Difference between revisions of "ClpX"

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===Phenotypes of a mutant ===
 
===Phenotypes of a mutant ===
 +
* increased thermotolerance due to increased stabiliy of [[Spx]] and thus increased expression of ''[[trxA]]'' {{PubMed|24417481}}
  
 
=== Database entries ===
 
=== Database entries ===
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=== Additional information===
 
=== Additional information===
 
 
 
  
 
=The protein=
 
=The protein=
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* '''Kinetic information:'''
 
* '''Kinetic information:'''
  
* '''Domains:''' AAA-ATPase [http://pfam.sanger.ac.uk/family?acc=PF07724 PFAM], Zinc finger [http://pfam.sanger.ac.uk/family?acc=PF06689 PFAM]
+
* '''[[Domains]]:'''  
 +
** AAA-ATPase [http://pfam.sanger.ac.uk/family?acc=PF07724 PFAM]
 +
** Zinc finger [http://pfam.sanger.ac.uk/family?acc=PF06689 PFAM]
  
 
* '''Modification:'''
 
* '''Modification:'''
  
* '''Cofactor(s):'''
+
* '''[[Cofactors]]:'''
  
 
* '''Effectors of protein activity:'''
 
* '''Effectors of protein activity:'''
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=References=
 
=References=
 
==Reviews==
 
==Reviews==
'''Additional reviews: ''' {{PubMed|23479438,19609260}}
+
<pubmed>23375660  19680248 17302811 23479438,19609260</pubmed>
<pubmed>23375660  19680248 17302811</pubmed>
 
 
==Original Publications==
 
==Original Publications==
'''Additional publications: ''' {{PubMed|18786145}}
+
<pubmed>12761164 10809708,9643546,11807061,14679237,18689476,16899079,8973311, 19136590 , 11325926 8973311 9852015 18689473 20525796 15948963 18786145 24417481</pubmed>
<pubmed>12761164 10809708,9643546,11807061,14679237,18689476,16899079,8973311, 19136590 , 11325926 8973311 9852015 18689473 20525796 15948963 </pubmed>
 
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 09:32, 16 January 2014

  • 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
ClpX context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
ClpX expression.png















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

  • 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

Targets of ClpX-ClpP-dependent protein degradation

Extended information on the protein

  • Kinetic information:
  • Modification:
  • Effectors of protein activity:
  • Localization: cytoplasmic polar clusters, excluded from the nucleoid, induced clustering upon heat shock, 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:
    • 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

Your additional remarks

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)

Original Publications