Difference between revisions of "FusA"
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* '''Swiss prot entry:''' [http://www.uniprot.org/uniprot/P80868 P80868] | * '''Swiss prot entry:''' [http://www.uniprot.org/uniprot/P80868 P80868] | ||
− | * '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu+BSU01120] | + | * '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu+BSU01120 BSU01120] |
* '''E.C. number:''' | * '''E.C. number:''' |
Revision as of 22:53, 13 May 2009
- Description: elongation factor G
Gene name | fusA |
Synonyms | fus |
Essential | yes PubMed |
Product | elongation factor G |
Function | translation |
MW, pI | 76 kDa, 4.615 |
Gene length, protein length | 2076 bp, 692 aa |
Immediate neighbours | rpsG, tufA |
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
essential PubMed
Database entries
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- Protein family: EF-G/EF-2 subfamily (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification: phosphorylation on Ser-213 AND Ser-302 AND Ser-569 AND Ser-680 AND (Thr-24 OR Thr-25) AND (Thr-43 OR Ser 48) PubMed, PubMed
- Cofactor(s):
- Effectors of protein activity:
- Interactions:
- Localization: cytoplasm (according to Swiss-Prot)
Database entries
- Structure:
- Swiss prot entry: P80868
- KEGG entry: BSU01120
- E.C. number:
Additional information
Expression and regulation
- Operon:
- Regulation:
- Regulatory mechanism:
- Additional information:
Biological materials
- Mutant:
- Expression vector: pGP840 (N-terminal Strep-tag, purification from B. subtilis, for SPINE, in pGP380), available in Stülke lab
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
- Eymann et al. (2007) Dynamics of protein phosphorylation on Ser/Thr/Tyr in Bacillus subtilis. Proteomics 7: 3509-3526. PubMed
- Macek et al. (2007) The serine/ threonine/ tyrosine phosphoproteome of the model bacterium Bacillus subtilis. Mol. Cell. Proteomics 6: 697-707 PubMed
- Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed