Difference between revisions of "CspB"

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=== Database entries ===
 
=== Database entries ===
  
* '''Structure:''' [http://www.rcsb.org/pdb/explore.do?structureId=1NMG 1NMG] (NMR)
+
* '''Structure:''' [http://www.rcsb.org/pdb/explore.do?structureId=1CSQ 1CSQ],  [http://www.rcsb.org/pdb/explore.do?structureId=1NMG 1NMG] (NMR)
  
 
* '''Swiss prot entry:''' [http://www.uniprot.org/uniprot/P32081 P32081]
 
* '''Swiss prot entry:''' [http://www.uniprot.org/uniprot/P32081 P32081]

Revision as of 21:52, 5 May 2009

  • Description: major cold-shock protein

Gene name cspB
Synonyms
Essential no
Product major cold-shock protein
Function RNA chaperone
MW, pI 7 kDa, 4.341
Gene length, protein length 201 bp, 67 aa
Immediate neighbours yhcI, yhcJ
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
CspB context.gif
This image was kindly provided by SubtiList



The gene

Basic information

  • Coordinates:

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:
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:
  • Localization: cytoplasm (according to Swiss-Prot), cytoplasma, colocalizes with the ribosomes PubMed

Database entries

  • KEGG entry: [3]
  • E.C. number:

Additional information

  • subject to Clp-dependent proteolysis upon glucose starvation PubMed

Expression and regulation

  • Operon:
  • Regulation:
  • Regulatory mechanism:
  • Additional information: subject to Clp-dependent proteolysis upon glucose starvation PubMed

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Mohamed Marahiel, Marburg University, Germany homepage

Your additional remarks

References

  1. Gerth et al. (2008) Clp-dependent proteolysis down-regulates central metabolic pathways in glucose-starved Bacillus subtilis. J Bacteriol 190:321-331 PubMed
  2. Hunger, K., Beckering, C. L., Wiegeshoff, F., Graumann, P. L. & Marahiel, M. A. (2006). Cold-induced putative DEAD box RNA helicases CshA and CshB are essential for cold adaptation and interact with cold shock protein B in Bacillus subtilis. J Bacteriol. 188:240-248. PubMed
  3. Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed