BACR_HALHP
ID BACR_HALHP Reviewed; 211 AA.
AC P33971;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Bacteriorhodopsin;
DE Short=BR;
DE Flags: Fragment;
GN Name=bop;
OS Halobacterium halobium (strain port).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium.
OX NCBI_TaxID=33004;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1479357; DOI=10.1099/00221287-138-11-2389;
RA Otomo J., Urabe Y., Tomioka H., Sasabe H.;
RT "The primary structures of helices A to G of three new bacteriorhodopsin-
RT like retinal proteins.";
RL J. Gen. Microbiol. 138:2389-2396(1992).
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; D11057; BAA01800.1; -; Genomic_DNA.
DR PIR; A47686; A47686.
DR AlphaFoldDB; P33971; -.
DR SMR; P33971; -.
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.
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..>211
FT /note="Bacteriorhodopsin"
FT /id="PRO_0000196270"
FT TRANSMEM 1..19
FT /note="Helical; Name=Helix A"
FT /evidence="ECO:0000250"
FT TOPO_DOM 20..33
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 34..52
FT /note="Helical; Name=Helix B"
FT /evidence="ECO:0000250"
FT TOPO_DOM 53..68
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 69..86
FT /note="Helical; Name=Helix C"
FT /evidence="ECO:0000250"
FT TOPO_DOM 87..97
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 98..117
FT /note="Helical; Name=Helix D"
FT /evidence="ECO:0000250"
FT TOPO_DOM 118..130
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 131..150
FT /note="Helical; Name=Helix E"
FT /evidence="ECO:0000250"
FT TOPO_DOM 151..168
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 169..187
FT /note="Helical; Name=Helix F"
FT /evidence="ECO:0000250"
FT TOPO_DOM 188..199
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 200..>211
FT /note="Helical; Name=Helix G"
FT /evidence="ECO:0000250"
FT SITE 75
FT /note="Primary proton acceptor"
FT /evidence="ECO:0000250"
FT NON_TER 1
FT NON_TER 211
SQ SEQUENCE 211 AA; 23163 MW; 71EFE20C4876AA19 CRC64;
IWLWLGTAGM FLGMLYFIAR GWGETDSRRQ KFYIATILIT AIAFVNYLAM ALGFGLTIVE
FAGEEHPIYW ARYSDWLFTT PLLLYDLGLL AGADRNTITS LVSLDVLMIG TGLVATLSAG
SGVLSAGAER LVWWGISTAF LLVLLYFLFS SLSGRVADLP SDTRSTFKTL RNLVTVVWLV
YPVWWLIGTE GIGLVGIGIE TAGFMVIDLT A