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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)
glutathione ABC transporter permease
glutathione ABC transporter permease GsiD is the transmembrane subunit of the ABC transporter complex GsiABCD involved in glutathione import; responsible for the translocation of the substrate across the membrane
glutathione ABC transporter permease GsiD
With GsiABC is involved in the transport of glutathione into the cell
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