Identification of methionine-processed HPr in the equine pathogen Streptococcus equi
Sutcliffe, I.C. Trigg, J. Harrington, Dean J.
Sutcliffe, I.C.
Trigg, J.
Harrington, Dean J.
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2000-10
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Using preparative electrophoresis, a low molecular weight protein has been partially purified from a cell extract of the equine pathogen Streptococcus equi susp. equi. N-terminal sequence analysis and Western blotting revealed the protein to be HPr, a central component of the phosphoenolpyruvate:sugar phosphotransferase system (PTS). Interestingly, the only form of the HPr protein detected in S. equi was one with the amino-terminal methionine removed, a modification that has previously been associated with surface localization of streptococcal HPr proteins.
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Sutcliffe IC, Trigg J and Harrington DJ (2000) Identification of methionine-processed HPr in the equine pathogen Streptococcus equi. Systematic and Applied Microbiology. 23(3): 330-332.
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