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

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 FoF1 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 FoF1 ATPase (the b and δ subunits).