Difference between revisions of "ClpP"

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(Original Publications)
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|colspan="2" style="background:#FAF8CC;" align="center"| '''Interactions involving this protein in [http://subtiwiki.uni-goettingen.de/interact/ ''Subt''Interact]''': [http://subtiwiki.uni-goettingen.de/interact/index.php?protein=ClpP ClpP]
 
|colspan="2" style="background:#FAF8CC;" align="center"| '''Interactions involving this protein in [http://subtiwiki.uni-goettingen.de/interact/ ''Subt''Interact]''': [http://subtiwiki.uni-goettingen.de/interact/index.php?protein=ClpP ClpP]
 
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|colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/pathways/phosphorelay.html Phosphorelay], [http://subtiwiki.uni-goettingen.de/pathways/stress_response.html Stress]'''
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|colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/subtipathways/search.php?enzyme=clpP clpP]'''
 
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|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 21 kDa, 5.008   
 
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 21 kDa, 5.008   

Revision as of 11:44, 7 January 2014

  • 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
Gene expression levels in SubtiExpress: clpP
Interactions involving this protein in SubtInteract: ClpP
Metabolic function and regulation of this protein in SubtiPathways:
clpP
MW, pI 21 kDa, 5.008
Gene length, protein length 591 bp, 197 aa
Immediate neighbours trnQ-Arg, pgcM
Sequences Protein DNA DNA_with_flanks
Genetic context
ClpP context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
ClpP expression.png















Categories containing this gene/protein

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

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

Targets of ClpX-ClpP-dependent protein degradation

Extended information on the protein

  • Kinetic information:
  • Modification:
    • phosphorylated on Arg-13 PubMed
  • 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

  • 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

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)

Noël Molière, Kürşad Turgay
Chaperone-protease systems in regulation and protein quality control in Bacillus subtilis.
Res Microbiol: 2009, 160(9);637-44
[PubMed:19781636] [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)

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

Original Publications