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- ***********************************
- * Bacterial rhodopsins signatures *
- ***********************************
-
- Bacterial rhodopsins [1,2,3] are a family of retinal-containing proteins found
- in extremely halophilic bacteria which provide light-dependent ion transport
- and sensory functions for these organisms. Bacterial rhodopsins are integral
- membrane proteins with seven transmembrane regions. The retinal choromophore
- is covalently linked, via a Schiff's base, to the epsilon-amino group of a
- conserved lysine residue in the middle of the last transmembrane helix (called
- helix G). There are at least three types of bacterial rhodopsins:
-
- - Bacteriorhodopsin (bop), and archaerhodopsins 1 and 2, light-driven proton
- pumps.
- - Halorhodopsin (hop), a light-driven chloride pump.
- - Sensory rhodopsin (sop), which mediates both photoattractant (in the red)
- and photophobic (in the near UV) responses.
-
- We developed two patterns which allow the specific detection of bacterial
- rhodopsins. The first pattern corresponds to the third transmembrane region
- (called helix C) and includes an arginine residue which seems involved in the
- release of a proteon from the Schiff's base to the extracellular medium. The
- second pattern includes the retinal binding lysine
-
- -Consensus pattern: R-Y-x-[DT]-W-x-[LIVMF]-[ST]-T-P-[LIVM](3)
- -Sequences known to belong to this class detected by the pattern: ALL.
- -Other sequence(s) detected in SWISS-PROT: NONE.
-
- -Consensus pattern: [FY]-x-[FVG]-[LIVM]-D-[LIVM]-x-A-K-x(2)-[FY]
- [K is the retinal binding site]
- -Sequences known to belong to this class detected by the pattern: ALL.
- -Other sequence(s) detected in SWISS-PROT: NONE.
-
- -Last update: June 1994 / Patterns and text revised.
-
- [ 1] Osterhelt D., Tittor J.
- Trends Biochem. Sci. 14:57-61(1989).
- [ 2] Soppa J., Duschl J., Oesterhelt D.
- J. Bacteriol. 175:2720-2726(1993).
- [ 3] Kuan G., Saier M.H. Jr.
- Res. Microbiol. Submitted(1994).
-