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 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).
Pallen
Mark J
MJ
Division of Immunity & Infection, University of Birmingham Medical School, Edgbaston, Birmingham B15 2TT, United Kingdom. m.pallen@bham.ac.uk
Bailey
Christopher M
CM
Beatson
Scott A
SA
D000595:Amino Acid Sequence; D000818:Animals; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D019295:Computational Biology; D017124:Conserved Sequence; D019143:Evolution, Molecular; D006801:Humans; D008954:Models, Biological; D008969:Molecular Sequence Data; D021122:Protein Subunits / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D006180:Proton-Translocating ATPases / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D016415:Sequence Alignment; D017385:Sequence Homology; D025262:Vacuolar Proton-Translocating ATPases / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism
D001426:Bacterial Proteins; D021122:Protein Subunits; C069250:fliH protein, Bacteria; D025262:Vacuolar Proton-Translocating ATPases; D006180:Proton-Translocating ATPases