ClpC

• Description: ATPase subunit of the ATP-dependent ClpC-ClpP protease, involved in competence development, heat shock regulation, motility, sporulation, protein quality control, biofilm formation

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: clpC
MW, pI	89 kDa, 5.746
Gene length, protein length	2430 bp, 810 aa
Immediate neighbours	mcsB, radA
Sequences	Protein DNA DNA_with_flanks
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

• BsubCyc: BSU00860

• 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

• Cofactors:

• 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

• BsubCyc: BSU00860

• Structure:
  • 2K77 (N-terminal domain)
  • 3PXG, 3J3U 3J3U (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
  • number of protein molecules per cell (minimal medium with glucose and ammonium): 1157 PubMed
  • number of protein molecules per cell (complex medium with amino acids, without glucose): 2624 PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 711 PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 495 PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 617 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

Noël Molière, Kürşad Turgay
General and regulatory proteolysis in Bacillus subtilis.
Subcell Biochem: 2013, 66;73-103
[PubMed:23479438] [WorldCat.org] [DOI] (P p)

Aurelia Battesti, Susan Gottesman
Roles of adaptor proteins in regulation of bacterial proteolysis.
Curr Opin Microbiol: 2013, 16(2);140-7
[PubMed:23375660] [WorldCat.org] [DOI] (I p)

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)

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)