Bacterialbinding protein-dependent
transport systems,[1][2] are multicomponent systems typically composed of a periplasmic substrate-binding protein, one or two reciprocally
homologous integral inner-membrane
proteins and one or two
peripheralmembrane ATP-binding
proteins that couple
energy to the
active transport system. The integral inner-membrane
proteins translocate the
substrate across the
membrane. It has been shown,[3][4] that most of these proteins contain a
conserved region located about 80 to 100
residues from their C-terminal extremity. This region seems [5] to be located in a
cytoplasmicloop between two
transmembrane domains. Apart from the
conserved region, the
sequence of these proteins is quite divergent, and they have a variable number of
transmembrane helices, however they can be classified into seven families which have been respectively termed: araH, cysTW, fecCD, hisMQ, livHM, malFG and oppBC.
^Saurin W, Kaster W, Dassa E (June 1994). "Bacterial binding protein-dependent permeases: characterization of distinctive signatures for functionally related integral cytoplasmic membrane proteins". Mol. Microbiol. 12 (6): 993–1004.
doi:
10.1111/j.1365-2958.1994.tb01087.x.
PMID7934906.
S2CID889103.
^Pearce SR, Mimmack ML, Gallagher MP, Gileadi U, Hyde SC, Higgins CF (January 1992). "Membrane topology of the integral membrane components, OppB and OppC, of the oligopeptide permease of Salmonella typhimurium". Mol. Microbiol. 6 (1): 47–57.
doi:
10.1111/j.1365-2958.1992.tb00836.x.
PMID1738314.
S2CID1660114.
Bacterialbinding protein-dependent
transport systems,[1][2] are multicomponent systems typically composed of a periplasmic substrate-binding protein, one or two reciprocally
homologous integral inner-membrane
proteins and one or two
peripheralmembrane ATP-binding
proteins that couple
energy to the
active transport system. The integral inner-membrane
proteins translocate the
substrate across the
membrane. It has been shown,[3][4] that most of these proteins contain a
conserved region located about 80 to 100
residues from their C-terminal extremity. This region seems [5] to be located in a
cytoplasmicloop between two
transmembrane domains. Apart from the
conserved region, the
sequence of these proteins is quite divergent, and they have a variable number of
transmembrane helices, however they can be classified into seven families which have been respectively termed: araH, cysTW, fecCD, hisMQ, livHM, malFG and oppBC.
^Saurin W, Kaster W, Dassa E (June 1994). "Bacterial binding protein-dependent permeases: characterization of distinctive signatures for functionally related integral cytoplasmic membrane proteins". Mol. Microbiol. 12 (6): 993–1004.
doi:
10.1111/j.1365-2958.1994.tb01087.x.
PMID7934906.
S2CID889103.
^Pearce SR, Mimmack ML, Gallagher MP, Gileadi U, Hyde SC, Higgins CF (January 1992). "Membrane topology of the integral membrane components, OppB and OppC, of the oligopeptide permease of Salmonella typhimurium". Mol. Microbiol. 6 (1): 47–57.
doi:
10.1111/j.1365-2958.1992.tb00836.x.
PMID1738314.
S2CID1660114.