Elongation factor Tu is a multifunctional and processed moonlighting protein

Sci Rep. 2017 Sep 11;7(1):11227. doi: 10.1038/s41598-017-10644-z.


Many bacterial moonlighting proteins were originally described in medically, agriculturally, and commercially important members of the low G + C Firmicutes. We show Elongation factor Tu (Ef-Tu) moonlights on the surface of the human pathogens Staphylococcus aureus (SaEf-Tu) and Mycoplasma pneumoniae (MpnEf-Tu), and the porcine pathogen Mycoplasma hyopneumoniae (MhpEf-Tu). Ef-Tu is also a target of multiple processing events on the cell surface and these were characterised using an N-terminomics pipeline. Recombinant MpnEf-Tu bound strongly to a diverse range of host molecules, and when bound to plasminogen, was able to convert plasminogen to plasmin in the presence of plasminogen activators. Fragments of Ef-Tu retain binding capabilities to host proteins. Bioinformatics and structural modelling studies indicate that the accumulation of positively charged amino acids in short linear motifs (SLiMs), and protein processing promote multifunctional behaviour. Codon bias engendered by an A + T rich genome may influence how positively-charged residues accumulate in SLiMs.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Computational Biology
  • Fibrinolysin / metabolism
  • Host-Pathogen Interactions
  • Membrane Proteins / metabolism
  • Models, Molecular
  • Mycoplasma hyopneumoniae / enzymology*
  • Mycoplasma hyopneumoniae / genetics
  • Mycoplasma pneumoniae / enzymology*
  • Mycoplasma pneumoniae / genetics
  • Peptide Elongation Factor Tu / metabolism*
  • Plasminogen / metabolism
  • Protein Binding
  • Staphylococcus aureus / enzymology*
  • Staphylococcus aureus / genetics
  • Virulence Factors / metabolism*


  • Membrane Proteins
  • Virulence Factors
  • Plasminogen
  • Fibrinolysin
  • Peptide Elongation Factor Tu