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N-terminal TM domain of oligopeptide transport permease C
Oligopeptide permeases (Opp) have been identified in numerous gram-negative and -positive bacteria. These transport systems belong to the superfamily of highly conserved ATP-binding cassette transporters. Typically, Opp importers comprise a complex of five proteins. The oligopeptide-binding protein OppA is responsible for the capture of peptides from the external medium. Two integral highly hydrophobic membrane spanning proteins, OppB and OppC, form a channel through the membrane used for peptide translocation. This N-terminal domain appears to be the first TM domain of the molecule [1]. [1]. 1738314. Membrane topology of the integral membrane components, OppB and OppC, of the oligopeptide permease of Salmonella typhimurium. Pearce SR, Mimmack ML, Gallagher MP, Gileadi U, Hyde SC, Higgins CF;. Mol Microbiol. 1992;6:47-57. (from Pfam)
ABC transporter permease subunit
The alignments cover the most conserved region of the proteins, which is thought to be located in a cytoplasmic loop between two transmembrane domains. The members of this family have a variable number of transmembrane helices. (from Pfam)
oligopeptide ABC transporter permease OppC
oligopeptide ABC transporter permease OppC is the transmembrane subunit (TM) of the periplasmic binding protein (PBP)-dependent ABC transporter complex OppABCDF involved in the import of peptides and is responsible for mediating passage of peptides across the cytoplasmic membrane
With OppBCDF is involved in the transport of oligopeptides of up to 5 amino acids into the cell
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