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Transport of natural peptides and antibacterial phosphonopeptide analogues was studied in Streptococcus faecalis ATCC 9790. Competition studies, and the isolation of peptide-transport deficient mutants, indicate the presence of two peptide permeases. One is a high-rate system used by dipeptides, and to a lesser extent tripeptides; the other is a low-rate oligopeptide system. Following uptake, peptides are cleaved and their amino acid residues may undergo rapid exodus. Different strains of S. faecalis differ in their rates of peptide transport.
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