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tufA [Mon Jan 18 2016 18:50:21 GMT+0100 (CET)]
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tufA [Mon Jan 18 2016 18:50:21 GMT+0100 (CET)]

elongation factor Tu
43.00 kDa
elongation factor Tu

Genomic Context



  • [category|SW 3|Information processing] → [category|SW 3.3|Protein synthesis, modification and degradation] → [category|SW 3.3.1|Translation] → [category|SW|Translation factors]
  • [category|SW 6|Groups of genes] → [category|SW 6.1|Essential genes]
  • [category|SW 6|Groups of genes] → [category|SW 6.2|Membrane proteins]
  • [category|SW 6|Groups of genes] → [category|SW 6.4|Phosphoproteins] → [category|SW 6.4.1|Phosphorylation on an Arg residue]
  • [category|SW 6|Groups of genes] → [category|SW 6.4|Phosphoproteins] → [category|SW 6.4.7|Phosphorylation on a Tyr residue]
  • [category|SW 6|Groups of genes] → [category|SW 6.4|Phosphoproteins] → [category|SW 6.4.8|Phosphorylation on either a Ser, Thr or Tyr residue]
  • [SW|Categories] containing this gene/protein

  • [SW|translation], [SW|essential genes], [SW|membrane proteins], [SW|phosphoproteins], [SW|most abundant proteins]
  • This gene is a member of the following [SW|regulons]

  • [SW|stringent response]
  • Gene

    Coordinates on the chromosome (coding sequence)
    132,882 -> 134,072

    Phenotypes of a mutant

  • essential [Pubmed|12682299]
  • The protein

    Protein family

  • EF-Tu/EF-1A subfamily (according to Swiss-Prot)
  • Modification

  • phosphorylated on Thr-384 by [protein|search|PrkC], dephosphorylated by [protein|search|PrpC] [Pubmed|19246764], [Pubmed|17726680]
  • Cys83 is S-bacillithiolated in B. subtilis and other Bacillus species [Pubmed|22938038]
  • phosphorylated on several Arg residues [Pubmed|24263382]
  • phosphorylated during [SW|sporulation] on Thr-63 by [protein|search|YabT], dephosphorylated by [protein|search|PrpC] [Pubmed|26056311]
  • phosphorylated on Tyr-270 [Pubmed|26381121]
  • Effectors of protein activity

  • phosphorylation by YabT results in inhibtion of GTP hydrolysis; as a result, EF-Tu remains stably bound
  • to the [SW|ribosome], stalling protein [SW|translation] [Pubmed|26056311]
  • Structure

  • [PDB|3U6B] (from ''E. coli '', 77% identity) [Pubmed|21999529]
  • [SW|Localization]

  • EF-Tu localizes in a helical pattern underneath the cell membrane and colocalizes with [protein|search|MreB] [Pubmed|20133608]
  • membrane [Pubmed|18763711]
  • [SW|Interactions]

  • [protein|search|MreB]-[protein|search|TufA] [Pubmed|20133608]
  • [protein|search|YabT]-[tufA|search|EF-tu] [Pubmed|26056311]
  • [protein|search|PrpC]-[tufA|search|EF-tu] [Pubmed|26056311]
  • Expression and Regulation


  • [protein|search|RelA] dependent downregulation (Class I) during stringent response [Pubmed|11948165]
  • Additional information

  • belongs to the 100 [SW|most abundant proteins] [PubMed|15378759]
  • Biological materials

    Expression vector

  • for expression/ purification from ''B. subtilis'' with N-terminal Strep-tag, for [SW|SPINE], in [SW|pGP380]: pGP839, available in [SW|Stülke] lab
  • for expression/ purification from ''E. coli'' with N-terminal His-tag, in [SW|pWH844]: pGP847, available in [SW|Stülke] lab
  • References

  • 22938038,19246764,20133608,25707802,19246764,17726680,18763711,24263382,15378759,25676310,26056311,26381121