Difference between revisions of "ClpP"

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(Reviews)
(References)
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=References=
 
=References=
 
 
==Reviews==
 
==Reviews==
 
'''Additional reviews:''' {{PubMed|19609260,19781636}}
 
'''Additional reviews:''' {{PubMed|19609260,19781636}}
 
<pubmed> 16211032 17302811 </pubmed>
 
<pubmed> 16211032 17302811 </pubmed>
 
 
==Original Publications==
 
==Original Publications==
 
'''Additional publications:''' {{PubMed|17380125,12598648,9890793,20049702,20049702}}
 
'''Additional publications:''' {{PubMed|17380125,12598648,9890793,20049702,20049702}}
 
<pubmed>9643546,10809708,11807061,9987115,14679237,18689476,15317791,17586624,11684022,12923101,17560370, 16899079,19226326 , 20070525,9987115,11544224 14763982 9643546, 19767395 11112444 9535081 18689473 20305655 20852588 16200071 21969594 </pubmed>
 
<pubmed>9643546,10809708,11807061,9987115,14679237,18689476,15317791,17586624,11684022,12923101,17560370, 16899079,19226326 , 20070525,9987115,11544224 14763982 9643546, 19767395 11112444 9535081 18689473 20305655 20852588 16200071 21969594 </pubmed>
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 09:40, 31 October 2011

  • Description: ATP-dependent Clp protease proteolytic subunit (class III heat-shock protein)

Gene name clpP
Synonyms yvdN
Essential no
Product ATP-dependent Clp protease proteolytic subunit
Function protein degradation
Interactions involving this protein in SubtInteract: ClpP
Metabolic function and regulation of this protein in SubtiPathways:
Phosphorelay, Stress
MW, pI 21 kDa, 5.008
Gene length, protein length 591 bp, 197 aa
Immediate neighbours trnQ-Arg, pgcM
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
ClpP context.gif
This image was kindly provided by SubtiList







Categories containing this gene/protein

proteolysis, general stress proteins (controlled by SigB), heat shock proteins

This gene is a member of the following regulons

CtsR regulon, SigB regulon

The gene

Basic information

  • Locus tag: BSU34540

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: Hydrolysis of proteins to small peptides in the presence of ATP and magnesium (according to Swiss-Prot) endopeptidase/proteolysis
  • Protein family: peptidase S14 family (according to Swiss-Prot) ClpP (IPR001907) InterPro, (PF00574) PFAM
  • Paralogous protein(s):

Targets of ClpC-ClpP-dependent protein degradation

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:
    • the novel antibiotic ADEP (acyldepsipeptides) dysregulates ClpP activity and allows FtsZ degradation in the absence of an ATPase subunit (ClpC, ClpE, or ClpX) PubMed
  • Localization:
    • cytoplasmic polar clusters, excluded from the nucleoid, induced clustering upon heat shock, colocalization with ClpX, ClpC and ClpE PubMed

ClpP.jpg

Database entries

  • KEGG entry: [3]

Additional information

Expression and regulation

  • Regulatory mechanism:
  • Additional information:

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion: C-terminal GFP fusions (both single copy and as 2th copy in amyE locus, also as CFP and YFP variants) available in the Leendert Hamoen lab
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Leendert Hamoen, Newcastle University, UK homepage

Your additional remarks

References

Reviews

Additional reviews: PubMed

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)

John S Blanchard
Old approach yields new antibiotic.
Nat Med: 2005, 11(10);1045-6
[PubMed:16211032] [WorldCat.org] [DOI] (P p)

Original Publications

Additional publications: PubMed