Difference between revisions of "CspB"
Line 76: | Line 76: | ||
=== 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 This image was kindly provided by SubtiList
|
Contents
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
- Swiss prot entry: P32081
- 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
- Gerth et al. (2008) Clp-dependent proteolysis down-regulates central metabolic pathways in glucose-starved Bacillus subtilis. J Bacteriol 190:321-331 PubMed
- 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
- Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed