Difference between revisions of "ClpP"

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==Original Publications==
 
==Original Publications==
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<pubmed>17380125,9643546,10809708,11807061,9987115,14679237,18689476,15317791,17586624,11684022,12923101,17560370,12598648,16899079,19226326,9890793, 20070525,9987115,11544224 14763982 9643546, 19767395 11112444 9535081 18689473 20049702 </pubmed>
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<pubmed>17380125,9643546,10809708,11807061,9987115,14679237,18689476,15317791,17586624,11684022,12923101,17560370,12598648,16899079,19226326,9890793, 20070525,9987115,11544224 14763982 9643546, 19767395 11112444 9535081 18689473 20049702 20305655 </pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 09:14, 23 March 2010

  • 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:
Phosphorelay, 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
ClpP context.gif
This image was kindly provided by SubtiList







The gene

Basic information

  • Locus tag: BSU34540

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

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

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:
  • Localization: cytoplasmic polar clusters, excluded from the nucleoid, induced clustering upon heat shock, colocalization with ClpX, ClpC and ClpE PubMed

ClpP.jpg

Database entries

  • Structure: Two homologue structures resolved 1TYF, 1Y7O, structural model of B. subtilis ClpP available from hstrahl
  • KEGG entry: [3]

Additional information

Expression and regulation

  • Regulatory mechanism:
  • Additional information:

Biological materials

  • Mutant:
    • clpP::spec and clpP::cat available , available in the Leendert Hamoen lab
    • GP551 (spc), available in the Stülke 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 in the Leendert Hamoen lab
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Leendert Hamoen, Newcastle University, UK homepage

Your additional remarks

References

Reviews

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)


Original Publications

Byung-Gil Lee, Eun Young Park, Kyung-Eun Lee, Hyesung Jeon, Kwang Hoon Sung, Holger Paulsen, Helga Rübsamen-Schaeff, Heike Brötz-Oesterhelt, Hyun Kyu Song
Structures of ClpP in complex with acyldepsipeptide antibiotics reveal its activation mechanism.
Nat Struct Mol Biol: 2010, 17(4);471-8
[PubMed:20305655] [WorldCat.org] [DOI] (I p)

Mitsuo Ogura, Kensuke Tsukahara
Autoregulation of the Bacillus subtilis response regulator gene degU is coupled with the proteolysis of DegU-P by ClpCP.
Mol Microbiol: 2010, 75(5);1244-59
[PubMed:20070525] [WorldCat.org] [DOI] (I p)

Janine Kirstein, Anja Hoffmann, Hauke Lilie, Ronny Schmidt, Helga Rübsamen-Waigmann, Heike Brötz-Oesterhelt, Axel Mogk, Kürşad Turgay
The antibiotic ADEP reprogrammes ClpP, switching it from a regulated to an uncontrolled protease.
EMBO Mol Med: 2009, 1(1);37-49
[PubMed:20049702] [WorldCat.org] [DOI] (I p)

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)

Lyle A Simmons, Alan D Grossman, Graham C Walker
Clp and Lon proteases occupy distinct subcellular positions in Bacillus subtilis.
J Bacteriol: 2008, 190(20);6758-68
[PubMed:18689473] [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)

H Nanamiya, K Takahashi, M Fujita, F Kawamura
Deficiency of the initiation events of sporulation in Bacillus subtilis clpP mutant can be suppressed by a lack of the Spo0E protein phosphatase.
Biochem Biophys Res Commun: 2000, 279(1);229-33
[PubMed:11112444] [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)

T Msadek, V Dartois, F Kunst, M L Herbaud, F Denizot, G Rapoport
ClpP of Bacillus subtilis is required for competence development, motility, degradative enzyme synthesis, growth at high temperature and sporulation.
Mol Microbiol: 1998, 27(5);899-914
[PubMed:9535081] [WorldCat.org] [DOI] (P p)

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