Difference between revisions of "CshA"
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* '''Structure:''' | * '''Structure:''' | ||
− | * '''Swiss prot entry:''' | + | * '''Swiss prot entry:''' [http://www.uniprot.org/uniprot/P96614 P96614] |
* '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu+BSU04580] | * '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu+BSU04580] |
Revision as of 16:16, 4 May 2009
- Description: DEAD-box RNA helicase
Gene name | cshA |
Synonyms | ydbR |
Essential | no |
Product | DEAD-box RNA helicase |
Function | RNA helicase |
MW, pI | 57 kDa, 9.89 |
Gene length, protein length | 1533 bp, 511 aa |
Immediate neighbours | murF, ydbS |
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: no entry
- SubtiList entry: [1]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: RNA helicase
- Protein family: DEAD-box RNA helicase
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Interactions:
- Localization: cytoplasm (according to Swiss-Prot), cytoplasma, colocalizes with the ribosomes PubMed
Database entries
- Structure:
- Swiss prot entry: P96614
- KEGG entry: [2]
- E.C. number:
Additional information
Expression and regulation
- Operon:
- Sigma factor:
- Regulation:
- Regulatory mechanism:
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Stülke lab
- Antibody:
Labs working on this gene/protein
Mohamed Marahiel, Marburg University, Germany homepage
Your additional remarks
References
- 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
- Ando, Y. and K. Nakamura (2006) Bacillus subtilis DEAD protein YdbR possesses ATPase, RNA binding, and RNA unwinding activities.Biosci. Biotechnol. Biochem. 70: 1606-1615. PubMed
- Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed