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. 1991 Jan;173(1):234–244. doi: 10.1128/jb.173.1.234-244.1991

Identification and characterization of dppA, an Escherichia coli gene encoding a periplasmic dipeptide transport protein.

E R Olson 1, D S Dunyak 1, L M Jurss 1, R A Poorman 1
PMCID: PMC207180  PMID: 1702779

Abstract

We describe the isolation and analysis of an Escherichia coli gene, dppA, and its role in dipeptide transport. dppA maps near min 79 and encodes a protein (DppA) that has regions of amino acid similarity with a peptide-binding protein from Salmonella typhimurium (OppA). Like OppA, DppA is found in the periplasmic space and thus is most likely a dipeptide-binding protein. Insertional inactivation of dppA results in the inability of a proline auxotroph to utilize Pro-Gly as a proline source. dppA-dependent Pro-Gly utilization does not require any of the three major proline transport systems, demonstrating that DppA is not simply a dipeptidase. An in vivo competition assay was used to show that DppA is probably involved in the transport of dipeptides other than Pro-Gly. Transcription of dppA is repressed by the presence of casamino acids, suggesting that the cell alters its dipeptide transport capabilities in response to an environmental signal.

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