ID   BACS2_HALMA             Reviewed;         236 AA.
AC   Q5V5V3;
DT   14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Sensory rhodopsin II;
DE            Short=HmSRII;
GN   Name=sop2; OrderedLocusNames=rrnAC0014;
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).
CC   -!- FUNCTION: Mediates the photorepellent response.
CC       {ECO:0000269|PubMed:20802037}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Absorption:
CC         Abs(max)=483 nm {ECO:0000269|PubMed:20802037};
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; AAV45099.1; -; Genomic_DNA.
DR   RefSeq; WP_011222779.1; NZ_CP039138.1.
DR   AlphaFoldDB; Q5V5V3; -.
DR   SMR; Q5V5V3; -.
DR   STRING; 272569.rrnAC0014; -.
DR   EnsemblBacteria; AAV45099; AAV45099; rrnAC0014.
DR   GeneID; 40154333; -.
DR   KEGG; hma:rrnAC0014; -.
DR   PATRIC; fig|272569.17.peg.828; -.
DR   eggNOG; arCOG02810; Archaea.
DR   HOGENOM; CLU_054785_5_1_2; -.
DR   OMA; IFHYITA; -.
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 II"
FT                   /id="PRO_0000428853"
FT   TRANSMEM        4..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        38..58
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        73..93
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        101..121
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        122..142
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        167..187
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        196..216
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   SITE            75
FT                   /note="Primary proton acceptor"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         206
FT                   /note="N6-(retinylidene)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   236 AA;  25053 MW;  DCB6DC5713C150E1 CRC64;
     MATITTWFTL GLLGELLGTA VLAYGYTLVP EETRKRYLLL IAIPGIAIVA YALMALGFGS
     IQSEGHAVYV VRYVDWLLTT PLNVWFLALL AGASREDTVK LVVLQALTIV FGFAGAVTPS
     PVSYALFAVG GALFGGVIYL LYRNIAVAAK STLSDIEVSL YRTLRNFVVV LWLVYPVVWL
     LGAAGVGLMD VETATLVVVY LDVVTKVGFG VIALLAMIDL GSAGETAEEP TAVAGD