ClpP

• Description: ATP-dependent Clp protease proteolytic subunit (class III heat-shock protein)
  
  

Gene name	clpP
Synonyms	yvdN
Essential	no
Product	ATP-dependent Clp protease proteolytic subunit
Function	protein degradation
Gene expression levels in SubtiExpress: clpP
Interactions involving this protein in SubtInteract: ClpP
Metabolic function and regulation of this protein in SubtiPathways: clpP
MW, pI	21 kDa, 5.008
Gene length, protein length	591 bp, 197 aa
Immediate neighbours	trnQ-Arg, pgcM
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, general stress proteins (controlled by SigB), heat shock proteins, phosphoproteins, most abundant proteins

This gene is a member of the following regulons

CtsR regulon, SigB regulon

The gene

Basic information

• Locus tag: BSU34540

Phenotypes of a mutant

• increased thermotolerance due to increased stabiliy of Spx and thus increased expression of trxA PubMed

Database entries

• BsubCyc: BSU34540

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: Hydrolysis of proteins to small peptides in the presence of ATP and magnesium (according to Swiss-Prot) endopeptidase/proteolysis

• Protein family: peptidase S14 family (according to Swiss-Prot) ClpP (IPR001907) InterPro, (PF00574) PFAM

• Paralogous protein(s):

Targets of ClpC-ClpP-dependent protein degradation

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

Targets of ClpX-ClpP-dependent protein degradation

• MgsR PubMed

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:
  • phosphorylated on Arg-13 PubMed

• Cofactors:

• Effectors of protein activity:
  • the novel antibiotic ADEP (acyldepsipeptides) dysregulates ClpP activity and allows FtsZ degradation in the absence of an ATPase subunit (ClpC, ClpE, or ClpX) PubMed

• Interactions:
  • ClpE-ClpP, ClpC-ClpP, ClpX-ClpP
  • CtsR-ClpP/ClpC (degradation of CtsR) PubMed
  • McsB-ClpP/ClpC (rapid degradation of non-phosphorylated McsB) PubMed
  • Spx-ClpP/ClpX (degradation of Spx) PubMed

• Localization:
  • cytoplasmic polar clusters, excluded from the nucleoid, induced clustering upon heat shock, colocalization with ClpX, ClpC and ClpE PubMed

Database entries

• BsubCyc: BSU34540

• Structure: 3KTG PubMed

• UniProt: P80244

• KEGG entry: [3]

• E.C. number: 3.4.21.92

Expression and regulation

• Operon: clpP PubMed

• Expression browser: clpP PubMed

• Sigma factor: SigA PubMed, SigB PubMed

• Regulation:
  • induced by stress (SigB) PubMed
  • induced by heat (CtsR) PubMed

• Regulatory mechanism:
  • CtsR: transcription repression PubMed

• Additional information:
  • belongs to the 100 most abundant proteins PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium): 4011 PubMed
  • number of protein molecules per cell (complex medium with amino acids, without glucose): 11118 PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 1536 PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 731 PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 1056 PubMed

Biological materials

• Mutant:
  • clpP::spec and clpP::cat, available in the Leendert Hamoen lab
  • BP99 (clpP::tet), available in Fabian Commichau's lab PubMed
  • GP551 (spc), available in Jörg Stülke's lab
  • 1S139 (clpP::erm), PubMed, available at BGSC
  • 1S140 ( clpP::spec), PubMed, available at BGSC

• Expression vector:

• lacZ fusion:

• GFP fusion: C-terminal GFP fusions (both single copy and as 2th copy in amyE locus, also as CFP and YFP variants) available in the Leendert Hamoen lab

• two-hybrid system:

• Antibody:

Labs working on this gene/protein

• Leendert Hamoen, Newcastle University, UK 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)

John S Blanchard
Old approach yields new antibiotic.
Nat Med: 2005, 11(10);1045-6
[PubMed:16211032] [WorldCat.org] [DOI] (P p)