Difference between revisions of "ClpP"

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(Original Publications)
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* '''Mutant:'''  
 
* '''Mutant:'''  
 
** ''clpP::spec'' and ''clpP::cat'', available in the [[Leendert Hamoen]] lab
 
** ''clpP::spec'' and ''clpP::cat'', available in the [[Leendert Hamoen]] lab
** GP551 (spc), available in the [[Stülke]] lab
+
** BP99 (''clpP''::''tet''), available in [[Fabian Commichau]]'s lab {{PubMed|25610436}}
** 1S139 ( ''clpP''::''erm''), {{PubMed| }}, available at [http://pasture.asc.ohio-state.edu/BGSC/getdetail.cfm?bgscid=1S139&Search=1S139 BGSC]
+
** GP551 (spc), available in [[Jörg Stülke]]'s lab
 +
** 1S139 (''clpP''::''erm''), {{PubMed| }}, available at [http://pasture.asc.ohio-state.edu/BGSC/getdetail.cfm?bgscid=1S139&Search=1S139 BGSC]
 
** 1S140 ( ''clpP''::''spec''), {{PubMed| }}, available at [http://pasture.asc.ohio-state.edu/BGSC/getdetail.cfm?bgscid=1S140&Search=1S140 BGSC]
 
** 1S140 ( ''clpP''::''spec''), {{PubMed| }}, available at [http://pasture.asc.ohio-state.edu/BGSC/getdetail.cfm?bgscid=1S140&Search=1S140 BGSC]
  
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=Labs working on this gene/protein=
 
=Labs working on this gene/protein=
[[Leendert Hamoen]], Newcastle University, UK [http://www.ncl.ac.uk/camb/staff/profile/l.hamoen homepage]
+
* [[Leendert Hamoen]], Newcastle University, UK [http://www.ncl.ac.uk/camb/staff/profile/l.hamoen homepage]
  
 
=Your additional remarks=
 
=Your additional remarks=
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<pubmed> 16211032 17302811 23375660 23479438,19609260,19781636</pubmed>
 
<pubmed> 16211032 17302811 23375660 23479438,19609260,19781636</pubmed>
 
==Original Publications==
 
==Original Publications==
<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 22080375 22517742 17380125,12598648,9890793,20049702,20049702 23927726 24263382 24226776 24417481 15378759 23361916 24942655 25212124 25433860 </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 22080375 22517742 17380125,12598648,9890793,20049702,20049702 23927726 24263382 24226776 24417481 15378759 23361916 24942655 25212124 25433860 25610436</pubmed>
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 09:04, 23 January 2015

  • 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, most abundant 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

  • 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: 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:
    • belongs to the 100 most abundant proteins PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium): 4011 PubMed
    • number of protein molecules per cell (complex medium with amino acids, without glucose): 11118 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 1536 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 731 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 1056 PubMed

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

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