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| Archaeal/bacterial/fungal rhodopsins | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Bacteriorhodopsin trimer | |||||||||
| Identifiers | |||||||||
| Symbol | Bac_rhodopsin | ||||||||
| Pfam | PF01036 | ||||||||
| InterPro | IPR001425 | ||||||||
| SMART | SM01021 | ||||||||
| PROSITE | PDOC00291 | ||||||||
| SCOP2 | 2brd / SCOPe / SUPFAM | ||||||||
| TCDB | 3.E.1 | ||||||||
| OPM superfamily | 6 | ||||||||
| OPM protein | 1vgo | ||||||||
| |||||||||
Microbial rhodopsins, also known as bacterial rhodopsins, are retinal-binding proteins that provide light-dependent ion transport and sensory functions in halophilic[2][3] and other bacteria. They are integral membrane proteins with seven transmembrane helices, the last of which contains the attachment point (a conserved lysine) for retinal. Most microbial rhodopsins pump inwards, however "mirror rhodopsins" which function outwards. have been discovered.[4]
This protein family includes light-driven proton pumps, ion pumps and ion channels, as well as light sensors. For example, 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.
As their name indicates, microbial rhodopsins are found in Archaea and Bacteria, and also in Eukaryota (such as algae) and viruses; although they are rare in complex multicellular organisms.[5][6]
- ^ Oren A (January 2002). "Molecular ecology of extremely halophilic Archaea and Bacteria". FEMS Microbiology Ecology. 39 (1): 1–7. Bibcode:2002FEMME..39....1O. doi:10.1111/j.1574-6941.2002.tb00900.x. PMID 19709178.
- ^ Oesterhelt D, Tittor J (February 1989). "Two pumps, one principle: light-driven ion transport in halobacteria". Trends in Biochemical Sciences. 14 (2): 57–61. doi:10.1016/0968-0004(89)90044-3. PMID 2468194.
- ^ Blanck A, Oesterhelt D, Ferrando E, Schegk ES, Lottspeich F (December 1989). "Primary structure of sensory rhodopsin I, a prokaryotic photoreceptor". The EMBO Journal. 8 (13): 3963–71. doi:10.1002/j.1460-2075.1989.tb08579.x. PMC 401571. PMID 2591367.
- ^ Okhrimenko, Ivan S.; Kovalev, Kirill; Petrovskaya, Lada E.; Ilyinsky, Nikolay S.; Alekseev, Alexey A.; Marin, Egor; Rokitskaya, Tatyana I.; Antonenko, Yuri N.; Siletsky, Sergey A.; Popov, Petr A.; Zagryadskaya, Yuliya A.; Soloviov, Dmytro V.; Chizhov, Igor V.; Zabelskii, Dmitrii V.; Ryzhykau, Yury L. (2023-05-02). "Mirror proteorhodopsins". Communications Chemistry. 6 (1): 88. doi:10.1038/s42004-023-00884-8. ISSN 2399-3669. PMC 10154332. PMID 37130895.
- ^ Boeuf D, Audic S, Brillet-Guéguen L, Caron C, Jeanthon C (2015). "MicRhoDE: a curated database for the analysis of microbial rhodopsin diversity and evolution". Database. 2015: bav080. doi:10.1093/database/bav080. PMC 4539915. PMID 26286928.
- ^ Yawo H, Kandori H, Koizumi A (5 June 2015). Optogenetics: Light-Sensing Proteins and Their Applications. Springe r. pp. 3–4. ISBN 978-4-431-55516-2. Retrieved 30 September 2015.
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