Evolutionary links between FliH/YscL-like proteins from bacterial type III secretion systems and second-stalk components of the FoF1 and vacuolar ATPases

Protein Sci. 2006 Apr;15(4):935-41. doi: 10.1110/ps.051958806. Epub 2006 Mar 7.


Bacterial type III secretion drives flagellar biosynthesis and mediates bacterial-eukaryotic interactions. Type III secretion is driven by an ATPase that is homologous to the catalytic subunits of proton-translocating ATPases, such as the F(o)F(1) ATPase. Here we use PSI-BLAST searches to show that some noncalatytic components are also conserved between type III secretion systems and proton-translocating ATPases. In particular, we show that the FliH/YscL-like proteins and the E subunits of vacuolar ATPases represent fusions of domains homologous to second-stalk components of the F(o)F(1) ATPase (the b and delta subunits).

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / genetics*
  • Bacterial Proteins / metabolism
  • Computational Biology
  • Conserved Sequence
  • Evolution, Molecular*
  • Humans
  • Models, Biological
  • Molecular Sequence Data
  • Protein Subunits / chemistry
  • Protein Subunits / genetics
  • Protein Subunits / metabolism
  • Proton-Translocating ATPases / chemistry
  • Proton-Translocating ATPases / genetics*
  • Proton-Translocating ATPases / metabolism
  • Sequence Alignment
  • Sequence Homology
  • Vacuolar Proton-Translocating ATPases / chemistry
  • Vacuolar Proton-Translocating ATPases / genetics*
  • Vacuolar Proton-Translocating ATPases / metabolism


  • Bacterial Proteins
  • Protein Subunits
  • fliH protein, Bacteria
  • Vacuolar Proton-Translocating ATPases
  • Proton-Translocating ATPases