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
Metabolic function and regulation of this protein in SubtiPathways: Stress
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

• UniProt: 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
  • repressed at low temperatures (CtsR) PubMed

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

• 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

Original Publications

Ziqing Mei, Feng Wang, Yutao Qi, Zhiyuan Zhou, Qi Hu, Han Li, Jiawei Wu, Yigong Shi
Molecular determinants of MecA as a degradation tag for the ClpCP protease.
J Biol Chem: 2009, 284(49);34366-75
[PubMed:19767395] [WorldCat.org] [DOI] (I p)

Jeanette Hahn, Naomi Kramer, Kenneth Briley, David Dubnau
McsA and B mediate the delocalization of competence proteins from the cell poles of Bacillus subtilis.
Mol Microbiol: 2009, 72(1);202-15
[PubMed:19226326] [WorldCat.org] [DOI] (I p)

James Kain, Gina G He, Richard Losick
Polar localization and compartmentalization of ClpP proteases during growth and sporulation in Bacillus subtilis.
J Bacteriol: 2008, 190(20);6749-57
[PubMed:18689476] [WorldCat.org] [DOI] (I p)

Adam Reeves, Ulf Gerth, Uwe Völker, W G Haldenwang
ClpP modulates the activity of the Bacillus subtilis stress response transcription factor, sigmaB.
J Bacteriol: 2007, 189(17);6168-75
[PubMed:17586624] [WorldCat.org] [DOI] (P p)

Peter Prepiak, David Dubnau
A peptide signal for adapter protein-mediated degradation by the AAA+ protease ClpCP.
Mol Cell: 2007, 26(5);639-47
[PubMed:17560370] [WorldCat.org] [DOI] (P p)

Janine Kirstein, David A Dougan, Ulf Gerth, Michael Hecker, Kürşad Turgay
The tyrosine kinase McsB is a regulated adaptor protein for ClpCP.
EMBO J: 2007, 26(8);2061-70
[PubMed:17380125] [WorldCat.org] [DOI] (P p)

Stephan Zellmeier, Wolfgang Schumann, Thomas Wiegert
Involvement of Clp protease activity in modulating the Bacillus subtilissigmaw stress response.
Mol Microbiol: 2006, 61(6);1569-82
[PubMed:16899079] [WorldCat.org] [DOI] (P p)

Holger Kock, Ulf Gerth, Michael Hecker
The ClpP peptidase is the major determinant of bulk protein turnover in Bacillus subtilis.
J Bacteriol: 2004, 186(17);5856-64
[PubMed:15317791] [WorldCat.org] [DOI] (P p)

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)

Ulf Gerth, Janine Kirstein, Jörg Mostertz, Torsten Waldminghaus, Marcus Miethke, Holger Kock, Michael Hecker
Fine-tuning in regulation of Clp protein content in Bacillus subtilis.
J Bacteriol: 2004, 186(1);179-91
[PubMed:14679237] [WorldCat.org] [DOI] (P p)

Qi Pan, Richard Losick
Unique degradation signal for ClpCP in Bacillus subtilis.
J Bacteriol: 2003, 185(17);5275-8
[PubMed:12923101] [WorldCat.org] [DOI] (P p)

Tilman Schlothauer, Axel Mogk, David A Dougan, Bernd Bukau, Kürşad Turgay
MecA, an adaptor protein necessary for ClpC chaperone activity.
Proc Natl Acad Sci U S A: 2003, 100(5);2306-11
[PubMed:12598648] [WorldCat.org] [DOI] (P p)

Tiina Pummi, Soile Leskelä, Eva Wahlström, Ulf Gerth, Harold Tjalsma, Michael Hecker, Matti Sarvas, Vesa P Kontinen
ClpXP protease regulates the signal peptide cleavage of secretory preproteins in Bacillus subtilis with a mechanism distinct from that of the Ecs ABC transporter.
J Bacteriol: 2002, 184(4);1010-8
[PubMed:11807061] [WorldCat.org] [DOI] (P p)

Q Pan, D A Garsin, R Losick
Self-reinforcing activation of a cell-specific transcription factor by proteolysis of an anti-sigma factor in B. subtilis.
Mol Cell: 2001, 8(4);873-83
[PubMed:11684022] [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)

E Krüger, E Witt, S Ohlmeier, R Hanschke, M Hecker
The clp proteases of Bacillus subtilis are directly involved in degradation of misfolded proteins.
J Bacteriol: 2000, 182(11);3259-65
[PubMed:10809708] [WorldCat.org] [DOI] (P p)

I Derré, G Rapoport, T Msadek
CtsR, a novel regulator of stress and heat shock response, controls clp and molecular chaperone gene expression in gram-positive bacteria.
Mol Microbiol: 1999, 31(1);117-31
[PubMed:9987115] [WorldCat.org] [DOI] (P p)

K Turgay, J Hahn, J Burghoorn, D Dubnau
Competence in Bacillus subtilis is controlled by regulated proteolysis of a transcription factor.
EMBO J: 1998, 17(22);6730-8
[PubMed:9890793] [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)