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For The Record

Evolutionary links between FliH/YscL-like proteins from bacterial type III secretion systems and second-stalk components of the F_oF₁ and vacuolar ATPases

Division of Immunity & Infection, University of Birmingham Medical School, Edgbaston, Birmingham,B15 2TT, United Kingdom

(RECEIVED November 8, 2005; FINAL REVISION December 1, 2005; ACCEPTED December 1, 2005)

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_oF₁ ATPase. Here we use PSI-BLAST searches to show that some noncalatytic components are also conserved between type III secretion systems and protontranslocating 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_oF₁ ATPase (the b and subunits).

Keywords: F_oF₁ ATPase; vacuolar ATPase; bacterial flagellum; FliH; YscL; type III secretion; sequence homology; evolution

Article published online ahead of print. Article and publication date are at http://www.proteinscience.org/cgi/doi/10.1110/ps.051958806

Supplementary material: see www.proteinscience.org

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