Bacterial rhodopsins

From Wikipedia, the free encyclopedia
Jump to: navigation, search
Bacteriorhodopsin-like protein
1m0l opm.png
Bacteriorhodopsin trimer
Symbol Bac_rhodopsin
Pfam PF01036
InterPro IPR001425
SCOP 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.


  1. ^ Oesterhelt, Dieter; Tittor, Jörg (1989). "Two pumps, one principle: light-driven ion transport in halobacteria". Trends in Biochemical Sciences. 14 (2): 57–61. ISSN 0968-0004. doi:10.1016/0968-0004(89)90044-3. 
  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 401571Freely accessible. PMID 2591367. 

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