A cyclophilin-like peptidyl-prolyl cis/trans isomerase from Legionella pneumophila--characterization, molecular cloning and overexpression.

@article{Schmidt1996ACP,
  title={A cyclophilin-like peptidyl-prolyl cis/trans isomerase from Legionella pneumophila--characterization, molecular cloning and overexpression.},
  author={Beat Schmidt and Thomas Tradler and J U Rahfeld and Bernd Ludwig and Bhagyachand Jain and Karlheinz Mann and Karl Peter R{\"u}cknagel and Bernhard Janowski and Angelika Schierhorn and Gerhard Kuellertz and Joerg Hacker and Gabriele Fischer},
  journal={Molecular microbiology},
  year={1996},
  volume={21 6},
  pages={
          1147-60
        }
}
Legionella pneumophila is the causative agent of a severe form of pneumonia in humans (Legionnaires' disease). A major virulence factor, the Mip protein (FK506-binding protein, FKBP25mem), belongs to the enzyme family of peptidyl-prolyl cis/trans isomerases (PPlases). Here we show that L. pneumophila Philadelphia I possesses an additional cytoplasmic PPlase at a level of enzyme activity comparable to that of FKBP25mem. The N-terminal amino acid sequence of the purified protein was obtained by… CONTINUE READING

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