BACH_HALS3
ID BACH_HALS3 Reviewed; 274 AA.
AC B0R2U4; P16102; Q9HSK9;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Halorhodopsin;
DE Short=HR;
DE Flags: Precursor;
GN Name=hop; OrderedLocusNames=OE_1299R;
OS Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium.
OX NCBI_TaxID=478009;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=R1 / S9 / L33;
RX PubMed=15981336; DOI=10.1002/j.1460-2075.1987.tb04749.x;
RA Blanck A., Oesterhelt D.;
RT "The halo-opsin gene. II. Sequence, primary structure of halorhodopsin and
RT comparison with bacteriorhodopsin.";
RL EMBO J. 6:265-273(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29341 / DSM 671 / R1;
RX PubMed=18313895; DOI=10.1016/j.ygeno.2008.01.001;
RA Pfeiffer F., Schuster S.C., Broicher A., Falb M., Palm P., Rodewald K.,
RA Ruepp A., Soppa J., Tittor J., Oesterhelt D.;
RT "Evolution in the laboratory: the genome of Halobacterium salinarum strain
RT R1 compared to that of strain NRC-1.";
RL Genomics 91:335-346(2008).
RN [3]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR LOCATION.
RC STRAIN=R1 / S9 / L33;
RX PubMed=24409552; DOI=10.1021/bi00320a050;
RA Barnberg E., Hegemann P., Oesterhelt D.;
RT "The chromoprotein of halorhodopsin is the light-driven electrogenic
RT chloride pump in halobacterium halobium.";
RL Biochemistry 23:6216-6221(1984).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 22-274 IN COMPLEX WITH CHLORIDE,
RP SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY, AND RETINAL-BINDING SITE.
RC STRAIN=R1 / S9 / D2;
RX PubMed=10827943; DOI=10.1126/science.288.5470.1390;
RA Kolbe M., Besir H., Essen L.-O., Oesterhelt D.;
RT "Structure of the light-driven chloride pump halorhodopsin at 1.8-A
RT resolution.";
RL Science 288:1390-1396(2000).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH CHLORIDE, AND
RP RETINAL-BINDING SITE.
RC STRAIN=R1 / S9 / D2;
RX PubMed=17117890; DOI=10.1562/2006-06-23-ra-947;
RA Gmelin W., Zeth K., Efremov R., Heberle J., Tittor J., Oesterhelt D.;
RT "The crystal structure of the L1 intermediate of halorhodopsin at 1.9
RT angstroms resolution.";
RL Photochem. Photobiol. 83:369-377(2007).
CC -!- FUNCTION: Light-driven chloride pump. {ECO:0000269|PubMed:24409552}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Absorption:
CC Abs(max)=578 nm {ECO:0000269|PubMed:24409552};
CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:10827943,
CC ECO:0000269|PubMed:17117890}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10827943,
CC ECO:0000269|PubMed:24409552}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:10827943, ECO:0000269|PubMed:24409552}.
CC -!- SIMILARITY: Belongs to the archaeal/bacterial/fungal opsin family.
CC {ECO:0000305}.
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DR EMBL; X04777; CAB37866.1; -; Genomic_DNA.
DR EMBL; AM774415; CAP13054.1; -; Genomic_DNA.
DR PIR; A26161; A26161.
DR RefSeq; WP_010902090.1; NC_010364.1.
DR PDB; 1E12; X-ray; 1.80 A; A=22-274.
DR PDB; 2JAF; X-ray; 1.70 A; A=1-274.
DR PDB; 2JAG; X-ray; 1.93 A; A=1-274.
DR PDB; 5AHY; X-ray; 2.15 A; A=20-274.
DR PDB; 5AHZ; X-ray; 2.45 A; A=20-274.
DR PDB; 5G36; X-ray; 2.60 A; A=20-274.
DR PDBsum; 1E12; -.
DR PDBsum; 2JAF; -.
DR PDBsum; 2JAG; -.
DR PDBsum; 5AHY; -.
DR PDBsum; 5AHZ; -.
DR PDBsum; 5G36; -.
DR AlphaFoldDB; B0R2U4; -.
DR SMR; B0R2U4; -.
DR EnsemblBacteria; CAP13054; CAP13054; OE_1299R.
