ID   BACR_HALS4              Reviewed;         250 AA.
AC   O93740;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Bacteriorhodopsin;
DE            Short=BR;
GN   Name=bop;
OS   Haloterrigena sp. (strain arg-4).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC   Natrialbaceae; Haloterrigena; unclassified Haloterrigena.
OX   NCBI_TaxID=160432;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9878396; DOI=10.1006/jmbi.1998.2286;
RA   Ihara K., Umemura T., Katagiri I., Kitajima-Ihara T., Sugiyama Y.,
RA   Kimura Y., Mukohata Y.;
RT   "Evolution of the archaeal rhodopsins: evolution rate changes by gene
RT   duplication and functional differentiation.";
RL   J. Mol. Biol. 285:163-174(1999).
CC   -!- FUNCTION: Light-driven proton pump.
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; AB009620; BAA75200.1; -; Genomic_DNA.
DR   AlphaFoldDB; O93740; -.
DR   SMR; O93740; -.
DR   TCDB; 3.E.1.1.7; the ion-translocating microbial rhodopsin (mr) family.
DR   PRIDE; O93740; -.
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   3: Inferred from homology;
KW   Cell membrane; Chromophore; Hydrogen ion transport; Ion transport;
KW   Membrane; Photoreceptor protein; Receptor; Retinal protein;
KW   Sensory transduction; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..250
FT                   /note="Bacteriorhodopsin"
FT                   /id="PRO_0000196272"
FT   TOPO_DOM        1..18
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        19..37
FT                   /note="Helical; Name=Helix A"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        38..51
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        52..70
FT                   /note="Helical; Name=Helix B"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        71..86
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        87..104
FT                   /note="Helical; Name=Helix C"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        105..115
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        116..135
FT                   /note="Helical; Name=Helix D"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        136..142
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        143..162
FT                   /note="Helical; Name=Helix E"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        163..180
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        181..199
FT                   /note="Helical; Name=Helix F"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        200..212
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        213..232
FT                   /note="Helical; Name=Helix G"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        233..250
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   SITE            93
FT                   /note="Primary proton acceptor"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         225
FT                   /note="N6-(retinylidene)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   250 AA;  27041 MW;  B72D3373506FD275 CRC64;
     MCCAALAPPM AATVGPESIW LWIGTIGMTL GTLYFVGRGR GVRDRKMQEF YIITIFITTI
     AAAMYFAMAT GFGVTEVMVG DEALTIYWAR YADWLFTTPL LLLDLSLLAG ANRNTIATLI
     GLDVFMIGTG AIAALSSTPG TRIAWWAIST GALLALLYVL VGTLSENARN RAPEVASLFG
     RLRNLVIALW FLYPVVWILG TEGTFGILPL YWETAAFMVL DLSAKVGFGV ILLQSRSVLE
     RVATPTAAPT