BACS2_NATPH
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 03-AUG-2022, entry version 121.
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; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; 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 (2.4 ANGSTROMS) OF 1-217, 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 (1.9 ANGSTROMS) OF 1-225, FUNCTION, INTERACTION WITH
RP HTR-II, AND 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 (2.1 ANGSTROMS) OF 2-219, SUBUNIT, AND
RP 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 (2.27 ANGSTROMS) OF 2-219, SUBCELLULAR LOCATION, AND
RP 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 PDBsum; 1GU8; -.
DR PDBsum; 1GUE; -.
DR PDBsum; 1H2S; -.
DR PDBsum; 1H68; -.
DR PDBsum; 1JGJ; -.
DR PDBsum; 2F93; -.
DR PDBsum; 2F95; -.
DR PDBsum; 3QAP; -.
DR PDBsum; 3QDC; -.
DR PDBsum; 4GYC; -.
DR PDBsum; 5JJE; -.
DR PDBsum; 5JJF; -.
DR PDBsum; 5JJJ; -.
DR PDBsum; 5JJN; -.
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 EvolutionaryTrace; P42196; -.
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; 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 2..26
FT /evidence="ECO:0007829|PDB:3QAP"
FT TURN 31..33
FT /evidence="ECO:0007829|PDB:3QAP"
FT HELIX 34..55
FT /evidence="ECO:0007829|PDB:3QAP"
FT TURN 56..59
FT /evidence="ECO:0007829|PDB:1JGJ"
FT STRAND 60..63
FT /evidence="ECO:0007829|PDB:3QAP"
FT STRAND 66..69
FT /evidence="ECO:0007829|PDB:3QAP"
FT HELIX 70..91
FT /evidence="ECO:0007829|PDB:3QAP"
FT HELIX 95..117
FT /evidence="ECO:0007829|PDB:3QAP"
FT HELIX 123..142
FT /evidence="ECO:0007829|PDB:3QAP"
FT HELIX 144..149
FT /evidence="ECO:0007829|PDB:3QAP"
FT HELIX 154..171
FT /evidence="ECO:0007829|PDB:3QAP"
FT HELIX 173..180
FT /evidence="ECO:0007829|PDB:3QAP"
FT TURN 182..185
FT /evidence="ECO:0007829|PDB:3QAP"
FT HELIX 190..218
FT /evidence="ECO:0007829|PDB:3QAP"
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
