FusA

• 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 This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

translation, essential genes, phosphoproteins, most abundant proteins

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

• BsubCyc: BSU01120

• DBTBS entry: no entry

• SubtiList entry: [1]

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

• Cofactors:

• Effectors of protein activity:

• Interactions:
  • FusA-RplL PubMed
  • FusA-RpsL PubMed

• Localization: cytoplasm (according to Swiss-Prot)

Database entries

• BsubCyc: BSU01120

• Structure:
  • 1ELO (from Thermus thermophilus) PubMed
  • 4BTC, 4BTD, the Thermus thermophilus EF-G–ribosome complex in a pretranslocation state PubMed

• UniProt: P80868

• KEGG entry: [2]

• E.C. number:

Expression and regulation

• Operon:

• Expression browser: fusA PubMed

• Sigma factor:

• Regulation:
  • RelA dependent downregulation (Class I) during stringent response PubMed

• Regulatory mechanism:

• Additional information:
  • belongs to the 100 most abundant proteins PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium): 11452 PubMed
  • number of protein molecules per cell (complex medium with amino acids, without glucose): 49524 PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 23259 PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 12858 PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 16612 PubMed

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:

References

Wolf Holtkamp, Carlos E Cunha, Frank Peske, Andrey L Konevega, Wolfgang Wintermeyer, Marina V Rodnina
GTP hydrolysis by EF-G synchronizes tRNA movement on small and large ribosomal subunits.
EMBO J: 2014, 33(9);1073-85
[PubMed:24614227] [WorldCat.org] [DOI] (I p)

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)

Christine Eymann, Annette Dreisbach, Dirk Albrecht, Jörg Bernhardt, Dörte Becher, Sandy Gentner, Le Thi Tam, Knut Büttner, Gerrit Buurman, Christian Scharf, Simone Venz, Uwe Völker, Michael Hecker
A comprehensive proteome map of growing Bacillus subtilis cells.
Proteomics: 2004, 4(10);2849-76
[PubMed:15378759] [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)