Difference between revisions of "CtsR"

From SubtiWiki
Jump to: navigation, search
Line 31: Line 31:
 
  <div align="right"> <small>This image was kindly provided by [http://genolist.pasteur.fr/SubtiList/ SubtiList]</small></div>
 
  <div align="right"> <small>This image was kindly provided by [http://genolist.pasteur.fr/SubtiList/ SubtiList]</small></div>
 
|-
 
|-
|colspan="2" |'''[http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=ctsR_101449_101913_1 Expression at a glance]'''&#160;&#160;&#160;{{PubMed|22383849}}<br/>[[Image:ctsR_expression.png|500px]]
+
|colspan="2" |'''[http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=ctsR_101449_101913_1 Expression at a glance]'''&#160;&#160;&#160;{{PubMed|22383849}}<br/>[[Image:ctsR_expression.png|500px|link=http://subtiwiki.uni-goettingen.de/apps/expression/expression.php?search=BSU00830]]
 
|-
 
|-
 
|}
 
|}

Revision as of 12:20, 16 May 2013

  • Description: transcription repressor of class III heat shock genes (clpC operon, clpE, clpP)

Gene name ctsR
Synonyms yacG
Essential no
Product transcription repressor
Function regulation of protein degradation
Gene expression levels in SubtiExpress: ctsR
Interactions involving this protein in SubtInteract: CtsR
Regulatory function and regulation of this protein in SubtiPathways:
Stress, Phosphorelay
MW, pI 17 kDa, 9.261
Gene length, protein length 462 bp, 154 aa
Immediate neighbours rrnW-5S, mcsA
Sequences Protein DNA DNA_with_flanks
Genetic context
CtsR context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
CtsR expression.png















Categories containing this gene/protein

proteolysis, transcription factors and their control, general stress proteins (controlled by SigB), heat shock proteins, phosphoproteins

This gene is a member of the following regulons

CtsR regulon, SigB regulon

The CtsR regulon

The gene

Basic information

  • Locus tag: BSU00830

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family: ctsR family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
    • phosphorylation of a tyrosine residue by McsB PubMed
    • recently, it was reported that CtsR is phosphorylated by McsB on Arg-62 rather than on a tyrosine residue PubMed
    • in addition, Arg-15 was reported to be a phosphorylation site PubMed
  • Cofactor(s):
  • Effectors of protein activity:
    • CtsR is inactivated by heat, heat sensing requires Gly-64 PubMed
    • non-phosphorylated McsB targets CtsR for degradation PubMed
    • regulated proteolysis by ClpP/ClpC PubMed

Database entries

  • Structure: 3H0D (complex with a 26bp DNA duplex, from Geobacillus stearothermophilus) PubMed
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Regulatory mechanism:
  • Additional information: the mRNA is very stable (half-life > 15 min) PubMed

Biological materials

  • Mutant: ctsR::aphA3 availbale from the Gerth lab

ctsRG65P::spec available from the Gerth lab

  • Expression vector: for expression, purification in E. coli with N-terminal His-tag, pRSETA available in Gerth lab
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody: available in Gerth lab

Labs working on this gene/protein

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)

Alexander K W Elsholz, Ulf Gerth, Michael Hecker
Regulation of CtsR activity in low GC, Gram+ bacteria.
Adv Microb Physiol: 2010, 57;119-44
[PubMed:21078442] [WorldCat.org] [DOI] (I p)

Wolfgang Schumann
The Bacillus subtilis heat shock stimulon.
Cell Stress Chaperones: 2003, 8(3);207-17
[PubMed:14984053] [WorldCat.org] [DOI] (P p)

Original publications

Additional publications: PubMed