Identification of methionine-processed HPr in the equine pathogen Streptococcus equi.
Syst Appl Microbiol
; 23(3): 330-2, 2000 Oct.
Article
em En
| MEDLINE
| ID: mdl-11108010
ABSTRACT
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 phosphoenolpyruvatesugar 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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Base de dados:
MEDLINE
Assunto principal:
Proteínas de Bactérias
/
Sistema Fosfotransferase de Açúcar do Fosfoenolpiruvato
/
Streptococcus equi
Idioma:
En
Ano de publicação:
2000
Tipo de documento:
Article