BACS1_HALS3
ID BACS1_HALS3 Reviewed; 239 AA.
AC B0R633; P25964; Q9HPF5;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Sensory rhodopsin-1;
DE AltName: Full=Sensory rhodopsin I;
DE Short=SR-I;
GN Name=sopI; OrderedLocusNames=OE_3348F;
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=2591367; DOI=10.1002/j.1460-2075.1989.tb08579.x;
RA Blanck A., Oesterhelt D., Ferrando E., Schegk E.S., Lottspeich F.;
RT "Primary structure of sensory rhodopsin I, a prokaryotic photoreceptor.";
RL EMBO J. 8:3963-3971(1989).
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.
RC STRAIN=M407;
RX PubMed=2213884; DOI=10.1016/s0022-2836(05)80346-8;
RA Marwan W., Oesterhelt D.;
RT "Quantitation of photochromism of sensory rhodopsin-I by computerized
RT tracking of Halobacterium halobium cells.";
RL J. Mol. Biol. 215:277-285(1990).
RN [4]
RP FUNCTION, INTERACTION WITH HTR-I, AND SUBCELLULAR LOCATION.
RC STRAIN=R1 / S9 / L33;
RX PubMed=8187768; DOI=10.1002/j.1460-2075.1994.tb06491.x;
RA Krah M., Marwan W., Vermeglio A., Oesterhelt D.;
RT "Phototaxis of Halobacterium salinarium requires a signalling complex of
RT sensory rhodopsin I and its methyl-accepting transducer HtrI.";
RL EMBO J. 13:2150-2155(1994).
RN [5]
RP FUNCTION.
RC STRAIN=R1 / S9 / L33 / M417;
RX PubMed=7877170; DOI=10.1006/jmbi.1994.0101;
RA Marwan W., Bibikov S.I., Montrone M., Oesterhelt D.;
RT "Mechanism of photosensory adaptation in Halobacterium salinarium.";
RL J. Mol. Biol. 246:493-499(1995).
CC -!- FUNCTION: Involved in the control of phototaxis. Mediates both
CC photoattractant (in the orange light) and photophobic (in the near UV
CC light) responses. The signal is then transmitted to the sensory
CC rhodopsin I transducer (HTR-I). {ECO:0000269|PubMed:2213884,
CC ECO:0000269|PubMed:7877170, ECO:0000269|PubMed:8187768}.
CC -!- SUBUNIT: Interacts with HTR-I. {ECO:0000269|PubMed:8187768}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8187768};
CC Multi-pass membrane protein {ECO:0000269|PubMed:8187768}.
CC -!- SIMILARITY: Belongs to the archaeal/bacterial/fungal opsin family.
CC {ECO:0000305}.
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DR EMBL; X51682; CAA35984.1; -; Genomic_DNA.
DR EMBL; AM774415; CAP14202.1; -; Genomic_DNA.
DR PIR; S09277; S09277.
DR RefSeq; WP_010903211.1; NC_010364.1.
DR AlphaFoldDB; B0R633; -.
DR SMR; B0R633; -.
DR EnsemblBacteria; CAP14202; CAP14202; OE_3348F.
DR GeneID; 5953902; -.
DR KEGG; hsl:OE_3348F; -.
DR HOGENOM; CLU_054785_5_1_2; -.
DR OMA; SIMIMYM; -.
DR PhylomeDB; B0R633; -.
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 Cell membrane; Chromophore; Direct protein sequencing; Membrane;
KW Photoreceptor protein; Receptor; Retinal protein; Sensory transduction;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..239
FT /note="Sensory rhodopsin-1"
FT /id="PRO_0000428960"
FT TOPO_DOM 1..3
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 4..25
FT /note="Helical; Name=Helix A"
FT /evidence="ECO:0000250"
FT TOPO_DOM 26..34
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 35..56
FT /note="Helical; Name=Helix B"
FT /evidence="ECO:0000250"
FT TOPO_DOM 57..70
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 71..92
FT /note="Helical; Name=Helix C"
FT /evidence="ECO:0000250"
FT TOPO_DOM 93..95
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 96..118
FT /note="Helical; Name=Helix D"
FT /evidence="ECO:0000250"
FT TOPO_DOM 119..122
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 123..150
FT /note="Helical; Name=Helix E"
FT /evidence="ECO:0000250"
FT TOPO_DOM 151..153
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 154..181
FT /note="Helical; Name=Helix F"
FT /evidence="ECO:0000250"
FT TOPO_DOM 182..189
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 190..222
FT /note="Helical; Name=Helix G"
FT /evidence="ECO:0000250"
FT TOPO_DOM 223..239
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT MOD_RES 205
FT /note="N6-(retinylidene)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 239 AA; 25501 MW; 2496161B60425DE3 CRC64;
MDAVATAYLG GAVALIVGVA FVWLLYRSLD GSPHQSALAP LAIIPVFAGL SYVGMAYDIG
TVIVNGNQIV GLRYIDWLVT TPILVGYVGY AAGASRRSII GVMVADALMI AVGAGAVVTD
GTLKWALFGV SSIFHLSLFA YLYVIFPRVV PDVPEQIGLF NLLKNHIGLL WLAYPLVWLF
GPAGIGEATA AGVALTYVFL DVLAKVPYVY FFYARRRVFM HSESPPAPEQ ATVEATAAD
