BACR2_HALS2
ID BACR2_HALS2 Reviewed; 259 AA.
AC P29563;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Archaerhodopsin-2;
DE Short=AR 2;
DE Flags: Precursor;
OS Halobacterium sp. (strain aus-2).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium.
OX NCBI_TaxID=29285;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=1654776; DOI=10.1016/0003-9861(91)90014-a;
RA Uegaki K., Sugiyama Y., Mukohata Y.;
RT "Archaerhodopsin-2, from Halobacterium sp. aus-2 further reveals essential
RT amino acid residues for light-driven proton pumps.";
RL Arch. Biochem. Biophys. 286:107-110(1991).
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; S56354; AAB19870.2; -; Genomic_DNA.
DR PIR; S14731; S14731.
DR PDB; 1VGO; X-ray; 2.50 A; A/B=7-259.
DR PDB; 2EI4; X-ray; 2.10 A; A=7-259.
DR PDB; 2Z55; X-ray; 2.50 A; A/B/D/E=7-259.
DR PDB; 3WQJ; X-ray; 1.80 A; A=1-259.
DR PDBsum; 1VGO; -.
DR PDBsum; 2EI4; -.
DR PDBsum; 2Z55; -.
DR PDBsum; 3WQJ; -.
DR AlphaFoldDB; P29563; -.
DR SMR; P29563; -.
DR TCDB; 3.E.1.1.2; the ion-translocating microbial rhodopsin (mr) family.
DR EvolutionaryTrace; P29563; -.
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 3D-structure; Cell membrane; Chromophore; Direct protein sequencing;
KW Hydrogen ion transport; Ion transport; Membrane; Photoreceptor protein;
KW Pyrrolidone carboxylic acid; Receptor; Retinal protein;
KW Sensory transduction; Transmembrane; Transmembrane helix; Transport.
FT PROPEP 1..6
FT /id="PRO_0000020252"
FT CHAIN 7..259
FT /note="Archaerhodopsin-2"
FT /id="PRO_0000020253"
FT TOPO_DOM 7..18
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 19..40
FT /note="Helical; Name=Helix A"
FT /evidence="ECO:0000250"
FT TOPO_DOM 41..49
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 50..71
FT /note="Helical; Name=Helix B"
FT /evidence="ECO:0000250"
FT TOPO_DOM 72..90
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 91..112
FT /note="Helical; Name=Helix C"
FT /evidence="ECO:0000250"
FT TOPO_DOM 113..115
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 116..138
FT /note="Helical; Name=Helix D"
FT /evidence="ECO:0000250"
FT TOPO_DOM 139..142
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 143..171
FT /note="Helical; Name=Helix E"
FT /evidence="ECO:0000250"
FT TOPO_DOM 172..174
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 175..203
FT /note="Helical; Name=Helix F"
FT /evidence="ECO:0000250"
FT TOPO_DOM 204..211
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 212..244
FT /note="Helical; Name=Helix G"
FT /evidence="ECO:0000250"
FT TOPO_DOM 245..259
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT MOD_RES 7
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250"
FT MOD_RES 227
FT /note="N6-(retinylidene)lysine"
FT /evidence="ECO:0000250"
FT STRAND 14..16
FT /evidence="ECO:0007829|PDB:3WQJ"
FT HELIX 20..41
FT /evidence="ECO:0007829|PDB:3WQJ"
FT HELIX 47..72
FT /evidence="ECO:0007829|PDB:3WQJ"
FT STRAND 77..80
FT /evidence="ECO:0007829|PDB:3WQJ"
FT STRAND 86..89
FT /evidence="ECO:0007829|PDB:3WQJ"
FT HELIX 92..112
FT /evidence="ECO:0007829|PDB:3WQJ"
FT HELIX 116..138
FT /evidence="ECO:0007829|PDB:3WQJ"
FT HELIX 142..164
FT /evidence="ECO:0007829|PDB:3WQJ"
FT HELIX 166..171
FT /evidence="ECO:0007829|PDB:3WQJ"
FT HELIX 176..202
FT /evidence="ECO:0007829|PDB:3WQJ"
FT TURN 204..207
FT /evidence="ECO:0007829|PDB:3WQJ"
FT HELIX 212..235
FT /evidence="ECO:0007829|PDB:3WQJ"
FT HELIX 238..240
FT /evidence="ECO:0007829|PDB:2EI4"
SQ SEQUENCE 259 AA; 27938 MW; 918F368373DFED84 CRC64;
MDPIALQAGF DLLNDGRPET LWLGIGTLLM LIGTFYFIAR GWGVTDKEAR EYYAITILVP
GIASAAYLAM FFGIGVTEVE LASGTVLDIY YARYADWLFT TPLLLLDLAL LAKVDRVTIG
TLIGVDALMI VTGLIGALSK TPLARYTWWL FSTIAFLFVL YYLLTSLRSA AAKRSEEVRS
TFNTLTALVA VLWTAYPILW IVGTEGAGVV GLGIETLAFM VLDVTAKVGF GFVLLRSRAI
LGETEAPEPS AGADASAAD
