Difference between revisions of "FusA"

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* '''Description:''' elongation factor G <br/><br/>
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* '''Description:''' elongation factor G, facilitates movement of tRNA–mRNA by one codon <br/><br/>
  
 
{| align="right" border="1" cellpadding="2"  
 
{| align="right" border="1" cellpadding="2"  
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|style="background:#ABCDEF;" align="center"| '''Product''' || elongation factor G
 
|style="background:#ABCDEF;" align="center"| '''Product''' || elongation factor G
 
|-
 
|-
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|style="background:#ABCDEF;" align="center"|'''Function''' || translation  
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|style="background:#ABCDEF;" align="center"|'''Function''' || [[translation]]
 
|-
 
|-
 
|colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http://subtiwiki.uni-goettingen.de/apps/expression/ ''Subti''Express]''': [http://subtiwiki.uni-goettingen.de/apps/expression/expression.php?search=BSU01120 fusA]
 
|colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http://subtiwiki.uni-goettingen.de/apps/expression/ ''Subti''Express]''': [http://subtiwiki.uni-goettingen.de/apps/expression/expression.php?search=BSU01120 fusA]
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|-
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|colspan="2" style="background:#FAF8CC;" align="center"| '''Interactions involving this protein in [http://cellpublisher.gobics.de/subtinteract/startpage/start/ ''Subt''Interact]''': [http://cellpublisher.gobics.de/subtinteract/interactionList/2/FusA FusA]
 
|-
 
|-
 
|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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<br/><br/><br/><br/>
 
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* '''[[SubtInteract|Interactions]]:'''
 
* '''[[SubtInteract|Interactions]]:'''
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** FusA-RplL {{PubMed|23912278}}
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** FusA-RpsL {{PubMed|23912278}}
  
 
* '''[[Localization]]:''' cytoplasm (according to Swiss-Prot)
 
* '''[[Localization]]:''' cytoplasm (according to Swiss-Prot)
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=== Database entries ===
 
=== Database entries ===
  
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* '''Structure:''' [http://www.rcsb.org/pdb/explore/explore.do?pdbId=1ELO 1ELO] (from ''Thermus thermophilus'') {{PubMed|8070397}}
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* '''Structure:'''  
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** [http://www.rcsb.org/pdb/explore/explore.do?pdbId=1ELO 1ELO] (from ''Thermus thermophilus'') {{PubMed|8070397}}
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** [http://www.pdb.org/pdb/explore/explore.do?structureId=4BTC 4BTC], [http://www.pdb.org/pdb/explore/explore.do?structureId=4BTD 4BTD], the ''Thermus thermophilus'' EF-G–[[ribosome]] complex in a pretranslocation state {{PubMed|23912278}}
  
 
* '''UniProt:''' [http://www.uniprot.org/uniprot/P80868 P80868]
 
* '''UniProt:''' [http://www.uniprot.org/uniprot/P80868 P80868]
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* '''Expression vector:'''  
 
* '''Expression vector:'''  
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** for expression/ purification from ''B. subtilis'' with N-terminal Strep-tag, for [[SPINE]], in [[pGP380]]: pGP840, available in [[Stülke]] lab
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** for expression/ purification from ''B. subtilis'' with N-terminal Strep-tag, for [[SPINE]], in [[pGP380]]: pGP840, available in [[Jörg Stülke]]'s lab
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** for expression/ purification from ''E. coli'' with N-terminal His-tag, in [[pWH844]]: pGP848, available in [[Stülke]] lab
+
** for expression/ purification from ''E. coli'' with N-terminal His-tag, in [[pWH844]]: pGP848, available in [[Jörg Stülke]]'s lab
 
      
 
      
 
* '''lacZ fusion:'''
 
* '''lacZ fusion:'''
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=References=
 
=References=
  
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<pubmed> 17726680, 17218307 20348921 8070397 </pubmed>
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<pubmed> 17726680, 17218307 20348921 8070397 23912278</pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 11:28, 20 August 2013

  • Description: elongation factor G, facilitates movement of tRNA–mRNA by one codon

Gene name fusA
Synonyms fus
Essential yes PubMed
Product elongation factor G
Function translation
Gene expression levels in SubtiExpress: fusA
Interactions involving this protein in SubtInteract: FusA
MW, pI 76 kDa, 4.615
Gene length, protein length 2076 bp, 692 aa
Immediate neighbours rpsG, tufA
Sequences Protein DNA DNA_with_flanks
Genetic context
FusA context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
FusA expression.png















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

  • KEGG entry: [2]
  • E.C. number:

Additional information

Expression and regulation

  • Operon:
  • Sigma factor:
  • 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 Jörg Stülke's lab
    • for expression/ purification from E. coli with N-terminal His-tag, in pWH844: pGP848, available in Jörg Stülke's lab
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Yun Chen, Shu Feng, Veerendra Kumar, Rya Ero, Yong-Gui Gao
Structure of EF-G-ribosome complex in a pretranslocation state.
Nat Struct Mol Biol: 2013, 20(9);1077-84
[PubMed:23912278] [WorldCat.org] [DOI] (I p)

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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