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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
 
 
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