Difference between revisions of "ClpX"
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==Original Publications== | ==Original Publications== | ||
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[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 12:10, 1 June 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 This image was kindly provided by SubtiList
|
Contents
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:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- 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:
Additional information
Expression and regulation
- Operon: clpX PubMed
- 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