BACR1_HALWD
ID BACR1_HALWD Reviewed; 254 AA.
AC Q18DH8;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Bacteriorhodopsin-I;
DE Short=HwBR;
DE AltName: Full=Squarebop I;
DE Flags: Precursor;
GN Name=bop1; Synonyms=bopI; OrderedLocusNames=HQ_1014A;
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, AND BIOPHYSICOCHEMICAL PROPERTIES.
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).
RN [3]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR LOCATION.
RX PubMed=22248212; DOI=10.1111/j.1751-1097.2012.01089.x;
RA Lobasso S., Lopalco P., Vitale R., Saponetti M.S., Capitanio G.,
RA Mangini V., Milano F., Trotta M., Corcelli A.;
RT "The light-activated proton pump Bop I of the archaeon Haloquadratum
RT walsbyi.";
RL Photochem. Photobiol. 88:690-700(2012).
RN [4]
RP FUNCTION, AND MUTAGENESIS OF MET-126; SER-149 AND ALA-223.
RX PubMed=23720753; DOI=10.1074/jbc.m113.475533;
RA Sudo Y., Okazaki A., Ono H., Yagasaki J., Sugo S., Kamiya M., Reissig L.,
RA Inoue K., Ihara K., Kandori H., Takagi S., Hayashi S.;
RT "A blue-shifted light-driven proton pump for neural silencing.";
RL J. Biol. Chem. 288:20624-20632(2013).
CC -!- FUNCTION: Light-driven proton pump. The chromophore contains 78% all-
CC trans- and 22% 13-cis-retinal in the dark and 90% all-trans- and 10%
CC 13-cis-retinal upon illumination with >500 nm light.
CC {ECO:0000269|PubMed:21135094, ECO:0000269|PubMed:22248212,
CC ECO:0000269|PubMed:23720753}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Absorption:
CC Abs(max)=552 nm {ECO:0000269|PubMed:21135094,
CC ECO:0000269|PubMed:22248212};
CC Note=In light-adapted form, max=555 nm. In the mutated form, max=498
CC nm.;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22248212};
CC Multi-pass membrane protein {ECO:0000269|PubMed:22248212}.
CC -!- PTM: The covalent binding of retinal to the apoprotein, bacterioopsin,
CC generates bacteriorhodopsin. {ECO:0000250}.
CC -!- MISCELLANEOUS: Different protein aggregation states can be observed,
CC leading to variations in the absorbance maxima.
CC {ECO:0000305|PubMed:22248212}.
CC -!- SIMILARITY: Belongs to the archaeal/bacterial/fungal opsin family.
CC {ECO:0000305}.
CC -!- CAUTION: Is called bop2 in PubMed:21135094. {ECO:0000305}.
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DR EMBL; AM180088; CAJ51144.1; -; Genomic_DNA.
DR RefSeq; WP_011570311.1; NC_008212.1.
DR PDB; 4QI1; X-ray; 1.85 A; A/B/C=3-254.
DR PDB; 4QID; X-ray; 2.57 A; A/B=3-254.
DR PDB; 5ITC; X-ray; 2.00 A; A/B/C=3-254.
DR PDB; 5ITE; X-ray; 2.18 A; A/B/C=3-254.
DR PDB; 5KKH; X-ray; 2.12 A; A/B/C=1-254.
DR PDBsum; 4QI1; -.
DR PDBsum; 4QID; -.
DR PDBsum; 5ITC; -.
DR PDBsum; 5ITE; -.
DR PDBsum; 5KKH; -.
DR AlphaFoldDB; Q18DH8; -.
DR SMR; Q18DH8; -.
DR STRING; 362976.HQ_1014A; -.
DR EnsemblBacteria; CAJ51144; CAJ51144; HQ_1014A.
DR GeneID; 4193772; -.
DR KEGG; hwa:HQ_1014A; -.
DR eggNOG; arCOG02812; Archaea.
DR HOGENOM; CLU_054785_5_1_2; -.
DR OMA; VGWAIYP; -.
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.
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; Reference proteome; Retinal protein;
KW Sensory transduction; Transmembrane; Transmembrane helix; Transport.
FT PROPEP 1..6
FT /evidence="ECO:0000250"
FT /id="PRO_0000428846"
FT CHAIN 7..254
FT /note="Bacteriorhodopsin-I"
FT /id="PRO_0000428847"
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 MUTAGEN 126
FT /note="M->A: Large spectral blue shift, but no effect on
FT pumping activity; when associated with A-149 and T-223."
FT /evidence="ECO:0000269|PubMed:23720753"
FT MUTAGEN 149
FT /note="S->A: Large spectral blue shift, but no effect on
FT pumping activity; when associated with A-126 and T-223."
FT /evidence="ECO:0000269|PubMed:23720753"
FT MUTAGEN 223
FT /note="A->T: Large spectral blue shift, but no effect on
FT pumping activity; when associated with A-126 and A-149."
FT /evidence="ECO:0000269|PubMed:23720753"
FT STRAND 13..15
FT /evidence="ECO:0007829|PDB:4QI1"
FT HELIX 17..38
FT /evidence="ECO:0007829|PDB:4QI1"
FT HELIX 44..68
FT /evidence="ECO:0007829|PDB:4QI1"
FT TURN 69..72
FT /evidence="ECO:0007829|PDB:4QI1"
FT STRAND 73..77
FT /evidence="ECO:0007829|PDB:4QI1"
FT STRAND 83..87
FT /evidence="ECO:0007829|PDB:4QI1"
FT HELIX 89..109
FT /evidence="ECO:0007829|PDB:4QI1"
FT HELIX 113..135
FT /evidence="ECO:0007829|PDB:4QI1"
FT HELIX 139..168
FT /evidence="ECO:0007829|PDB:4QI1"
FT HELIX 173..199
FT /evidence="ECO:0007829|PDB:4QI1"
FT TURN 201..204
FT /evidence="ECO:0007829|PDB:4QI1"
FT HELIX 209..232
FT /evidence="ECO:0007829|PDB:4QI1"
FT HELIX 235..237
FT /evidence="ECO:0007829|PDB:4QI1"
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
