Abstract
Transport of natural peptides and antibacterial phosphonopeptide analogs was studied in S. faecalis ATCC 9790. Competition studies and the isolation of peptide-transport deficient mutants indicate the presence of 2 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.