PRRB_PRB02
ID PRRB_PRB02 Reviewed; 251 AA.
AC Q9AFF7;
DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2003, sequence version 2.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Blue-light absorbing proteorhodopsin;
DE Short=BPR;
DE Flags: Precursor;
OS Gamma-proteobacterium Hot 75m4.
OC Bacteria; Proteobacteria; Gammaproteobacteria.
OX NCBI_TaxID=245185;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11459054; DOI=10.1038/35081051;
RA Beja O., Spudich E.N., Spudich J.L., Leclerc M., DeLong E.F.;
RT "Proteorhodopsin phototrophy in the ocean.";
RL Nature 411:786-789(2001).
RN [2]
RP ENVIRONMENTAL DISTRIBUTION, AND MUTAGENESIS OF ILE-69 AND GLN-106.
RX PubMed=12682005; DOI=10.1093/emboj/cdg183;
RA Man D., Wang W., Sabehi G., Aravind L., Post A.F., Massana R.,
RA Spudich E.N., Spudich J.L., Beja O.;
RT "Diversification and spectral tuning in marine proteorhodopsins.";
RL EMBO J. 22:1725-1731(2003).
RN [3]
RP COMPARISON WITH PHOTOCHEMICAL CYCLE OF GREEN PROTEORHODOPSIN, AND
RP MUTAGENESIS OF ASP-98 AND GLU-109.
RX PubMed=12821661; DOI=10.1074/jbc.m305716200;
RA Wang W.W., Sineshchekov O.A., Spudich E.N., Spudich J.L.;
RT "Spectroscopic and photochemical characterization of a deep ocean
RT proteorhodopsin.";
RL J. Biol. Chem. 278:33985-33991(2003).
CC -!- FUNCTION: Light-driven proton pump. May have a regulatory rather than
CC energy harvesting function, based on light-induced opening of proton
CC channels, to modulate cell physiology depending on light intensity
CC variations. Could be, therefore, a sensory rhodopsin, potentially
CC associated with a transducer component.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- PTM: Contains one covalently linked retinal chromophore. {ECO:0000250}.
CC -!- MISCELLANEOUS: Presents a much slower photocycle than that of the
CC green-absorbing proteorhodopsin, probably an adaptation to the
CC intensity of solar illumination at a depth of 75m, where this bacterium
CC was collected. Transport occurs only at pHs above 7 and is
CC unidirectional.
CC -!- SIMILARITY: Belongs to the archaeal/bacterial/fungal opsin family.
CC {ECO:0000305}.
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DR EMBL; AF349981; AAK30179.1; -; Genomic_DNA.
DR PDB; 4KLY; X-ray; 2.70 A; A/B/C/D/E=1-251.
DR PDB; 4KNF; X-ray; 2.60 A; A/B/C/D/E=1-251.
DR PDBsum; 4KLY; -.
DR PDBsum; 4KNF; -.
DR AlphaFoldDB; Q9AFF7; -.
DR SMR; Q9AFF7; -.
DR TCDB; 3.E.1.6.12; the ion-translocating microbial rhodopsin (mr) family.
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:0010461; F:light-activated 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; IPR017402; Proteorhodopsin.
DR InterPro; IPR018229; Rhodopsin_retinal_BS.
DR Pfam; PF01036; Bac_rhodopsin; 1.
DR PIRSF; PIRSF038142; Rhodopsin_bac_prd; 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 3D-structure; Cell membrane; Chromophore; Hydrogen ion transport;
KW Ion transport; Membrane; Photoreceptor protein; Receptor; Retinal protein;
KW Sensory transduction; Signal; Transmembrane; Transmembrane helix;
KW Transport.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..251
FT /note="Blue-light absorbing proteorhodopsin"
FT /id="PRO_0000020257"
FT TRANSMEM 30..50
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 65..85
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 97..117
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 120..140
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 144..164
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 190..210
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 223..243
FT /note="Helical"
FT /evidence="ECO:0000255"
FT SITE 98
FT /note="Primary proton acceptor"
FT SITE 106
FT /note="Responsible for spectral tuning"
FT SITE 109
FT /note="Primary proton donor"
FT MOD_RES 233
FT /note="N6-(retinylidene)lysine"
FT /evidence="ECO:0000250"
FT MUTAGEN 69
FT /note="I->V: No effect."
FT /evidence="ECO:0000269|PubMed:12682005"
FT MUTAGEN 98
FT /note="D->N: Changes in the pH-induced shift."
FT /evidence="ECO:0000269|PubMed:12821661"
FT MUTAGEN 106
FT /note="Q->L: Absorbs green light; faster photocycle."
FT /evidence="ECO:0000269|PubMed:12682005"
FT MUTAGEN 109
FT /note="E->Q: Changes in the photocycle."
FT /evidence="ECO:0000269|PubMed:12821661"
FT HELIX 29..50
FT /evidence="ECO:0007829|PDB:4KNF"
FT HELIX 51..54
FT /evidence="ECO:0007829|PDB:4KNF"
FT TURN 57..59
FT /evidence="ECO:0007829|PDB:4KNF"
FT HELIX 60..87
FT /evidence="ECO:0007829|PDB:4KNF"
FT HELIX 92..115
FT /evidence="ECO:0007829|PDB:4KNF"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:4KLY"
FT HELIX 121..143
FT /evidence="ECO:0007829|PDB:4KNF"
FT HELIX 149..168
FT /evidence="ECO:0007829|PDB:4KNF"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:4KNF"
FT HELIX 174..177
FT /evidence="ECO:0007829|PDB:4KLY"
FT HELIX 181..195
FT /evidence="ECO:0007829|PDB:4KNF"
FT TURN 196..199
FT /evidence="ECO:0007829|PDB:4KNF"
FT HELIX 200..209
FT /evidence="ECO:0007829|PDB:4KNF"
FT HELIX 218..232
FT /evidence="ECO:0007829|PDB:4KNF"
FT HELIX 234..251
FT /evidence="ECO:0007829|PDB:4KNF"
SQ SEQUENCE 251 AA; 26796 MW; 6A0A3FAB9DEDFAD9 CRC64;
MGKLLLILGS AIALPSFAAA GGDLDISDTV GVSFWLVTAG MLAATVFFFV ERDQVSAKWK
TSLTVSGLIT GIAFWHYLYM RGVWIDTGDT PTVFRYIDWL LTVPLQVVEF YLILAACTSV
AASLFKKLLA GSLVMLGAGF AGEAGLAPVL PAFIIGMAGW LYMIYELYMG EGKAAVSTAS
PAVNSAYNAM MMIIVVGWAI YPAGYAAGYL MGGEGVYASN LNLIYNLADF VNKILFGLII
WNVAVKESSN A
