Difference between revisions of "ClpX"

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|style="background:#ABCDEF;" align="center"|'''Function''' || protein degradation
 
|style="background:#ABCDEF;" align="center"|'''Function''' || protein degradation
 
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|colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/pathways/stress_response.html Stress]'''
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|colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/pathways/phosphorelay.html Phosphorelay], [http://subtiwiki.uni-goettingen.de/pathways/stress_response.html Stress]'''
 
|-
 
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|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 46 kDa, 4.645   
 
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 46 kDa, 4.645   

Revision as of 14:08, 16 February 2010

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

Gene name clpX
Synonyms
Essential no
Product ATP-dependent Clp protease ATP-binding subunit
Function protein degradation
Metabolic function and regulation of this protein in SubtiPathways:
Phosphorelay, Stress
MW, pI 46 kDa, 4.645
Gene length, protein length 1260 bp, 420 aa
Immediate neighbours lonB, tig
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
ClpX context.gif
This image was kindly provided by SubtiList







The gene

Basic information

  • Locus tag: BSU28220

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: ATPase/chaperone
  • Protein family: clpX chaperone family (according to Swiss-Prot) ClpX (IP004487) InterPro, AAA+ -type ATPase (IPR013093) InterPro (PF07724) PFAM

Extended information on the protein

  • Kinetic information:
  • Domains: AAA-ATPase PFAM, Zinc finger PFAM
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:
  • Localization: cytoplasmic polar clusters, excluded from the nucleoid, induced clustering upon heat shock, colocalization with ClpP PubMed

ClpX.jpg

Database entries

  • Structure: homologue structure resolved 1UM8, structural model of B. subtilis ClpX available from hstrahl
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Regulation:
  • Regulatory mechanism:
  • Additional information:

Biological materials

  • Mutant: clpX::kan, clpX::spec and clpX::cat available from the Hamoen] Lab
  • Expression vector:
  • lacZ fusion:
  • GFP fusion: C-terminal GFP fusions (both single copy and 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

Your additional remarks

References

Reviews

Original Publications

Daniel P Haeusser, Amy H Lee, Richard B Weart, Petra Anne Levin
ClpX inhibits FtsZ assembly in a manner that does not require its ATP hydrolysis-dependent chaperone activity.
J Bacteriol: 2009, 191(6);1986-91
[PubMed:19136590] [WorldCat.org] [DOI] (I p)

Janine Kirstein, Henrik Strahl, Noël Molière, Leendert W Hamoen, Kürşad Turgay
Localization of general and regulatory proteolysis in Bacillus subtilis cells.
Mol Microbiol: 2008, 70(3);682-94
[PubMed:18786145] [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)

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)

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)

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)

M Serrano, S Hövel, C P Moran, A O Henriques, U Völker
Forespore-specific transcription of the lonB gene during sporulation in Bacillus subtilis.
J Bacteriol: 2001, 183(10);2995-3003
[PubMed:11325926] [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)

E Krüger, M Hecker
The first gene of the Bacillus subtilis clpC operon, ctsR, encodes a negative regulator of its own operon and other class III heat shock genes.
J Bacteriol: 1998, 180(24);6681-8
[PubMed:9852015] [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)

U Gerth, A Wipat, C R Harwood, N Carter, P T Emmerson, M Hecker
Sequence and transcriptional analysis of clpX, a class-III heat-shock gene of Bacillus subtilis.
Gene: 1996, 181(1-2);77-83
[PubMed:8973311] [WorldCat.org] [DOI] (P p)