Difference between revisions of "FusA"

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=== Basic information ===
 
=== Basic information ===
  
* '''Locus tag:'''
+
* '''Locus tag:''' BSU01120
  
 
===Phenotypes of a mutant ===
 
===Phenotypes of a mutant ===
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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 BSU01120]
+
* '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu+BSU01120]
  
 
* '''E.C. number:'''
 
* '''E.C. number:'''

Revision as of 09:29, 3 June 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
FusA context.gif
This image was kindly provided by SubtiList



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:
  • 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:
  • KEGG entry: [2]
  • 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

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)


  1. Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed