Bacterial rhodopsins

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Bacteriorhodopsin-like protein
1m0l opm.png
Bacteriorhodopsin trimer
Identifiers
Symbol Bac_rhodopsin
Pfam PF01036
InterPro IPR001425
PROSITE PDOC00291
SCOP 2brd
SUPERFAMILY 2brd
TCDB 3.E.1
OPM superfamily 6
OPM protein 1vgo

Bacterial rhodopsins are a family of bacterial opsins. They are retinal-binding proteins that provide light-dependent ion transport and sensory functions to a family of halophilic[1][2] and other bacteria. They are integral membrane proteins with seven transmembrane helices, the last of which contains the attachment point for retinal (a conserved lysine).

The proteins from halobacteria include bacteriorhodopsin and archaerhodopsin, which are light-driven proton pumps; halorhodopsin, a light-driven chloride pump; and sensory rhodopsin, which mediates both photoattractant (in the red) and photophobic (in the ultra-violet) responses. Proteins from other bacteria include proteorhodopsin.

References[edit]

  1. ^ Oesterhelt D, Tittor J (1989). "Two pumps, one principle: light-driven ion transport in halobacteria". Trends Biochem. Sci. 14 (2): 57–61. doi:10.1016/0968-0004(89)90044-3. PMID 2468194. 
  2. ^ Lottspeich F, Oesterhelt D, Blanck A, Ferrando E, Schegk ES (1989). "Primary structure of sensory rhodopsin I, a prokaryotic photoreceptor". EMBO J. 8 (13): 3963–3971. PMC 401571. PMID 2591367. 

This article incorporates text from the public domain Pfam and InterPro IPR001425