ID   BACS2_NATPH             Reviewed;         239 AA.
AC   P42196;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   04-NOV-2026, entry version 134.
DE   RecName: Full=Sensory rhodopsin-2;
DE   AltName: Full=Sensory rhodopsin II;
DE            Short=SR-II;
GN   Name=sop2; Synonyms=sopII;
OS   Natronomonas pharaonis (Natronobacterium pharaonis).
OC   Archaea; Methanobacteriati; Methanobacteriota; Stenosarchaea group;
OC   Halobacteria; Halobacteriales; Natronomonadaceae; Natronomonas.
OX   NCBI_TaxID=2257;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=SP-1 / 28;
RX   PubMed=7708770; DOI=10.1073/pnas.92.7.3036;
RA   Seidel R., Scharf B., Gautel M., Kleine K., Oesterhelt D., Engelhard M.;
RT   "The primary structure of sensory rhodopsin II: a member of an additional
RT   retinal protein subgroup is coexpressed with its transducer, the
RT   halobacterial transducer of rhodopsin II.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:3036-3040(1995).
RN   [2]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RC   STRAIN=SP-1 / 28;
RX   PubMed=1597180; DOI=10.1111/j.1432-1033.1992.tb16935.x;
RA   Scharf B., Pevec B., Hess B., Engelhard M.;
RT   "Biochemical and photochemical properties of the photophobic receptors from
RT   Halobacterium halobium and Natronobacterium pharaonis.";
RL   Eur. J. Biochem. 206:359-366(1992).
RN   [3]
RP   FUNCTION.
RX   PubMed=9598990; DOI=10.1016/s0014-5793(98)00322-6;
RA   Luttenberg B., Wolff E.K., Engelhard M.;
RT   "Heterologous coexpression of the blue light receptor psRII and its
RT   transducer pHtrII from Natronobacterium pharaonis in the Halobacterium
RT   salinarium strain Pho81/w restores negative phototaxis.";
RL   FEBS Lett. 426:117-120(1998).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY, AND RETINAL-BINDING SITE.
RX   PubMed=11452084; DOI=10.1126/science.1062977;
RA   Luecke H., Schobert B., Lanyi J.K., Spudich E.N., Spudich J.L.;
RT   "Crystal structure of sensory rhodopsin II at 2.4 Angstroms: insights into
RT   color tuning and transducer interaction.";
RL   Science 293:1499-1503(2001).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY, FUNCTION, INTERACTION WITH HTR-II, AND
RP   RETINAL-BINDING SITE.
RX   PubMed=12368857; DOI=10.1038/nature01109;
RA   Gordeliy V.I., Labahn J., Moukhametzianov R., Efremov R., Granzin J.,
RA   Schlesinger R., Bueldt G., Savopol T., Scheidig A.J., Klare J.P.,
RA   Engelhard M.;
RT   "Molecular basis of transmembrane signalling by sensory rhodopsin II-
RT   transducer complex.";
RL   Nature 419:484-487(2002).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY, SUBUNIT, AND RETINAL-BINDING SITE.
RX   PubMed=11504917; DOI=10.1073/pnas.181203898;
RA   Royant A., Nollert P., Edman K., Neutze R., Landau E.M., Pebay-Peyroula E.,
RA   Navarro J.;
RT   "X-ray structure of sensory rhodopsin II at 2.1-A resolution.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:10131-10136(2001).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY, SUBCELLULAR LOCATION, AND RETINAL-BINDING SITE.
RX   PubMed=11937052; DOI=10.1016/s0969-2126(02)00736-0;
RA   Edman K., Royant A., Nollert P., Maxwell C.A., Pebay-Peyroula E.,
RA   Navarro J., Neutze R., Landau E.M.;
RT   "Early structural rearrangements in the photocycle of an integral membrane
RT   sensory receptor.";
RL   Structure 10:473-482(2002).
