Identification of methionine-processed HPr in the equine pathogen Streptococcus equi.
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.
Sutcliffe
I C
IC
School of Sciences, University of Sunderland, UK. iain.sutcliffe@sunderland.ac.uk
Trigg
J
J
Harrington
D
D
D000818:Animals; D001426:Bacterial Proteins; D015153:Blotting, Western; D006734:Horse Diseases / Q000382:microbiology; D006736:Horses; D008715:Methionine; D008969:Molecular Sequence Data; D010731:Phosphoenolpyruvate Sugar Phosphotransferase System / Q000302:isolation & purification* / Q000378:metabolism; D011499:Protein Processing, Post-Translational; D020539:Sequence Analysis, Protein; D018502:Streptococcus equi / Q000737:chemistry* / Q000472:pathogenicity
D001426:Bacterial Proteins; D008715:Methionine; D010731:Phosphoenolpyruvate Sugar Phosphotransferase System; C030182:phosphocarrier protein HPr