Protein Family Models

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)

Date:

2024-10-16

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)

Date:

2024-08-14

D,D-dipeptide ABC transporter permease similar to Escherichia coli DdpC, part of the ABC transporter complex DdpABCDF, which is probably involved in D-alanine-D-alanine dipeptide transport; responsible for the translocation of the substrate across the membrane

Date:

2018-10-22

Gene:

ddpC

Date:

2023-07-17