Legends: 1, SITE Primary proton acceptor; 2, SITE Responsible for spectral tuning; 3, SITE Primary proton donor; 4, N6-(retinylidene)lysine. {ECO:0000250}; 5, MUTAGEN I->V: No effect. {ECO:0000269|PubMed:12682005}; 6, MUTAGEN D->N: Changes in the pH-induced shift. {ECO:0000269|PubMed:12821661}; 7, MUTAGEN Q->L: Absorbs green light; faster photocycle. {ECO:0000269|PubMed:12682005}; 8, MUTAGEN E->Q: Changes in the photocycle. {ECO:0000269|PubMed:12821661}; 9, SIGNAL {ECO:0000255}; 10, TRANSMEM Helical. {ECO:0000255}; 11, ipat:BACTERIAL_OPSIN_1 [T]; 12, HELIX {ECO:0000244|PDB:4KNF}; 13, TURN {ECO:0000244|PDB:4KNF}; 14, STRAND {ECO:0000244|PDB:4KLY}; 15, HELIX {ECO:0000244|PDB:4KLY}.
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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 02-NOV-2016, entry version 77.
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
CC than energy harvesting function, based on light-induced opening of
CC proton channels, to modulate cell physiology depending on light
CC intensity variations. Could be, therefore, a sensory rhodopsin,
CC potentially associated with a transducer component.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000305}.
CC -!- PTM: Contains one covalently linked retinal chromophore.
CC {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
CC bacterium was collected. Transport occurs only at pHs above 7 and
CC is unidirectional.
CC -!- SIMILARITY: Belongs to the archaeal/bacterial/fungal opsin family.
CC {ECO:0000305}.
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 ProteinModelPortal; Q9AFF7; -.
DR SMR; Q9AFF7; -.
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 GO; GO:0018298; P:protein-chromophore linkage; IEA:UniProtKB-KW.
DR GO; GO:0015992; P:proton transport; 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;
KW Retinal protein; Sensory transduction; Signal; Transmembrane;
KW Transmembrane helix; Transport.
FT SIGNAL 1 18 {ECO:0000255}.
FT CHAIN 19 251 Blue-light absorbing proteorhodopsin.
FT /FTId=PRO_0000020257.
FT TRANSMEM 30 50 Helical. {ECO:0000255}.
FT TRANSMEM 65 85 Helical. {ECO:0000255}.
FT TRANSMEM 97 117 Helical. {ECO:0000255}.
FT TRANSMEM 120 140 Helical. {ECO:0000255}.
FT TRANSMEM 144 164 Helical. {ECO:0000255}.
FT TRANSMEM 190 210 Helical. {ECO:0000255}.
FT TRANSMEM 223 243 Helical. {ECO:0000255}.
FT SITE 98 98 Primary proton acceptor.
FT SITE 106 106 Responsible for spectral tuning.
FT SITE 109 109 Primary proton donor.
FT MOD_RES 233 233 N6-(retinylidene)lysine. {ECO:0000250}.
FT MUTAGEN 69 69 I->V: No effect.
FT {ECO:0000269|PubMed:12682005}.
FT MUTAGEN 98 98 D->N: Changes in the pH-induced shift.
FT {ECO:0000269|PubMed:12821661}.
FT MUTAGEN 106 106 Q->L: Absorbs green light; faster
FT photocycle.
FT {ECO:0000269|PubMed:12682005}.
FT MUTAGEN 109 109 E->Q: Changes in the photocycle.
FT {ECO:0000269|PubMed:12821661}.
FT HELIX 29 50 {ECO:0000244|PDB:4KNF}.
FT HELIX 51 54 {ECO:0000244|PDB:4KNF}.
FT TURN 57 59 {ECO:0000244|PDB:4KNF}.
FT HELIX 60 87 {ECO:0000244|PDB:4KNF}.
FT HELIX 92 115 {ECO:0000244|PDB:4KNF}.
FT STRAND 117 119 {ECO:0000244|PDB:4KLY}.
FT HELIX 121 143 {ECO:0000244|PDB:4KNF}.
FT HELIX 149 168 {ECO:0000244|PDB:4KNF}.
FT HELIX 171 173 {ECO:0000244|PDB:4KNF}.
FT HELIX 174 177 {ECO:0000244|PDB:4KLY}.
FT HELIX 181 195 {ECO:0000244|PDB:4KNF}.
FT TURN 196 199 {ECO:0000244|PDB:4KNF}.
FT HELIX 200 209 {ECO:0000244|PDB:4KNF}.
FT HELIX 218 232 {ECO:0000244|PDB:4KNF}.
FT HELIX 234 251 {ECO:0000244|PDB:4KNF}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 30 251 ismart:Bac_rhodopsin [T]
FT MYHIT 95 107 ipat:BACTERIAL_OPSIN_1 [T]
FT MYHIT 32 249 ipfam:Bac_rhodopsin [T]
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
//
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