ID   BACS3_HALMA             Reviewed;         232 AA.
AC   Q5V4H7;
DT   14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=Sensory rhodopsin III;
DE            Short=HmSRIII;
DE   AltName: Full=Opsin;
DE   AltName: Full=Sensory-like rhodopsin;
DE            Short=HmSMR;
GN   Name=xop2; Synonyms=sop3; OrderedLocusNames=rrnAC0559;
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, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP   INTERACTION WITH HTRM.
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, BIOPHYSICOCHEMICAL PROPERTIES, AND NOMENCLATURE.
RX   PubMed=20880715; DOI=10.1016/j.jphotobiol.2010.09.004;
RA   Nakao Y., Kikukawa T., Shimono K., Tamogami J., Kimitsuki N., Nara T.,
RA   Unno M., Ihara K., Kamo N.;
RT   "Photochemistry of a putative new class of sensory rhodopsin (SRIII) coded
RT   by xop2 of Haloarcular marismortui.";
RL   J. Photochem. Photobiol. B 102:45-54(2011).
CC   -!- FUNCTION: Sensory rhodopsin. Associates with an unusual transducer
CC       lacking a methyl-accepting transducer domain found in all other
CC       photosensory transducers. The chromophore is all-trans-retinal in the
CC       dark. {ECO:0000269|PubMed:20802037, ECO:0000269|PubMed:20880715}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Absorption:
CC         Abs(max)=506 nm {ECO:0000269|PubMed:20802037,
CC         ECO:0000269|PubMed:20880715};
CC   -!- SUBUNIT: Interacts with HtrM. {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; AAV45575.1; -; Genomic_DNA.
DR   RefSeq; WP_004962072.1; NZ_CP039138.1.
DR   AlphaFoldDB; Q5V4H7; -.
DR   SMR; Q5V4H7; -.
DR   STRING; 272569.rrnAC0559; -.
DR   TCDB; 3.E.1.3.4; the ion-translocating microbial rhodopsin (mr) family.
DR   EnsemblBacteria; AAV45575; AAV45575; rrnAC0559.
DR   GeneID; 40151614; -.
DR   GeneID; 64822726; -.
DR   KEGG; hma:rrnAC0559; -.
DR   PATRIC; fig|272569.17.peg.1323; -.
DR   eggNOG; arCOG02810; Archaea.
DR   HOGENOM; CLU_054785_5_1_2; -.
DR   Proteomes; UP000001169; Chromosome I.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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   PANTHER; PTHR28286; PTHR28286; 1.
DR   Pfam; PF01036; Bac_rhodopsin; 1.
DR   PRINTS; PR00251; BACTRLOPSIN.
DR   SMART; SM01021; Bac_rhodopsin; 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..232
FT                   /note="Sensory rhodopsin III"
FT                   /id="PRO_0000428855"
FT   TRANSMEM        5..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        39..59
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        73..93
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        100..120
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        125..145
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        168..188
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        194..214
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   SITE            75
FT                   /note="Primary proton acceptor"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         205
FT                   /note="N6-(retinylidene)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   232 AA;  25084 MW;  198AD3B352481652 CRC64;
     MAQEIVWYGA GAGAFFVSAV VFVWFAATRG NIRSSFYYLP PIHTSVAGAA YVAMALIAGG
     QLGDTVSITT LRFADWIVST PIITYYLARL AGVDTQTRRL AVAANVVMIG VGYGFVSMSG
     SLRWIAFAVS TVAFIGLLYL YIKTFARKIN AATASVRSLF QSLRDLTVVT WSLYPVVYFL
     GPLGTGIIQA PDLNFLVAVL DTIAKVGFMS ILLVRYNSVE TFVDSWSVAP AK