Difference between revisions of "ClpP"
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|style="background:#ABCDEF;" align="center"|'''Function''' || protein degradation | |style="background:#ABCDEF;" align="center"|'''Function''' || protein degradation | ||
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− | |colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http:// | + | |colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http://subtiwiki.uni-goettingen.de/apps/expression/ ''Subti''Express]''': [http://subtiwiki.uni-goettingen.de/apps/expression/expression.php?search=BSU34540 clpP] |
|- | |- | ||
|colspan="2" style="background:#FAF8CC;" align="center"| '''Interactions involving this protein in [http://cellpublisher.gobics.de/subtinteract/startpage/start/ ''Subt''Interact]''': [http://cellpublisher.gobics.de/subtinteract/interactionList/2/ClpP ClpP] | |colspan="2" style="background:#FAF8CC;" align="center"| '''Interactions involving this protein in [http://cellpublisher.gobics.de/subtinteract/startpage/start/ ''Subt''Interact]''': [http://cellpublisher.gobics.de/subtinteract/interactionList/2/ClpP ClpP] | ||
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|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[trnQ-Arg]]'', ''[[pgcM]]'' | |style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[trnQ-Arg]]'', ''[[pgcM]]'' | ||
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− | | | + | |style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU34540 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU34540 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU34540 Advanced_DNA] |
|- | |- | ||
|colspan="2" | '''Genetic context''' <br/> [[Image:clpP_context.gif]] | |colspan="2" | '''Genetic context''' <br/> [[Image:clpP_context.gif]] |
Revision as of 13:55, 13 May 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 |
Sequences | Protein DNA Advanced_DNA |
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