| Primary Identifier | IPR023517 | Type | Family |
| Short Name | AA/pep_transptr_DtpA |
| description | The transport of peptides into cells is a well-documented biological phenomenon which is accomplished by specific, energy-dependent transporters found in a number of organisms as diverse as bacteria and humans. The amino acid/peptide transporter family of proteins is distinct from the ABC-type peptide transporters and was uncovered by sequence analysis of a number of recently discovered peptide transport proteins []. This family consists of bacterial proton-dependent oligopeptide transporters, although they are found in yeast, plants and animals. They function by proton symport in a 1:1 stoichiometry, which is variable in different species. Structurally, these transporters present a conserved architecture consisting of 14 transmembrane α-helices with N-terminal and C-terminal six-helix bundles connected by two transmembrane α-helices (HA and HB) [].Dipeptide and tripeptide permease A (DtpA) is a proton-dependent permease that transports di- and tripeptides, and structurally related peptidomimetics such as aminocephalosporins into the cell [, , ]. The protein shows a distinct preference for dipeptides and tripeptides composed of L-amino acids, and discriminates dipeptides on the basis of the position of charges within the substrate. |
