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Protein Sci. 2006 Apr;15(4):935-41. Epub 2006 Mar 7.

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

Author information

1
Division of Immunity & Infection, University of Birmingham Medical School, Edgbaston, Birmingham B15 2TT, United Kingdom. m.pallen@bham.ac.uk

Abstract

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).

PMID:
16522800
PMCID:
PMC2242474
DOI:
10.1110/ps.051958806
[Indexed for MEDLINE]
Free PMC Article
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