ClpC

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
Gene expression levels in SubtiExpress: clpC
Interactions involving this protein in SubtInteract: ClpC
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
Expression at a glance   PubMed

Categories containing this gene/protein

proteolysis, sporulation proteins, general stress proteins (controlled by SigB), heat shock proteins, phosphoproteins

This gene is a member of the following regulons

CtsR regulon, SigB regulon, SigF regulon

The gene

Basic information

• Locus tag: BSU00860

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

Additional information

• A mutation was found in this gene after evolution under relaxed selection for sporulation PubMed

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 PubMed, CtsR PubMed, Mdh, MgsR PubMed

Extended information on the protein

• Kinetic information:

• Domains: AAA-ATPase PFAM

• Modification:
  • phosphorylated on Arg-5 and Arg-254 PubMed

• 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
  • CtsR-McsB-ClpC/ClpP (degradation of CtsR) 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)
  • 3PXG (the MecA-ClpC complex) PubMed

• 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

• Expression browser: clpC 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

Kürsad Turgay, Freie Universität Berlin, Germany homepage

References

Reviews

Additional reviews: PubMed

Dorte Frees, Kirsi Savijoki, Pekka Varmanen, Hanne Ingmer
Clp ATPases and ClpP proteolytic complexes regulate vital biological processes in low GC, Gram-positive bacteria.
Mol Microbiol: 2007, 63(5);1285-95
[PubMed:17302811] [WorldCat.org] [DOI] (P p)

Original Publications

Additional publications: PubMed