Difference between revisions of "ClpE"

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|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[motA]]'', ''[[ykvI]]''
 
|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[motA]]'', ''[[ykvI]]''
 
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|style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU13700 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU13700 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU13700 Advanced_DNA]
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|style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU13700 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU13700 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU13700 DNA_with_flanks]
 
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|colspan="2" | '''Genetic context''' <br/> [[Image:clpE_context.gif]]
 
|colspan="2" | '''Genetic context''' <br/> [[Image:clpE_context.gif]]

Revision as of 10:03, 14 May 2013

  • Description: ATP-dependent Clp protease-like (class III stress gene)

Gene name clpE
Synonyms ykvH
Essential no
Product ATP-dependent Clp protease-like
Function protein degradation
Gene expression levels in SubtiExpress: clpE
Interactions involving this protein in SubtInteract: ClpE
Metabolic function and regulation of this protein in SubtiPathways:
Stress
MW, pI 77 kDa, 5.135
Gene length, protein length 2097 bp, 699 aa
Immediate neighbours motA, ykvI
Sequences Protein DNA DNA_with_flanks
Genetic context
ClpE context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
ClpE expression.png















Categories containing this gene/protein

proteolysis, heat shock proteins

This gene is a member of the following regulons

CtsR regulon

The gene

Basic information

  • Locus tag: BSU13700

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

  • A mutation was found in this gene after evolution under relaxed selection for sporulation PubMed


The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: ATPase/chaperone
  • Protein family: AAA+ -type ATPase (IPR013093) InterPro (PF07724) PFAM

Extended information on the protein

  • Kinetic information:
  • Domains: AAA-ATPase PFAM
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:
  • Localization:
    • localization in cytoplasmic polar clusters, excluded from the nucleoid, colocalization with ClpP Pubmed
    • forms foci coincident with nucleoid edges, usually near cell poles PubMed

ClpE.jpg

Database entries

  • Structure:
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Regulatory mechanism:
  • Additional information:

Biological materials

  • Mutant: clpE::spec available from the Hamoen] Lab
  • Expression vector:
  • lacZ fusion:
  • GFP fusion: C-terminal YFP and CFP fusions (single copy) available from the 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

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)

Original Publications

Additional publications: PubMed

Christopher T Brown, Laura K Fishwick, Binna M Chokshi, Marissa A Cuff, Jay M Jackson, Travis Oglesby, Alison T Rioux, Enrique Rodriguez, Gregory S Stupp, Austin H Trupp, James S Woollcombe-Clarke, Tracy N Wright, William J Zaragoza, Jennifer C Drew, Eric W Triplett, Wayne L Nicholson
Whole-genome sequencing and phenotypic analysis of Bacillus subtilis mutants following evolution under conditions of relaxed selection for sporulation.
Appl Environ Microbiol: 2011, 77(19);6867-77
[PubMed:21821766] [WorldCat.org] [DOI] (I p)

E Krüger, D Zühlke, E Witt, H Ludwig, M Hecker
Clp-mediated proteolysis in Gram-positive bacteria is autoregulated by the stability of a repressor.
EMBO J: 2001, 20(4);852-63
[PubMed:11179229] [WorldCat.org] [DOI] (P p)

I Derré, G Rapoport, K Devine, M Rose, T Msadek
ClpE, a novel type of HSP100 ATPase, is part of the CtsR heat shock regulon of Bacillus subtilis.
Mol Microbiol: 1999, 32(3);581-93
[PubMed:10320580] [WorldCat.org] [DOI] (P p)

I Derré, G Rapoport, T Msadek
CtsR, a novel regulator of stress and heat shock response, controls clp and molecular chaperone gene expression in gram-positive bacteria.
Mol Microbiol: 1999, 31(1);117-31
[PubMed:9987115] [WorldCat.org] [DOI] (P p)