DR GeneID; 5952411; -.
DR GeneID; 62883752; -.
DR KEGG; hsl:OE_1299R; -.
DR HOGENOM; CLU_054785_5_1_2; -.
DR OMA; VCRQVFW; -.
DR PhylomeDB; B0R2U4; -.
DR Proteomes; UP000001321; Chromosome.
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; Chloride; Chromophore;
KW Direct protein sequencing; Ion transport; Membrane; Photoreceptor protein;
KW Receptor; Retinal protein; Sensory transduction; Transmembrane;
KW Transmembrane helix; Transport.
FT PROPEP 1..21
FT /id="PRO_0000428923"
FT CHAIN 22..274
FT /note="Halorhodopsin"
FT /id="PRO_0000428924"
FT TOPO_DOM 22..25
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:10827943"
FT TRANSMEM 26..51
FT /note="Helical; Name=Helix A"
FT TOPO_DOM 52..57
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:10827943"
FT TRANSMEM 58..81
FT /note="Helical; Name=Helix B"
FT TOPO_DOM 82..105
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:10827943"
FT TRANSMEM 106..127
FT /note="Helical; Name=Helix C"
FT TOPO_DOM 128..130
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:10827943"
FT TRANSMEM 131..154
FT /note="Helical; Name=Helix D"
FT TOPO_DOM 155..157
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:10827943"
FT TRANSMEM 158..180
FT /note="Helical; Name=Helix E"
FT TOPO_DOM 181..192
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:10827943"
FT TRANSMEM 193..216
FT /note="Helical; Name=Helix F"
FT TOPO_DOM 217..226
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:10827943"
FT TRANSMEM 227..255
FT /note="Helical; Name=Helix G"
FT TOPO_DOM 256..274
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:10827943"
FT BINDING 105
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:10827943,
FT ECO:0000269|PubMed:17117890"
FT BINDING 111
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:10827943,
FT ECO:0000269|PubMed:17117890"
FT BINDING 115
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:10827943,
FT ECO:0000269|PubMed:17117890"
FT MOD_RES 242
FT /note="N6-(retinylidene)lysine"
FT HELIX 27..50
FT /evidence="ECO:0007829|PDB:2JAF"
FT TURN 51..53
FT /evidence="ECO:0007829|PDB:2JAF"
FT HELIX 58..81
FT /evidence="ECO:0007829|PDB:2JAF"
FT TURN 82..85
FT /evidence="ECO:0007829|PDB:2JAF"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:2JAF"
FT TURN 96..99
FT /evidence="ECO:0007829|PDB:2JAF"
FT STRAND 100..104
FT /evidence="ECO:0007829|PDB:2JAF"
FT HELIX 106..127
FT /evidence="ECO:0007829|PDB:2JAF"
FT HELIX 131..153
FT /evidence="ECO:0007829|PDB:2JAF"
FT HELIX 158..180
FT /evidence="ECO:0007829|PDB:2JAF"
FT HELIX 182..189
FT /evidence="ECO:0007829|PDB:2JAF"
FT HELIX 193..216
FT /evidence="ECO:0007829|PDB:2JAF"
FT TURN 218..221
FT /evidence="ECO:0007829|PDB:2JAF"
FT HELIX 227..241
FT /evidence="ECO:0007829|PDB:2JAF"
FT HELIX 243..255
FT /evidence="ECO:0007829|PDB:2JAF"
FT HELIX 257..261
FT /evidence="ECO:0007829|PDB:2JAF"
SQ SEQUENCE 274 AA; 28874 MW; 8FEDBBEDC717CD6B CRC64;
MSITSVPGVV DAGVLGAQSA AAVRENALLS SSLWVNVALA GIAILVFVYM GRTIRPGRPR
LIWGATLMIP LVSISSYLGL LSGLTVGMIE MPAGHALAGE MVRSQWGRYL TWALSTPMIL
LALGLLADVD LGSLFTVIAA DIGMCVTGLA AAMTTSALLF RWAFYAISCA FFVVVLSALV
TDWAASASSA GTAEIFDTLR VLTVVLWLGY PIVWAVGVEG LALVQSVGVT SWAYSVLDVF
AKYVFAFILL RWVANNERTV AVAGQTLGTM SSDD