CC   -!- FUNCTION: Photophobic photoreceptor responsible for the negative
CC       phototaxis. Activates the sensory rhodopsin II transducer (HTR-II) in
CC       response to blue light. {ECO:0000269|PubMed:12368857,
CC       ECO:0000269|PubMed:1597180, ECO:0000269|PubMed:9598990}.
CC   -!- SUBUNIT: Homodimer. Interacts with HTR-II.
CC       {ECO:0000269|PubMed:11504917, ECO:0000269|PubMed:12368857}.
CC   -!- INTERACTION:
CC       P42196; P42259: htr2; NbExp=5; IntAct=EBI-1034509, EBI-1034515;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11937052,
CC       ECO:0000269|PubMed:1597180}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:11937052, ECO:0000269|PubMed:1597180}.
CC   -!- SIMILARITY: Belongs to the archaeal/bacterial/fungal opsin family.
CC       {ECO:0000305}.
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DR   EMBL; Z35086; CAA84469.1; -; Genomic_DNA.
DR   PIR; S55300; S55300.
DR   PDB; 1GU8; X-ray; 2.27 A; A=1-239.
DR   PDB; 1GUE; X-ray; 2.27 A; A=1-239.
DR   PDB; 1H2S; X-ray; 1.93 A; A=1-225.
DR   PDB; 1H68; X-ray; 2.10 A; A=1-239.
DR   PDB; 1JGJ; X-ray; 2.40 A; A=1-217.
DR   PDB; 2F93; X-ray; 2.00 A; A=2-239.
DR   PDB; 2F95; X-ray; 2.20 A; A=2-239.
DR   PDB; 3QAP; X-ray; 1.90 A; A=1-239.
DR   PDB; 3QDC; X-ray; 2.50 A; A=1-239.
DR   PDB; 4GYC; X-ray; 2.05 A; A=1-239.
DR   PDB; 5JJE; X-ray; 1.90 A; A=2-239.
DR   PDB; 5JJF; X-ray; 1.90 A; A=2-239.
DR   PDB; 5JJJ; X-ray; 2.50 A; A=2-239.
DR   PDB; 5JJN; X-ray; 2.25 A; A/C=2-239.
DR   PDB; 7ZCM; X-ray; 2.85 A; A=1-225.
DR   PDB; 8PWG; X-ray; 1.94 A; A=1-239.
DR   PDB; 8PWI; X-ray; 1.96 A; A=1-239.
DR   PDB; 8PWJ; X-ray; 2.14 A; A=1-239.
DR   PDB; 8PWP; X-ray; 2.08 A; A=1-239.
DR   PDB; 8PWQ; X-ray; 1.95 A; A=1-239.
DR   PDB; 9H1W; X-ray; 2.20 A; A=1-239.
DR   PDB; 9H1X; X-ray; 1.85 A; A=1-239.
DR   PDB; 9H20; X-ray; 2.20 A; A=1-239.
DR   AlphaFoldDB; P42196; -.
DR   BMRB; P42196; -.
DR   SASBDB; P42196; -.
DR   SMR; P42196; -.
DR   DIP; DIP-35282N; -.
DR   IntAct; P42196; 1.
DR   TCDB; 3.E.1.3.3; the ion-translocating microbial rhodopsin (mr) family.
DR   OMA; AAVHYWY; -.
DR   EvolutionaryTrace; P42196; -.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005216; F:monoatomic ion channel activity; IEA:InterPro.
DR   CDD; cd15029; 7tm_SRI_SRII; 1.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   InterPro; IPR001425; Arc/bac/fun_rhodopsins.
DR   InterPro; IPR018229; Rhodopsin_retinal_BS.
DR   PANTHER; PTHR28286; -; 1.
DR   PANTHER; PTHR28286:SF2; BACTERIORHODOPSIN _OPSIN, NOPA (EUROFUNG); 1.
DR   Pfam; PF01036; Bac_rhodopsin; 1.
DR   PRINTS; PR00251; BACTRLOPSIN.
