ClpX

• 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: Phosphorelay, Stress
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 This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

proteolysis

This gene is a member of the following regulons

CtsR regulon

The gene

Basic information

• Locus tag: BSU28220

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

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

• Paralogous protein(s): ClpC, ClpE

Targets of ClpX-ClpP-dependent protein degradation

• MgsR PubMed

Extended information on the protein

• Kinetic information:

• Domains: AAA-ATPase PFAM, Zinc finger PFAM

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:
  • ClpP-ClpX
  • Spx-ClpP/ClpX (degradation of Spx) PubMed

• Localization: cytoplasmic polar clusters, excluded from the nucleoid, induced clustering upon heat shock, colocalization with ClpP PubMed

Database entries

• Structure: homologue structure resolved 1UM8, structural model of B. subtilis ClpX available from hstrahl

• UniProt: P50866

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: clpX PubMed

• Expression browser: clpX PubMed

• Sigma factor: SigA PubMed

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

• Regulatory mechanism:
  • CtsR: transcription repression PubMed

• Additional information:
  • The mRNA has a long 5' leader region. This may indicate RNA-based regulation 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

References

Reviews

Additional reviews: PubMed

Original Publications

Additional publications: PubMed

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)

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)