ID   BACRM_HALWD             Reviewed;         246 AA.
AC   Q18DH5;
DT   14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Bacteriorhodopsin-II-like protein;
DE   AltName: Full=Bacteriorhodopsin-II;
DE   AltName: Full=Middle rhodopsin;
DE            Short=HwMR;
GN   Name=bop2; Synonyms=bopII; OrderedLocusNames=HQ_1017A;
OS   Haloquadratum walsbyi (strain DSM 16790 / HBSQ001).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae; Haloquadratum.
OX   NCBI_TaxID=362976;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16790 / HBSQ001;
RX   PubMed=16820047; DOI=10.1186/1471-2164-7-169;
RA   Bolhuis H., Palm P., Wende A., Falb M., Rampp M., Rodriguez-Valera F.,
RA   Pfeiffer F., Oesterhelt D.;
RT   "The genome of the square archaeon Haloquadratum walsbyi: life at the
RT   limits of water activity.";
RL   BMC Genomics 7:169-169(2006).
RN   [2]
RP   FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF ALA-201 AND
RP   MET-211.
RX   PubMed=21135094; DOI=10.1074/jbc.m110.190058;
RA   Sudo Y., Ihara K., Kobayashi S., Suzuki D., Irieda H., Kikukawa T.,
RA   Kandori H., Homma M.;
RT   "A microbial rhodopsin with a unique retinal composition shows both sensory
RT   rhodopsin II and bacteriorhodopsin-like properties.";
RL   J. Biol. Chem. 286:5967-5976(2011).
CC   -!- FUNCTION: Has no proton-pumping activity but is potentially capable of
CC       functioning as a sensory SRII-like protein. The chromophore contains
CC       36.5% all-trans-, 7.6% 11-cis- and 56.4% 13-cis-retinal in the dark and
CC       30.1% 11-cis- and 47.7% 13-cis-retinal upon illumination with >460 nm
CC       light. {ECO:0000269|PubMed:21135094}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Absorption:
CC         Abs(max)=485 nm {ECO:0000269|PubMed:21135094};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
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}.
CC   -!- CAUTION: Is called bop1 in PubMed:21135094. {ECO:0000305}.
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DR   EMBL; AM180088; CAJ51147.1; -; Genomic_DNA.
DR   RefSeq; WP_011570314.1; NC_008212.1.
DR   AlphaFoldDB; Q18DH5; -.
DR   SMR; Q18DH5; -.
DR   STRING; 362976.HQ_1017A; -.
DR   EnsemblBacteria; CAJ51147; CAJ51147; HQ_1017A.
DR   GeneID; 4193773; -.
DR   KEGG; hwa:HQ_1017A; -.
DR   eggNOG; arCOG02812; Archaea.
DR   HOGENOM; CLU_054785_5_1_2; -.
DR   OMA; IFHYITA; -.
DR   Proteomes; UP000001975; Chromosome.
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.
PE   1: Evidence at protein level;
KW   Cell membrane; Chromophore; Membrane; Photoreceptor protein; Receptor;
KW   Reference proteome; Retinal protein; Sensory transduction; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..246
FT                   /note="Bacteriorhodopsin-II-like protein"
FT                   /id="PRO_0000428848"
FT   TRANSMEM        7..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        45..65
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        82..102
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        107..127
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        135..155
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        182..202
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        205..225
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   SITE            84
FT                   /note="Primary proton acceptor"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         217
FT                   /note="N6-(retinylidene)lysine"
FT                   /evidence="ECO:0000250"
FT   MUTAGEN         201
FT                   /note="A->T: Able to induce phototactic response in
FT                   heterologous host; when associated with Y-211."
FT                   /evidence="ECO:0000269|PubMed:21135094"
FT   MUTAGEN         211
FT                   /note="M->Y: Able to induce phototactic response in
FT                   heterologous host; when associated with T-201."
FT                   /evidence="ECO:0000269|PubMed:21135094"
SQ   SEQUENCE   246 AA;  26658 MW;  5839F73BE76F4090 CRC64;
     MATPGSEATW LWIGTIGMVL GTVYFAVRGR GSTDPEQQTY YIITTLIPAI AAAAYLAMAT
     GLGVISMPIR GTEVIDIYWA RYADWLLTTP LLIIDLALVA GARKQTLYKL IIIDAIMILG
     GLAGSMMQQG AVIRIVWWAV STAAFIILLY YLLGELSERA RSRSAETGIV FNRLRNITLG
     LWALYPIVWI LGTGGGFGII AVTTEIMLYV MLDIGTKIGF GAVLLESQDV LQAASHPSST
     NDIKSH