ID   BACS1_HALMA             Reviewed;         236 AA.
AC   Q5UXM9;
DT   14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Sensory rhodopsin I;
DE            Short=HmSRI;
GN   Name=sop1; OrderedLocusNames=rrnAC3280;
OS   Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM
OS   B-1809) (Halobacterium marismortui).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Haloarcula.
OX   NCBI_TaxID=272569;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX   PubMed=15520287; DOI=10.1101/gr.2700304;
RA   Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W.,
RA   Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E.,
RA   Hood L., Ng W.V.;
RT   "Genome sequence of Haloarcula marismortui: a halophilic archaeon from the
RT   Dead Sea.";
RL   Genome Res. 14:2221-2234(2004).
RN   [2]
RP   FUNCTION, INDUCTION, CHARACTERIZATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=20802037; DOI=10.1128/jb.00642-10;
RA   Fu H.Y., Lin Y.C., Chang Y.N., Tseng H., Huang C.C., Liu K.C., Huang C.S.,
RA   Su C.W., Weng R.R., Lee Y.Y., Ng W.V., Yang C.S.;
RT   "A novel six-rhodopsin system in a single archaeon.";
RL   J. Bacteriol. 192:5866-5873(2010).
RN   [3]
RP   FUNCTION, INTERACTION WITH HTR1, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=23474528; DOI=10.1016/j.jphotobiol.2013.02.002;
RA   Fu H.Y., Lu Y.H., Yi H.P., Yang C.S.;
RT   "A transducer for microbial sensory rhodopsin that adopts GTG as a start
RT   codon is identified in Haloarcula marismortui.";
RL   J. Photochem. Photobiol. B 121:15-22(2013).
CC   -!- FUNCTION: Photoattractant rhodopsin. {ECO:0000269|PubMed:20802037,
CC       ECO:0000269|PubMed:23474528}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Absorption:
CC         Abs(max)=578 nm {ECO:0000269|PubMed:20802037,
CC         ECO:0000269|PubMed:23474528};
CC         Note=Lamda max is 538 nm when pH shifts from 5.0 to 8.0.;
CC   -!- SUBUNIT: Interacts with Htr1. {ECO:0000269|PubMed:23474528}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- INDUCTION: Expressed constitutively throughout the growth phases, both
CC       in presence and absence of white light. {ECO:0000269|PubMed:20802037}.
CC   -!- PTM: The covalent binding of retinal to the apoprotein, bacterioopsin,
CC       generates bacteriorhodopsin. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the archaeal/bacterial/fungal opsin family.
CC       {ECO:0000305}.
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DR   EMBL; AY596297; AAV47974.1; -; Genomic_DNA.
DR   RefSeq; WP_004964156.1; NZ_CP039138.1.
DR   AlphaFoldDB; Q5UXM9; -.
DR   SMR; Q5UXM9; -.
DR   STRING; 272569.rrnAC3280; -.
DR   EnsemblBacteria; AAV47974; AAV47974; rrnAC3280.
DR   GeneID; 40154076; -.
DR   GeneID; 64823472; -.
DR   KEGG; hma:rrnAC3280; -.
DR   PATRIC; fig|272569.17.peg.3811; -.
DR   eggNOG; arCOG02810; Archaea.
DR   HOGENOM; CLU_054785_5_1_2; -.
DR   OMA; SIMIMYM; -.
DR   Proteomes; UP000001169; Chromosome I.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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   Chromophore; Membrane; Photoreceptor protein; Receptor; Reference proteome;
KW   Retinal protein; Sensory transduction; Transmembrane; Transmembrane helix.
FT   CHAIN           1..236
FT                   /note="Sensory rhodopsin I"
FT                   /id="PRO_0000428854"
FT   TRANSMEM        6..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        37..57
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        74..94
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        98..118
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        126..146
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        167..187
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        192..212
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   SITE            76
FT                   /note="Primary proton acceptor"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         205
FT                   /note="N6-(retinylidene)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   236 AA;  25051 MW;  41A3A0481066C65E CRC64;
     MDAVSVVYGI TAAGFAVGVA IVGFLYASLE GSDERPILAA LALIPGVAGI SYVAMVFGIG
     TVTIGETTLV GFRYLDWVVT TPLLVGFIGY TAGASRRAIF GVMAADALMI LAGVGAVVAA
     GTLKWALFGV SAVFHISLFA YLYLIFPRSV PDDPQRIGLF SLLKNHVGLL WIAYPLVWLA
     GPEGLGFATY VGVSITYAFL DLLAKVPYVY FFYARRQVFA TKLLRDSGDT TVTPAD