Document Detail

Identification of methionine-processed HPr in the equine pathogen Streptococcus equi.
MedLine Citation:
PMID:  11108010     Owner:  NLM     Status:  MEDLINE    
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.
I C Sutcliffe; J Trigg; D Harrington
Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Systematic and applied microbiology     Volume:  23     ISSN:  0723-2020     ISO Abbreviation:  Syst. Appl. Microbiol.     Publication Date:  2000 Oct 
Date Detail:
Created Date:  2001-02-28     Completed Date:  2001-03-22     Revised Date:  2004-11-17    
Medline Journal Info:
Nlm Unique ID:  8306133     Medline TA:  Syst Appl Microbiol     Country:  GERMANY    
Other Details:
Languages:  eng     Pagination:  330-2     Citation Subset:  IM    
School of Sciences, University of Sunderland, UK.
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MeSH Terms
Bacterial Proteins*
Blotting, Western
Horse Diseases / microbiology
Molecular Sequence Data
Phosphoenolpyruvate Sugar Phosphotransferase System / isolation & purification*,  metabolism
Protein Processing, Post-Translational
Sequence Analysis, Protein
Streptococcus equi / chemistry*,  pathogenicity
Reg. No./Substance:
0/Bacterial Proteins; 63-68-3/Methionine; EC 2.7.1.-/Phosphoenolpyruvate Sugar Phosphotransferase System; EC 2.7.1.-/phosphocarrier protein HPr

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