PRRG_UNKP
ID PRRG_UNKP Reviewed; 250 AA.
AC Q6J4G7;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 50.
DE RecName: Full=Green-light absorbing proteorhodopsin {ECO:0000303|PubMed:34226545};
DE Short=GPR {ECO:0000303|PubMed:34226545};
DE Flags: Precursor;
OS Unknown prokaryotic organism.
OC Bacteria; environmental samples.
OX NCBI_TaxID=2725;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=15466697; DOI=10.1073/pnas.0403999101;
RA Bielawski J.P., Dunn K.A., Sabehi G., Beja O.;
RT "Darwinian adaptation of proteorhodopsin to different light intensities in
RT the marine environment.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14824-14829(2004).
RN [2]
RP SUBUNIT.
RX PubMed=32647827; DOI=10.1016/j.yjsbx.2020.100024;
RA Hirschi S., Kalbermatter D., Ucurum Z., Fotiadis D.;
RT "Cryo-electron microscopic and X-ray crystallographic analysis of the
RT light-driven proton pump proteorhodopsin reveals a pentameric assembly.";
RL J. Struct. Biol. 4:100024-100024(2020).
RN [3] {ECO:0007744|PDB:7B03}
RP STRUCTURE BY ELECTRON MICROSCOPY (2.93 ANGSTROMS) OF 19-250 IN COVALENT
RP COMPLEX WITH RETINAL, FUNCTION, SUBUNIT, PTM, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF LYS-58; TRP-59; TYR-96; GLU-143; SER-180; TYR-209; TYR-224
RP AND GLU-246.
RX PubMed=34226545; DOI=10.1038/s41467-021-24429-6;
RA Hirschi S., Kalbermatter D., Ucurum Z., Lemmin T., Fotiadis D.;
RT "Cryo-EM structure and dynamics of the green-light absorbing
RT proteorhodopsin.";
RL Nat. Commun. 12:4107-4107(2021).
CC -!- FUNCTION: Light-driven proton pump. {ECO:0000269|PubMed:34226545}.
CC -!- SUBUNIT: Homopentamer (PubMed:34226545, PubMed:32647827). GPR protomers
CC assemble into a pentamer around a central pore with a C5 symmetry axis
CC (PubMed:34226545). {ECO:0000269|PubMed:32647827,
CC ECO:0000269|PubMed:34226545}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255,
CC ECO:0000305|PubMed:34226545}; Multi-pass membrane protein {ECO:0000255,
CC ECO:0000305|PubMed:34226545}.
CC -!- PTM: Contains one covalently linked retinal chromophore per subunit.
CC {ECO:0000269|PubMed:34226545}.
CC -!- SIMILARITY: Belongs to the archaeal/bacterial/fungal opsin family.
CC {ECO:0000305}.
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DR EMBL; AY601905; AAT12291.1; -; Genomic_DNA.
DR PDB; 7B03; EM; 2.93 A; A/B/C/D/E=19-250.
DR PDBsum; 7B03; -.
DR SMR; Q6J4G7; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0010461; F:light-activated ion channel activity; IEA:InterPro.
DR GO; GO:0009881; F:photoreceptor activity; IEA:UniProtKB-KW.
DR GO; GO:0007602; P:phototransduction; IEA:UniProtKB-KW.
DR InterPro; IPR001425; Arc/bac/fun_rhodopsins.
DR InterPro; IPR017402; Proteorhodopsin.
DR InterPro; IPR018229; Rhodopsin_retinal_BS.
DR PANTHER; PTHR28286; PTHR28286; 1.
DR Pfam; PF01036; Bac_rhodopsin; 1.
DR PIRSF; PIRSF038142; Rhodopsin_bac_prd; 1.
DR SMART; SM01021; Bac_rhodopsin; 1.
