prolylglycine and prolyl-glycyl-glycine

Two previously identified Bacillus subtilis DNA segments, dciA and dciB, whose transcripts accumulate very rapidly after induction of sporulation, were found in the same 6.2 kb transcription unit, now known as the dciA operon. Analysis of the sequence of the dciA operon showed that its putative products are homologous to bacterial peptide transport systems. The product of the fifth gene, DciAE, is similar to peptide-binding proteins from Escherichia coli and Salmonella typhimurium (DppA and OppA) and B. subtilis (OppA). A null mutation in dciAE abolished the ability of a proline auxotroph to grow in a medium containing the dipeptide Pro-Gly as sole proline source, suggesting that the dciA operon encodes a dipeptide transport system.

Topics: Amino Acid Sequence; Bacillus subtilis; Bacterial Proteins; Base Sequence; Biological Transport, Active; Blotting, Southern; Dipeptides; DNA, Bacterial; Escherichia coli; Gene Expression; Kinetics; Membrane Transport Proteins; Molecular Sequence Data; Mutation; Oligopeptides; Operon; Plasmids; Promoter Regions, Genetic; Salmonella typhimurium; Sequence Homology, Nucleic Acid; Spores, Bacterial