Difference between revisions of "ClpP"
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{{SubtiWiki category|[[general stress proteins (controlled by SigB)]]}}, | {{SubtiWiki category|[[general stress proteins (controlled by SigB)]]}}, | ||
{{SubtiWiki category|[[heat shock proteins]]}}, | {{SubtiWiki category|[[heat shock proteins]]}}, | ||
− | {{SubtiWiki category|[[phosphoproteins]]}} | + | {{SubtiWiki category|[[phosphoproteins]]}}, |
+ | [[most abundant proteins]] | ||
= This gene is a member of the following [[regulons]] = | = This gene is a member of the following [[regulons]] = | ||
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* '''Additional information:''' | * '''Additional information:''' | ||
+ | ** belongs to the 100 [[most abundant proteins]] {{PubMed|15378759}} | ||
=Biological materials = | =Biological materials = | ||
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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</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</pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 16:52, 5 March 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 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, most abundant proteins
This gene is a member of the following regulons
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:
Database entries
- UniProt: P80244
- KEGG entry: [3]
- E.C. number: 3.4.21.92
Additional information
Expression and regulation
- Operon: clpP PubMed
- Additional information:
- belongs to the 100 most abundant proteins PubMed
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
Original Publications