DR PROSITE; PS00950; BACTERIAL_OPSIN_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Chromophore; Membrane; Photoreceptor protein;
KW Receptor; Retinal protein; Sensory transduction; Signal; Transmembrane;
KW Transmembrane helix; Transport.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..250
FT /note="Green-light absorbing proteorhodopsin"
FT /id="PRO_5004274813"
FT TOPO_DOM 19..29
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:34226545"
FT TRANSMEM 30..53
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:34226545"
FT TOPO_DOM 54..58
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:34226545"
FT TRANSMEM 59..87
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:34226545"
FT TOPO_DOM 88..90
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:34226545"
FT TRANSMEM 91..118
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:34226545"
FT TOPO_DOM 119..121
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:34226545"
FT TRANSMEM 122..144
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:34226545"
FT TOPO_DOM 145..147
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:34226545"
FT TRANSMEM 148..177
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:34226545"
FT TOPO_DOM 178..180
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:34226545"
FT TRANSMEM 181..208
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:34226545"
FT TOPO_DOM 209..218
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:34226545"
FT TRANSMEM 219..249
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:34226545"
FT TOPO_DOM 250
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:34226545"
FT SITE 98
FT /note="Primary proton acceptor"
FT /evidence="ECO:0000255|PIRSR:PIRSR038142-1,
FT ECO:0000305|PubMed:34226545"
FT SITE 106
FT /note="Responsible for spectral tuning"
FT /evidence="ECO:0000255|PIRSR:PIRSR038142-1"
FT SITE 109
FT /note="Primary proton donor"
FT /evidence="ECO:0000255|PIRSR:PIRSR038142-1,
FT ECO:0000305|PubMed:34226545"
FT SITE 143
FT /note="Proton release group"
FT /evidence="ECO:0000305|PubMed:34226545"
FT MOD_RES 232
FT /note="N6-(retinylidene)lysine"
FT /evidence="ECO:0000269|PubMed:34226545,
FT ECO:0007744|PDB:7B03"
FT MUTAGEN 58
FT /note="K->A: Reduced GPR photoactivity by about 30%."
FT /evidence="ECO:0000269|PubMed:34226545"
FT MUTAGEN 59
FT /note="W->A: Reduced GPR photoactivity by about 50%."
FT /evidence="ECO:0000269|PubMed:34226545"
FT MUTAGEN 96
FT /note="Y->F: Reduced GPR photoactivity by about 50%."
FT /evidence="ECO:0000269|PubMed:34226545"
FT MUTAGEN 143
FT /note="E->A: Reduced GPR photoactivity by about 50%."
FT /evidence="ECO:0000269|PubMed:34226545"
FT MUTAGEN 180
FT /note="S->A: Increased GPR photoactivity."
FT /evidence="ECO:0000269|PubMed:34226545"
FT MUTAGEN 209
FT /note="Y->F: Reduced GPR photoactivity by about 50%."
FT /evidence="ECO:0000269|PubMed:34226545"
FT MUTAGEN 224
FT /note="Y->F: Reduced GPR photoactivity by about 50%."
FT /evidence="ECO:0000269|PubMed:34226545"
FT MUTAGEN 246
FT /note="E->A: Increased GPR photoactivity."
FT /evidence="ECO:0000269|PubMed:34226545"
FT STRAND 27..30
FT /evidence="ECO:0007829|PDB:7B03"
FT HELIX 31..50
FT /evidence="ECO:0007829|PDB:7B03"
FT HELIX 51..54
FT /evidence="ECO:0007829|PDB:7B03"
FT HELIX 57..86
FT /evidence="ECO:0007829|PDB:7B03"
FT HELIX 92..115
FT /evidence="ECO:0007829|PDB:7B03"
FT HELIX 123..143
FT /evidence="ECO:0007829|PDB:7B03"
FT HELIX 149..168
FT /evidence="ECO:0007829|PDB:7B03"
FT HELIX 171..176
FT /evidence="ECO:0007829|PDB:7B03"
FT HELIX 181..196
FT /evidence="ECO:0007829|PDB:7B03"
FT TURN 197..199
FT /evidence="ECO:0007829|PDB:7B03"
FT HELIX 200..208
FT /evidence="ECO:0007829|PDB:7B03"
FT HELIX 220..232
FT /evidence="ECO:0007829|PDB:7B03"
FT HELIX 234..248
FT /evidence="ECO:0007829|PDB:7B03"
SQ SEQUENCE 250 AA; 27308 MW; 5FDB6DFB3209C7EA CRC64;
MGKLLLILGS VIALPTFAAG GGDLDASDYT GVSFWLVTAA LLASTVFFFV ERDRVSAKWK
TSLTVSGLVT GIAFWHYMYM RGVWIETGDS PTVFRYIDWL LTVPLLICEF YLILAAATNV
AGSLFKKLLV GSLVMLVFGY MGEAGIMAAW PAFIIGCLAW VYMIYELWAG EGKSACNTAS
PAVQSAYNTM MYIIIFGWAI YPVGYFTGYL MGDGGSALNL NLIYNLADFV NKILFGLIIW
NVAVKESSNA
