Difference between revisions of "ClpP"
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= [[Categories]] containing this gene/protein = | = [[Categories]] containing this gene/protein = | ||
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* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=clpP_3546234_3546827_1 clpP] {{PubMed|22383849}} | * '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=clpP_3546234_3546827_1 clpP] {{PubMed|22383849}} | ||
− | * '''Sigma factor:''' [[SigA]] {{PubMed|9643546}}, [[SigB]] {{PubMed|9643546,11544224}} | + | * '''[[Sigma factor]]:''' [[SigA]] {{PubMed|9643546}}, [[SigB]] {{PubMed|9643546,11544224}} |
* '''Regulation:''' | * '''Regulation:''' | ||
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==Reviews== | ==Reviews== | ||
'''Additional reviews:''' {{PubMed|19609260,19781636}} | '''Additional reviews:''' {{PubMed|19609260,19781636}} | ||
− | <pubmed> 16211032 17302811 </pubmed> | + | <pubmed> 16211032 17302811 23375660 </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 22080375 22517742</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</pubmed> | ||
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 12:44, 5 February 2013
- 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: 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 This image was kindly provided by SubtiList
| |
Expression at a glance PubMed |
Contents
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
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:
- Domains:
- Modification:
- phosphorylated on Arg-13 PubMed
- Cofactor(s):
- Effectors of protein activity:
Database entries
- UniProt: P80244
- KEGG entry: [3]
- E.C. number: 3.4.21.92
Additional information
Expression and regulation
- Operon: clpP PubMed
- 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
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)
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