ID   BACR1_HALSS             Reviewed;         260 AA.
AC   P69052; P19585;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 55.
DE   RecName: Full=Archaerhodopsin-1;
DE            Short=AR 1;
DE   AltName: Full=Bacterio-opsin;
DE   Flags: Precursor;
GN   Name=bop;
OS   Halobacterium sp. (strain SG1).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halobacteriaceae; Halobacterium.
OX   NCBI_TaxID=33006;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8478333; DOI=10.1128/jb.175.9.2720-2726.1993;
RA   Soppa J., Duschl J., Oesterhelt D.;
RT   "Bacterioopsin, haloopsin, and sensory opsin I of the halobacterial isolate
RT   Halobacterium sp. strain SG1: three new members of a growing family.";
RL   J. Bacteriol. 175:2720-2726(1993).
CC   -!- FUNCTION: Light-driven proton pump. It may interact with
CC       bacterioruberin in the claret membrane.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the archaeal/bacterial/fungal opsin family.
CC       {ECO:0000305}.
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DR   EMBL; X70291; CAA49772.1; -; Genomic_DNA.
DR   PIR; A34178; A34178.
DR   AlphaFoldDB; P69052; -.
DR   SMR; P69052; -.
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:0005216; F: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; IPR018229; Rhodopsin_retinal_BS.
DR   PANTHER; PTHR28286; PTHR28286; 1.
DR   Pfam; PF01036; Bac_rhodopsin; 1.
DR   PRINTS; PR00251; BACTRLOPSIN.
DR   SMART; SM01021; Bac_rhodopsin; 1.
DR   PROSITE; PS00950; BACTERIAL_OPSIN_1; 1.
DR   PROSITE; PS00327; BACTERIAL_OPSIN_RET; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Chromophore; Hydrogen ion transport; Ion transport;
KW   Membrane; Photoreceptor protein; Receptor; Retinal protein;
KW   Sensory transduction; Transmembrane; Transmembrane helix; Transport.
FT   PROPEP          1..6
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000020250"
FT   CHAIN           7..260
FT                   /note="Archaerhodopsin-1"
FT                   /id="PRO_0000020251"
FT   TOPO_DOM        7..20
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        21..42
FT                   /note="Helical; Name=Helix A"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        43..51
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        52..73
FT                   /note="Helical; Name=Helix B"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        74..91
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        92..113
FT                   /note="Helical; Name=Helix C"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        114..116
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        117..139
FT                   /note="Helical; Name=Helix D"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        140..143
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        144..172
FT                   /note="Helical; Name=Helix E"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        173..176
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        177..204
FT                   /note="Helical; Name=Helix F"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        205..212
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        213..245
FT                   /note="Helical; Name=Helix G"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        246..260
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         228
FT                   /note="N6-(retinylidene)lysine"
SQ   SEQUENCE   260 AA;  27852 MW;  64E1277EA641EB91 CRC64;
     MDPIALTAAV GADLLGDGRP ETLWLGIGTL LMLIGTFYFI VKGWGVTDKE AREYYSITIL
     VPGIASAAYL SMFFGIGLTE VQVGSEMLDI YYARYADWLF TTPLLLLDLA LLAKVDRVSI
     GTLVGVDALM IVTGLVGALS HTPLARYTWW LFSTICMIVV LYFLATSLRA AAKERGPEVA
     STFNTLTALV LVLWTAYPIL WIIGTEGAGV VGLGIETLLF MVLDVTAKVG FGFILLRSRA
     ILGDTEAPEP SAGAEASAAD