Difference between revisions of "ClpX"

From SubtiWiki
Jump to: navigation, search
(Reviews)
Line 93: Line 93:
 
=Expression and regulation=
 
=Expression and regulation=
  
* '''Operon:'''  
+
* '''Operon:''' ''clpX'' {{PubMed|11325926}}
  
* '''[[Sigma factor]]:'''  
+
* '''[[Sigma factor]]:''' [[SigA]] {{PubMed|8973311}}
  
 
* '''Regulation:'''  
 
* '''Regulation:'''  
 +
** induced by heat stress ([[CtsR]]) {{PubMed|9852015}}
  
 
* '''Regulatory mechanism:'''  
 
* '''Regulatory mechanism:'''  
 +
** [[CtsR]]: transcription repression {{PubMed|9852015}}
  
 
* '''Additional information:'''  
 
* '''Additional information:'''  
Line 123: Line 125:
  
 
=References=
 
=References=
 
 
==Reviews==
 
==Reviews==
 
<pubmed> 19609260  19680248 </pubmed>
 
<pubmed> 19609260  19680248 </pubmed>
 
 
==Original Publications==
 
==Original Publications==
<pubmed>10809708,9643546,11807061,14679237,18689476,16899079,8973311, 19136590 , 9643546, 18786145 </pubmed>
+
<pubmed>10809708,9643546,11807061,14679237,18689476,16899079,8973311, 19136590 , 9643546, 18786145 11325926 8973311 9852015 </pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 20:15, 13 December 2009

  • 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
ClpX context.gif
This image was kindly provided by SubtiList







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:
  • Domains: AAA-ATPase PFAM, Zinc finger PFAM
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:
  • Localization: cytoplasmic polar clusters, excluded from the nucleoid, induced clustering upon heatshock, 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:

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

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)

Original Publications