3.E.1.1.19 Glycylhalorhodopsins (GHR) of Salinarimonas soli of 263 aas and 7 TMSs (Ishizuka et al. 2024). See 3.E.1.1.18 for details. This system transports anions including chloride and sulfate in the inward direction. X-ray crystallographic analysis found large cavities on the cytoplasmic
side, which are produced by the small side-chain volume of the glycine
residue in the TTG motif in TMS3. The opened structure of GHR on the cytoplasmic
side is probably related to the anion releasing process to the cytoplasm during
the photoreaction compared to canonical halorhodopsin from Natronomonas
pharaonis (NpHR). GHR also transports SO42- and the extracellular glutamate residue plays an essential role in extracellular SO42- uptake. Thus, Ishizuka et al. 2024 have identified a TTG motif-contained in microbial rhodopsins that may relate to an anion-releasing mechanism.
|
Accession Number: | WP_149817501 |
Protein Name: | WP_149817501.1 bacteriorhodopsin [Salinarimonas soli] |
Length: | 264 |
Molecular Weight: | |
Species: | Salinarimonas soli [1638099] |
Number of TMSs: | 7 |
Substrate |
chloride, sulfate |
---|
1: MNPRPIEPAT EAWLWVGVAG MALAAIVMLA FVKRARTPFE ESQAVSQFFV LLIAFGTYLA
61: MALGQGSLTA DDGRQVFVSR YITWTFTTPL LLLGLATTAL GSPITRRKPV VAGLIGADII
121: MILTGLVAAL SPSGSHEKWI WYGVSSGAFL AVYYLICGPL LLEARVTGAD HRRLYLRNAV
181: VLSVIWFLYP VNFLLGNEGL GQWGGTATTA IYTLLDLASK AAYGFFAITG VRALTDRAGA
241: PALTLDEAAR RAGGTEADPA RSG