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BACR1_HALWC
ID   BACR1_HALWC             Reviewed;         254 AA.
AC   G0LFX8;
DT   14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT   19-OCT-2011, sequence version 1.
DT   03-AUG-2022, entry version 57.
DE   RecName: Full=Bacteriorhodopsin-I;
DE   Flags: Precursor;
GN   Name=bop1; OrderedLocusNames=Hqrw_1016;
OS   Haloquadratum walsbyi (strain DSM 16854 / JCM 12705 / C23).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae; Haloquadratum.
OX   NCBI_TaxID=768065;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   STRAIN=DSM 16854 / JCM 12705 / C23;
RX   PubMed=21701686; DOI=10.1371/journal.pone.0020968;
RA   Dyall-Smith M., Pfeiffer F., Klee K., Palm P., Gross K., Schuster S.C.,
RA   Rampp M., Oesterhelt D.;
RT   "Haloquadratum walsbyi: limited diversity in a global pond.";
RL   PLoS ONE 6:E20968-E20968(2011).
CC   -!- FUNCTION: Light-driven proton pump. {ECO:0000250}.
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}.
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DR   EMBL; FR746099; CCC38998.1; -; Genomic_DNA.
DR   RefSeq; WP_011570311.1; NC_017459.1.
DR   PDB; 4WAV; X-ray; 2.80 A; A/B=1-254.
DR   PDBsum; 4WAV; -.
DR   AlphaFoldDB; G0LFX8; -.
DR   SMR; G0LFX8; -.
DR   TCDB; 3.E.1.1.3; the ion-translocating microbial rhodopsin (mr) family.
DR   EnsemblBacteria; CCC38998; CCC38998; Hqrw_1016.
DR   GeneID; 4193772; -.
DR   KEGG; hwc:Hqrw_1016; -.
DR   HOGENOM; CLU_054785_5_1_2; -.
DR   OMA; VGWAIYP; -.
DR   OrthoDB; 90087at2157; -.
DR   Proteomes; UP000007954; 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.
DR   PROSITE; PS00327; BACTERIAL_OPSIN_RET; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell membrane; Chromophore; Hydrogen ion transport;
KW   Ion transport; Membrane; Photoreceptor protein;
KW   Pyrrolidone carboxylic acid; Receptor; Retinal protein;
KW   Sensory transduction; Transmembrane; Transmembrane helix; Transport.
FT   PROPEP          1..6
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000428844"
FT   CHAIN           7..254
FT                   /note="Bacteriorhodopsin-I"
FT                   /id="PRO_0000428845"
FT   TRANSMEM        16..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        51..71
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        91..111
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        116..136
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        144..164
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        185..205
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        212..232
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   SITE            93
FT                   /note="Primary proton acceptor"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         7
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         224
FT                   /note="N6-(retinylidene)lysine"
FT                   /evidence="ECO:0000250"
FT   HELIX           17..37
FT                   /evidence="ECO:0007829|PDB:4WAV"
FT   HELIX           44..68
FT                   /evidence="ECO:0007829|PDB:4WAV"
FT   TURN            69..72
FT                   /evidence="ECO:0007829|PDB:4WAV"
FT   STRAND          75..77
FT                   /evidence="ECO:0007829|PDB:4WAV"
FT   STRAND          83..85
FT                   /evidence="ECO:0007829|PDB:4WAV"
FT   HELIX           89..109
FT                   /evidence="ECO:0007829|PDB:4WAV"
FT   HELIX           113..135
FT                   /evidence="ECO:0007829|PDB:4WAV"
FT   HELIX           139..168
FT                   /evidence="ECO:0007829|PDB:4WAV"
FT   HELIX           173..190
FT                   /evidence="ECO:0007829|PDB:4WAV"
FT   HELIX           193..199
FT                   /evidence="ECO:0007829|PDB:4WAV"
FT   TURN            201..204
FT                   /evidence="ECO:0007829|PDB:4WAV"
FT   HELIX           209..232
FT                   /evidence="ECO:0007829|PDB:4WAV"
SQ   SEQUENCE   254 AA;  27423 MW;  110CC901DDF50298 CRC64;
     MSQLALQMSS LGVEGEGIWL ALGTIGMLLG MLYFIADGLD VQDPRQKEFY VITILIPAIA
     AASYLSMFFG FGLTEVSLAN GRVVDVYWAR YADWLFTTPL LLLDIGLLAG ASQRDIGALV
     GIDAFMIVTG LVATLTKVVV ARYAFWTIST ISMVFLLYYL VAVFGEAVSD ADEDTRSTFN
     ALRNIILVTW AIYPVAWLVG TEGLALTGLY GETLLFMVLD LVAKVGFGFI LLRSRAIMGG
     GSEPTPSAQE TAAD
 
 
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