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: 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 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

Phenotypes of a mutant

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

Database entries

• BsubCyc: BSU28220

• 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:

• Cofactors:

• 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

• BsubCyc: BSU28220

• 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
  • 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

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)