ID   BACR2_HALMA             Reviewed;         250 AA.
AC   Q5V0R5;
DT   14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Bacteriorhodopsin-II;
DE            Short=HmBRII;
GN   Name=xop1; OrderedLocusNames=rrnAC2030;
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: Light-driven proton pump. {ECO:0000269|PubMed:20802037}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Absorption:
CC         Abs(max)=552 nm {ECO:0000269|PubMed:20802037};
CC         Note=Unchanged lambda max with pHs of 3.0 to 9.0.;
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; AAV46888.1; -; Genomic_DNA.
DR   RefSeq; WP_004514987.1; NZ_CP039138.1.
DR   AlphaFoldDB; Q5V0R5; -.
DR   SMR; Q5V0R5; -.
DR   STRING; 272569.rrnAC2030; -.
DR   EnsemblBacteria; AAV46888; AAV46888; rrnAC2030.
DR   GeneID; 40152950; -.
DR   GeneID; 64821437; -.
DR   KEGG; hma:rrnAC2030; -.
DR   PATRIC; fig|272569.17.peg.2682; -.
DR   eggNOG; arCOG02812; Archaea.
DR   HOGENOM; CLU_054785_5_1_2; -.
DR   OMA; VGWAIYP; -.
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.
PE   1: Evidence at protein level;
KW   Chromophore; Hydrogen ion transport; Ion transport; Membrane;
KW   Photoreceptor protein; Receptor; Reference proteome; Retinal protein;
KW   Sensory transduction; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..250
FT                   /note="Bacteriorhodopsin-II"
FT                   /id="PRO_0000428850"
FT   TRANSMEM        14..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        49..69
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        89..109
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        114..134
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        142..162
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        183..203
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        210..230
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   SITE            91
FT                   /note="Primary proton acceptor"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         222
FT                   /note="N6-(retinylidene)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   250 AA;  27003 MW;  BD8FCB91D0CC2D45 CRC64;
     MLPLQVSSLG VEGEGIWLAL GTVGMLLGMV YFMAKGWDVQ DPEQEEFYVI TILIAGIAAS
     SYLSMFFGFG LTEVELVNGR VIDVYWARYA DWLFTTPLLL LDIGLLAGAS NRDMASLITI
     DAFMIVTGLA ATLMKVPVAR YAFWTISTIA MLFVLYYLVV VVGEAASDAS EEAQSTFNVL
     RNIILVAWAI YPVAWLVGTE GLGLVGLFGE TLLFMILDLT AKIGFGFILL RSRAIVGGDS
     APTPSAEAAD