Biology:Bacterial binding protein-dependent transporter

From HandWiki
Short description: Protein family


BPD_transp_1
Identifiers
SymbolBPD_transp_1
PfamPF00528
Pfam clanCL0404
InterProIPR000515
PROSITEPDOC00364
TCDB3.A.1
OPM superfamily17
OPM protein3puz

Bacterial binding 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 peripheral membrane 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 cytoplasmic loop 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.

References

  1. Ames GF (1986). "Bacterial periplasmic transport systems: structure, mechanism, and evolution". Annu. Rev. Biochem. 55: 397–425. doi:10.1146/annurev.bi.55.070186.002145. PMID 3527048. 
  2. "Binding protein-dependent transport systems". J. Bioenerg. Biomembr. 22 (4): 571–92. August 1990. doi:10.1007/BF00762962. PMID 2229036. 
  3. "Sequence of gene malG in E. coli K12: homologies between integral membrane components from binding protein-dependent transport systems". EMBO J. 4 (9): 2287–93. September 1985. doi:10.1002/j.1460-2075.1985.tb03928.x. PMID 3000770. 
  4. "Bacterial binding protein-dependent permeases: characterization of distinctive signatures for functionally related integral cytoplasmic membrane proteins". Mol. Microbiol. 12 (6): 993–1004. June 1994. doi:10.1111/j.1365-2958.1994.tb01087.x. PMID 7934906. 
  5. "Membrane topology of the integral membrane components, OppB and OppC, of the oligopeptide permease of Salmonella typhimurium". Mol. Microbiol. 6 (1): 47–57. January 1992. doi:10.1111/j.1365-2958.1992.tb00836.x. PMID 1738314. 
This article incorporates text from the public domain Pfam and InterPro: IPR000515