3.E.1.1.18 Glycylhalorhodopsin
is an anion pumping microbial rhodopsin. It is 260 aas long with 7
TMSs. It takes up anions including chloride and sulfate. The function of many
microbial rhodopsins is determined by three
residues in the third transmembrane helix called motif residues. Ishizuka et al. 2024 reported a group of microbial rhodopsins with a novel Thr–Thr–Gly (TTG)
motif. They function as
light-driven inward anion pumps similar to halorhodopsins. Based on the characteristic glycine
residue in their motif and light-driven anion-pumping function, these rhodopsins are called glycylhalorhodopsins (GHRs). X-ray
crystallographic analysis found large cavities on the cytoplasmic side of these proteins,
which are produced by the small side-chain volume of the glycine residue
in the motif. The opened structure of GHR on the cytoplasmic side is
related to the anion releasing process to the cytoplasm during the
photoreaction compared to canonical halorhodopsin from Natronomonas pharaonis (NpHR) (Ishizuka et al. 2024).
|
Accession Number: | WP_176473163.1 |
Protein Name: | WP_176473163.1 bacteriorhodopsin [Sphingomonas lenta] |
Length: | 260 |
Molecular Weight: | |
Species: | Sphingomonas lenta [1141887] |
Number of TMSs: | 7 |
Substrate |
chloride, sulfate |
---|
1: MNPKPLDTST EYWLWIGVAG MALSAAVMLF QARRSRTPFE EGQSVNQFFV LLIAFGTYLA
61: MALGQGSLTA DDGRQVFVSR YVTWAFTTPL LLLGLATTAL GVPVTRRKPI VFGMLGADVI
121: MILTGLVAAL SPSGSAEKWT WYLVSSGAFL AVLYLLWSTL RTEAHVSGPD QARLYGRNLR
181: FLTVIWLLYP VNFLLGNEGL RAYGGTETTA GYTLLDLISK AVYGFFAIAG VRRLVDAHGA
241: PDDSLDAVAR RAASDGMTS