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• 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
MW, pI	21 kDa, 5.008
Gene length, protein length	591 bp, 197 aa
Immediate neighbours	trnQ-Arg, pgcM
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: BSU34540

Database entries

• 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):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions: ClpE-ClpP, ClpC-ClpP, ClpX-ClpP

• Localization: cytoplasm (according to Swiss-Prot), cytoplasmic polar clusters, excluded from the nucleoid, induced clustering upon heatshock, colocalization with ClpX, ClpC and ClpE Pubmed

Database entries

• Structure: Two homologue structures resolved 1TYF, 1Y7O, structural model of B. subtilis ClpP available from hstrahl

• Swiss prot entry: P80244

• KEGG entry: [3]

• E.C. number: 3.4.21.92

Expression and regulation

• Operon:

• Sigma factor: SigB PubMed

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

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

• Additional information:

Biological materials

• Mutant: clpP::spec and clpP::cat available from the Hamoen] Lab

• 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 from the Hamoen] Lab

• two-hybrid system:

• Antibody:

Labs working on this gene/protein

Leendert Hamoen, Newcastle University, UK homepage

References

Holger Kock, Ulf Gerth, Michael Hecker
MurAA, catalysing the first committed step in peptidoglycan biosynthesis, is a target of Clp-dependent proteolysis in Bacillus subtilis.
Mol Microbiol: 2004, 51(4);1087-102
[PubMed:14763982] [WorldCat.org] [DOI] (P p)

A Petersohn, M Brigulla, S Haas, J D Hoheisel, U Völker, M Hecker
Global analysis of the general stress response of Bacillus subtilis.
J Bacteriol: 2001, 183(19);5617-31
[PubMed:11544224] [WorldCat.org] [DOI] (P p)

U Gerth, E Krüger, I Derré, T Msadek, M Hecker
Stress induction of the Bacillus subtilis clpP gene encoding a homologue of the proteolytic component of the Clp protease and the involvement of ClpP and ClpX in stress tolerance.
Mol Microbiol: 1998, 28(4);787-802
[PubMed:9643546] [WorldCat.org] [DOI] (P p)

1. Petersohn et al. (2001) Global Analysis of the General Stress Response of Bacillus subtilis. J Bacteriol. 183: 5617-5631 PubMed
2. 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
3. Gerth, U., Krüger, E., Derré, I., Msadek, T. and Hecker, M. 1998. Stress induction of the Bacillus subtilis clpP gene encoding a homologue of the proteolytic component of the ClpP protease and the involvement of ClpP and ClpX in stress tolerance. Mol. Microbiol. 28: 787-802. 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