Literature summary extracted from

Pearce, S.R.; Mimmack, M.L.; Gallagher, M.P.; Gileadi, U.; Hyde, S.C.; Higgins, C.F.
Membrane topology of the integral membrane components, OppB and OppC, of the oligopeptide permease of Salmonella typhimurium (1992), Mol. Microbiol., 6, 47-57.

Localization

EC Number	Localization	Comment	Organism	GeneOntology No.	Textmining
7.4.2.6	membrane	OppB and OppC are highly hydrophobic, integral membrane proteins. Each of these two proteins spans the membrane six times, with the N-terminus and the C-terminus both being located at the cytoplasmic face of the membrane	Salmonella enterica subsp. enterica serovar Typhimurium	16020	-

Organism

EC Number	Organism	UniProt	Comment	Textmining
7.4.2.6	Salmonella enterica subsp. enterica serovar Typhimurium	-	-	-

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
7.4.2.6	ATP + H2O + oligopeptide/out	-	Salmonella enterica subsp. enterica serovar Typhimurium	ADP + phosphate + oligopeptide/in	-	?

Subunits

EC Number	Subunits	Comment	Organism
7.4.2.6	More	ATP-binding cassette transporter	Salmonella enterica subsp. enterica serovar Typhimurium
7.4.2.6	More	five proteins OppA, OppB, OppC, OppD and OppF are required for Opp function	Salmonella enterica subsp. enterica serovar Typhimurium
7.4.2.6	More	OppB and OppC are responsible for mediating passage of peptides across the cytoplasmic membrane	Salmonella enterica subsp. enterica serovar Typhimurium

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Release 2023.1 (January 2023)