DR   SMART; SM01021; Bac_rhodopsin; 1.
DR   SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 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; Membrane; Photoreceptor protein;
KW   Receptor; Retinal protein; Sensory transduction; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..239
FT                   /note="Sensory rhodopsin-2"
FT                   /id="PRO_0000196282"
FT   TOPO_DOM        1..3
FT                   /note="Extracellular"
FT   TRANSMEM        4..25
FT                   /note="Helical; Name=Helix A"
FT   TOPO_DOM        26..33
FT                   /note="Cytoplasmic"
FT   TRANSMEM        34..55
FT                   /note="Helical; Name=Helix B"
FT   TOPO_DOM        56..69
FT                   /note="Extracellular"
FT   TRANSMEM        70..91
FT                   /note="Helical; Name=Helix C"
FT   TOPO_DOM        92..94
FT                   /note="Cytoplasmic"
FT   TRANSMEM        95..117
FT                   /note="Helical; Name=Helix D"
FT   TOPO_DOM        118..121
FT                   /note="Extracellular"
FT   TRANSMEM        122..149
FT                   /note="Helical; Name=Helix E"
FT   TOPO_DOM        150..153
FT                   /note="Cytoplasmic"
FT   TRANSMEM        154..181
FT                   /note="Helical; Name=Helix F"
FT   TOPO_DOM        182..189
FT                   /note="Extracellular"
FT   TRANSMEM        190..222
FT                   /note="Helical; Name=Helix G"
FT   TOPO_DOM        223..239
FT                   /note="Cytoplasmic"
FT   MOD_RES         205
FT                   /note="N6-(retinylidene)lysine"
FT   HELIX           4..25
FT                   /evidence="ECO:0007829|PDB:9H1X"
FT   TURN            26..28
FT                   /evidence="ECO:0007829|PDB:1H2S"
FT   TURN            31..33
FT                   /evidence="ECO:0007829|PDB:3QAP"
FT   HELIX           36..55
FT                   /evidence="ECO:0007829|PDB:9H1X"
FT   TURN            56..59
FT                   /evidence="ECO:0007829|PDB:9H1X"
FT   STRAND          60..63
FT                   /evidence="ECO:0007829|PDB:9H1X"
FT   STRAND          66..69
FT                   /evidence="ECO:0007829|PDB:9H1X"
FT   HELIX           70..91
FT                   /evidence="ECO:0007829|PDB:9H1X"
FT   HELIX           95..117
FT                   /evidence="ECO:0007829|PDB:9H1X"
FT   HELIX           123..142
FT                   /evidence="ECO:0007829|PDB:9H1X"
FT   HELIX           144..149
FT                   /evidence="ECO:0007829|PDB:9H1X"
FT   HELIX           154..180
FT                   /evidence="ECO:0007829|PDB:9H1X"
FT   TURN            182..185
FT                   /evidence="ECO:0007829|PDB:9H1X"
FT   HELIX           190..201
FT                   /evidence="ECO:0007829|PDB:9H1X"
FT   HELIX           202..207
FT                   /evidence="ECO:0007829|PDB:9H1X"
FT   HELIX           208..216
FT                   /evidence="ECO:0007829|PDB:9H1X"
SQ   SEQUENCE   239 AA;  25355 MW;  C0E93EAF341B6B19 CRC64;
     MVGLTTLFWL GAIGMLVGTL AFAWAGRDAG SGERRYYVTL VGISGIAAVA YVVMALGVGW
     VPVAERTVFA PRYIDWILTT PLIVYFLGLL AGLDSREFGI VITLNTVVML AGFAGAMVPG
     IERYALFGMG AVAFLGLVYY LVGPMTESAS QRSSGIKSLY VRLRNLTVIL WAIYPFIWLL
     GPPGVALLTP TVDVALIVYL DLVTKVGFGF IALDAAATLR AEHGESLAGV DTDAPAVAD
//