Identification of methionine-processed HPr in the equine pathogen Streptococcus equi
Publication date
2000-10Keyword
HPr; Strangles; StreptococcusPeer-Reviewed
Yes
Metadata
Show full item recordAbstract
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.Version
No full-text in the repositoryCitation
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.Link to Version of Record
https://doi.org/10.1016/S0723-2020(00)80061-2Type
Articleae974a485f413a2113503eed53cd6c53
https://doi.org/10.1016/S0723-2020(00)80061-2