Difference between revisions of "ClpP"
(→Original Publications) |
|||
| Line 74: | Line 74: | ||
* '''Interactions:''' [[ClpE]]-[[ClpP]], [[ClpC]]-[[ClpP]], [[ClpX]]-[[ClpP]] | * '''Interactions:''' [[ClpE]]-[[ClpP]], [[ClpC]]-[[ClpP]], [[ClpX]]-[[ClpP]] | ||
| − | * '''Localization:''' | + | * '''Localization:''' cytoplasmic polar clusters, excluded from the nucleoid, induced clustering upon heat shock, colocalization with [[ClpX]], [[ClpC]] and [[ClpE]] {{PubMed|18786145,18689473}} |
[[File:ClpP.jpg ]] | [[File:ClpP.jpg ]] | ||
| Line 130: | Line 130: | ||
<pubmed> 19609260 </pubmed> | <pubmed> 19609260 </pubmed> | ||
==Original Publications== | ==Original Publications== | ||
| − | <pubmed>17380125,9643546,10809708,11807061,9987115,14679237,18689476,15317791,17586624,11684022,12923101,17560370,12598648,16899079,19226326,9890793,,9987115,11544224 14763982 9643546, 19767395 11112444 9535081 </pubmed> | + | <pubmed>17380125,9643546,10809708,11807061,9987115,14679237,18689476,15317791,17586624,11684022,12923101,17560370,12598648,16899079,19226326,9890793,,9987115,11544224 14763982 9643546, 19767395 11112444 9535081 18689473</pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] | ||
Revision as of 05:58, 15 January 2010
- 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 |
| Metabolic function and regulation of this protein in SubtiPathways: 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
| |
Contents
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):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Localization: cytoplasmic polar clusters, excluded from the nucleoid, induced clustering upon heat shock, colocalization with ClpX, ClpC and ClpE PubMed
Database entries
- Structure: Two homologue structures resolved 1TYF, 1Y7O, structural model of B. subtilis ClpP available from hstrahl
- 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:
- clpP::spec and clpP::cat available , available in the Leendert Hamoen lab
- GP551 (spc), available in the Stülke lab
- 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
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)
Original Publications
