ClpX

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  • 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
Gene expression levels in SubtiExpress: clpX
Interactions involving this protein in SubtInteract: ClpX
Metabolic function and regulation of this protein in SubtiPathways:
clpX
MW, pI 46 kDa, 4.645
Gene length, protein length 1260 bp, 420 aa
Immediate neighbours lonB, tig
Sequences Protein DNA DNA_with_flanks
Genetic context
ClpX context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
ClpX expression.png















Categories containing this gene/protein

proteolysis

This gene is a member of the following regulons

CtsR regulon

The gene

Basic information

  • Locus tag: BSU28220

Phenotypes of a mutant

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

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

Targets of ClpX-ClpP-dependent protein degradation

Extended information on the protein

  • Kinetic information:
  • Modification:
  • 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:
    • The mRNA has a long 5' leader region. This may indicate RNA-based regulation PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium): 1690 PubMed
    • number of protein molecules per cell (complex medium with amino acids, without glucose): 6358 PubMed

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

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)

David W Adams, Jeff Errington
Bacterial cell division: assembly, maintenance and disassembly of the Z ring.
Nat Rev Microbiol: 2009, 7(9);642-53
[PubMed:19680248] [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)

Original Publications

Chio Mui Chan, Erik Hahn, Peter Zuber
Adaptor bypass mutations of Bacillus subtilis spx suggest a mechanism for YjbH-enhanced proteolysis of the regulator Spx by ClpXP.
Mol Microbiol: 2014, 93(3);426-38
[PubMed:24942655] [WorldCat.org] [DOI] (I p)

Stephanie Runde, Noël Molière, Anja Heinz, Etienne Maisonneuve, Armgard Janczikowski, Alexander K W Elsholz, Ulf Gerth, Michael Hecker, Kürşad Turgay
The role of thiol oxidative stress response in heat-induced protein aggregate formation during thermotolerance in Bacillus subtilis.
Mol Microbiol: 2014, 91(5);1036-52
[PubMed:24417481] [WorldCat.org] [DOI] (I p)

Irnov Irnov, Cynthia M Sharma, Jörg Vogel, Wade C Winkler
Identification of regulatory RNAs in Bacillus subtilis.
Nucleic Acids Res: 2010, 38(19);6637-51
[PubMed:20525796] [WorldCat.org] [DOI] (I p)

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)

Richard B Weart, Shunji Nakano, Brooke E Lane, Peter Zuber, Petra Anne Levin
The ClpX chaperone modulates assembly of the tubulin-like protein FtsZ.
Mol Microbiol: 2005, 57(1);238-49
[PubMed:15948963] [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)

Hideaki Nanamiya, Emiko Shiomi, Mitsuo Ogura, Teruo Tanaka, Kei Asai, Fujio Kawamura
Involvement of ClpX protein in the post-transcriptional regulation of a competence specific transcription factor, ComK protein, of Bacillus subtilis.
J Biochem: 2003, 133(3);295-302
[PubMed:12761164] [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)

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