Difference between revisions of "FusA"
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=== Database entries === | === Database entries === | ||
− | * '''Structure:''' | + | * '''Structure:''' [http://www.rcsb.org/pdb/explore/explore.do?pdbId=1ELO 1ELO] (from ''Thermus thermophilus'') {{PubMed|8070397}} |
* '''UniProt:''' [http://www.uniprot.org/uniprot/P80868 P80868] | * '''UniProt:''' [http://www.uniprot.org/uniprot/P80868 P80868] | ||
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=References= | =References= | ||
− | <pubmed> 17726680, 17218307 20348921 </pubmed> | + | <pubmed> 17726680, 17218307 20348921 8070397 </pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 17:14, 31 March 2010
- 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
- Locus tag: BSU01120
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: hydrolyses GTP
- 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
- UniProt: P80868
- KEGG entry: [2]
- E.C. number:
Additional information
Expression and regulation
- Operon:
- Regulatory mechanism:
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Nina Clementi, Anna Chirkova, Barbara Puffer, Ronald Micura, Norbert Polacek
Atomic mutagenesis reveals A2660 of 23S ribosomal RNA as key to EF-G GTPase activation.
Nat Chem Biol: 2010, 6(5);344-51
[PubMed:20348921]
[WorldCat.org]
[DOI]
(I p)
Christine Eymann, Dörte Becher, Jörg Bernhardt, Katrin Gronau, Anja Klutzny, Michael Hecker
Dynamics of protein phosphorylation on Ser/Thr/Tyr in Bacillus subtilis.
Proteomics: 2007, 7(19);3509-26
[PubMed:17726680]
[WorldCat.org]
[DOI]
(P p)
Boris Macek, Ivan Mijakovic, Jesper V Olsen, Florian Gnad, Chanchal Kumar, Peter R Jensen, Matthias Mann
The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis.
Mol Cell Proteomics: 2007, 6(4);697-707
[PubMed:17218307]
[WorldCat.org]
[DOI]
(P p)
A AEvarsson, E Brazhnikov, M Garber, J Zheltonosova, Y Chirgadze, S al-Karadaghi, L A Svensson, A Liljas
Three-dimensional structure of the ribosomal translocase: elongation factor G from Thermus thermophilus.
EMBO J: 1994, 13(16);3669-77
[PubMed:8070397]
[WorldCat.org]
[DOI]
(P p)