Literature summary for 7.4.2.6 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.

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Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
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

Organism	UniProt	Comment	Textmining
Salmonella enterica subsp. enterica serovar Typhimurium	-	-	-

Substrates and Products (Substrate)

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

Subunits

Subunits	Comment	Organism
More	ATP-binding cassette transporter	Salmonella enterica subsp. enterica serovar Typhimurium
More	five proteins OppA, OppB, OppC, OppD and OppF are required for Opp function	Salmonella enterica subsp. enterica serovar Typhimurium
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)