682-94. Pubmed
5. Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed