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
Metabolic function and regulation of this protein in SubtiPathways: 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 This image was kindly provided by SubtiList

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

Extended information on the protein

• Kinetic information:

• Domains: AAA-ATPase PFAM, Zinc finger PFAM

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions: ClpP-ClpX

• Localization: cytoplasmic polar clusters, excluded from the nucleoid, induced clustering upon heatshock, colocalization with ClpP Pubmed

Database entries

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

• Swiss prot entry: P50866

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon:

• Sigma factor:

• 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

References

1. Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed