Difference between revisions of "FusA"

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* '''Description:''' elongation factor G <br/><br/>
  
 
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|style="background:#ABCDEF;" align="center"|'''Function''' || translation  
 
|style="background:#ABCDEF;" align="center"|'''Function''' || translation  
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|colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http://cellpublisher.gobics.de/subtiexpress/ ''Subti''Express]''': [http://cellpublisher.gobics.de/subtiexpress/bsu/BSU01120 fusA]
 
 
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|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 76 kDa, 4.615   
 
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 76 kDa, 4.615   
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|colspan="2" | '''Genetic context''' <br/> [[Image:fusA_context.gif]]
 
|colspan="2" | '''Genetic context''' <br/> [[Image:fusA_context.gif]]
 
  <div align="right"> <small>This image was kindly provided by [http://genolist.pasteur.fr/SubtiList/ SubtiList]</small></div>
 
  <div align="right"> <small>This image was kindly provided by [http://genolist.pasteur.fr/SubtiList/ SubtiList]</small></div>
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|colspan="2" |'''[http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=fusA_130684_132762_1 Expression at a glance]'''&#160;&#160;&#160;{{PubMed|22383849}}<br/>[[Image:fusA_expression.png|500px]]
 
 
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* '''Operon:'''  
 
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* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=fusA_130684_132762_1 fusA] {{PubMed|22383849}}
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=Biological materials =
 
=Biological materials =

Revision as of 10:14, 7 August 2012

  • 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



Categories containing this gene/protein

translation, essential genes, phosphoproteins

This gene is a member of the following regulons

stringent response

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:

Database entries

  • Structure: 1ELO (from Thermus thermophilus) PubMed
  • KEGG entry: [2]
  • E.C. number:

Additional information

Expression and regulation

  • Operon:
  • Regulation:
    • RelA dependent downregulation (Class I) during stringent response PubMed
  • Regulatory mechanism:
  • Additional information:

Biological materials

  • Mutant:
  • Expression vector:
    • for expression/ purification from B. subtilis with N-terminal Strep-tag, for SPINE, in pGP380: pGP840, available in Stülke lab
    • for expression/ purification from E. coli with N-terminal His-tag, in pWH844: pGP848, available in Stülke lab
  • 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)

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