ClpC

• Description: ATP-dependent Clp protease, ATPase subunit of the ClpC-ClpP protease, involved in auto-cleavage of SlrR
  
  

Gene name	clpC
Synonyms	mecB
Essential	no
Product	ATPase subunit of the ClpC-ClpP protease
Function	protein degradation positive regulator of autolysin (LytC and LytD) synthesis
Metabolic function and regulation of this protein in SubtiPathways: Stress
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

• Locus tag: BSU00860

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: ATPase/chaperone

• Protein family: mecA family (according to Swiss-Prot) clpA/clpB family. ClpC subfamily (according to Swiss-Prot), AAA+ -type ATPase (IPR013093) InterPro (PF07724) PFAM

• Paralogous protein(s): ClpE, ClpX

Targets of ClpC-ClpP-dependent protein degradation

• DegU-P PubMed, MurAA PubMed, ComK, Mdh

Extended information on the protein

• Kinetic information:

• Domains: AAA-ATPase PFAM

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:
  • the protease: ClpC-ClpP
  • interactions with adaptor proteins of ClpC-ClpP: YpbH-ClpC, McsB-ClpC, MecA-ClpC PubMed

• Localization: cytoplasmic polar clusters, excluded from the nucleoid, induced clustering upon heatshock, colocalization with ClpP Pubmed; forms foci coincident with nucleoid edges, usually near cell poles PubMed

Database entries

• Structure: 2K77 (N-terminal domain)

• UniProt: P37571

• KEGG entry: [3]

• E.C. number:

Additional information

• subject to Clp-dependent proteolysis upon glucose starvation PubMed

Expression and regulation

• Operon: ctsR-mcsA-mcsB-clpC-radA-disA PubMed

• Sigma factor: SigA PubMed, SigB PubMed1 PubMed2, SigF PubMed

• Regulation:
  • expressed early during sporulation in the forespore (SigF) PubMed
  • induced by stress (SigB) PubMed
  • induced by heat (CtsR) PubMed

• Regulatory mechanism:
  • CtsR: transcription repression PubMed1, PubMed2, PubMed3, PubMed4

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

Biological materials

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

• Expression vector:

• lacZ fusion:

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

• two-hybrid system:

• Antibody:

Labs working on this gene/protein

Leendert Hamoen, Newcastle University, UK homepage

References

Reviews

Noël Molière, Kürşad Turgay
Chaperone-protease systems in regulation and protein quality control in Bacillus subtilis.
Res Microbiol: 2009, 160(9);637-44
[PubMed:19781636] [WorldCat.org] [DOI] (I p)

Janine Kirstein, Noël Molière, David A Dougan, Kürşad Turgay
Adapting the machine: adaptor proteins for Hsp100/Clp and AAA+ proteases.
Nat Rev Microbiol: 2009, 7(8);589-99
[PubMed:19609260] [WorldCat.org] [DOI] (I p)