PRRG_PRB01
ID PRRG_PRB01 Reviewed; 249 AA.
AC Q9F7P4;
DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Green-light absorbing proteorhodopsin;
DE Short=GPR;
DE Flags: Precursor;
OS Gamma-proteobacterium EBAC31A08.
OC Bacteria; Proteobacteria; Gammaproteobacteria; environmental samples.
OX NCBI_TaxID=133804;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10988064; DOI=10.1126/science.289.5486.1902;
RA Beja O., Aravind L., Koonin E.V., Suzuki M.T., Hadd A., Nguyen L.P.,
RA Jovanovich S.B., Gates C.M., Feldman R.A., Spudich J.L., Spudich E.N.,
RA DeLong E.F.;
RT "Bacterial rhodopsin: evidence for a new type of phototrophy in the sea.";
RL Science 289:1902-1906(2000).
RN [2]
RP CHARACTERIZATION OF PROTON RELEASE CYCLE, AND MUTAGENESIS OF CYS-107;
RP CYS-156 AND CYS-175.
RX PubMed=11943070; DOI=10.1186/1472-6793-2-5;
RA Krebs R.A., Alexiev U., Partha R., DeVita A., Braiman M.S.;
RT "Detection of fast light-activated H+ release and M intermediate formation
RT from proteorhodopsin.";
RL BMC Physiol. 2:5-5(2002).
RN [3]
RP CHARACTERIZATION OF PHOTOCHEMICAL CYCLE, AND MUTAGENESIS OF ASP-97 AND
RP GLU-108.
RX PubMed=11969395; DOI=10.1021/bi025563x;
RA Dioumaev A.K., Brown L.S., Shih J., Spudich E.N., Spudich J.L., Lanyi J.K.;
RT "Proton transfers in the photochemical reaction cycle of proteorhodopsin.";
RL Biochemistry 41:5348-5358(2002).
RN [4]
RP CHARACTERIZATION OF PHOTOCHEMICAL CYCLE.
RX PubMed=12547799; DOI=10.1016/s0006-3495(03)74934-0;
RA Varo G., Brown L.S., Lakatos M., Lanyi J.K.;
RT "Characterization of the photochemical reaction cycle of proteorhodopsin.";
RL Biophys. J. 84:1202-1207(2003).
RN [5]
RP COMPARISON WITH PHOTOCHEMICAL CYCLE OF BLUE PROTEORHODOPSIN.
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).
RN [6]
RP PRELIMINARY CHARACTERIZATION OF PUMP VECTORIALITY.
RX PubMed=12206764; DOI=10.1016/s0022-2836(02)00696-4;
RA Friedrich T., Geibel S., Kalmbach R., Chizhov I., Ataka K., Heberle J.,
RA Engelhard M., Bamberg E.;
RT "Proteorhodopsin is a light-driven proton pump with variable
RT vectoriality.";
RL J. Mol. Biol. 321:821-838(2002).
RN [7]
RP CHARACTERIZATION OF PUMP VECTORIALITY.
RX PubMed=12719254; DOI=10.1016/s0006-3495(03)70049-6;
RA Lakatos M., Lanyi J.K., Szakacs J., Varo G.;
RT "The photochemical reaction cycle of proteorhodopsin at low pH.";
RL Biophys. J. 84:3252-3256(2003).
RN [8]
RP CHARACTERIZATION OF PUMP VECTORIALITY.
RX PubMed=12767242; DOI=10.1021/bi034253r;
RA Dioumaev A.K., Wang J.M., Balint Z., Varo G., Lanyi J.K.;
RT "Proton transport by proteorhodopsin requires that the retinal Schiff base
RT counterion Asp-97 be anionic.";
RL Biochemistry 42:6582-6587(2003).
RN [9]
RP ENVIRONMENTAL DISTRIBUTION.
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 [10]
RP ENVIRONMENTAL DISTRIBUTION, AND MUTAGENESIS OF VAL-68 AND LEU-105.
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).
CC -!- FUNCTION: Light-driven proton pump that generates photothrophic energy.
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: It presents a fast proton release and an alkaliphilic
CC photocycle, consistent with its marine origin and the near-surface
CC environment where this bacterium was collected. Transport occurs only
CC at pHs above 7 and is unidirectional.
CC -!- MISCELLANEOUS: Mutagenesis experiments that removed all the Cys
CC residues of GPR show that at least one of the Cys residues in the
CC protein is probably modified post-translationally.
CC -!- SIMILARITY: Belongs to the archaeal/bacterial/fungal opsin family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF279106; AAG10475.1; -; Genomic_DNA.
DR PDB; 2L6X; NMR; -; A=19-249.
DR PDB; 5ABB; EM; 8.00 A; Z=19-83.
DR PDBsum; 2L6X; -.
DR PDBsum; 5ABB; -.
DR AlphaFoldDB; Q9F7P4; -.
DR BMRB; Q9F7P4; -.
DR SMR; Q9F7P4; -.
DR TCDB; 3.E.1.6.1; 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 PANTHER; PTHR28286; PTHR28286; 1.
DR Pfam; PF01036; Bac_rhodopsin; 1.
DR PIRSF; PIRSF038142; Rhodopsin_bac_prd; 1.
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..17
FT /evidence="ECO:0000255"
FT CHAIN 18..249
FT /note="Green-light absorbing proteorhodopsin"
FT /id="PRO_0000020256"
FT TRANSMEM 30..49
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 62..84
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 99..121
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 128..147
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 151..168
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 189..211
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 221..243
FT /note="Helical"
FT /evidence="ECO:0000255"
FT SITE 97
FT /note="Primary proton acceptor"
FT SITE 105
FT /note="Responsible for spectral tuning"
FT SITE 108
FT /note="Primary proton donor"
FT MOD_RES 231
FT /note="N6-(retinylidene)lysine"
FT /evidence="ECO:0000250"
FT MUTAGEN 68
FT /note="V->I: No effect."
FT /evidence="ECO:0000269|PubMed:12682005"
FT MUTAGEN 97
FT /note="D->E: Slight changes in spectral shifts; more rapid
FT formation of the M intermediate."
FT /evidence="ECO:0000269|PubMed:11969395"
FT MUTAGEN 97
FT /note="D->N: Elimination of the pH-induced shift and
FT stabilization of the absorption spectrum in the acidic
FT form."
FT /evidence="ECO:0000269|PubMed:11969395"
FT MUTAGEN 105
FT /note="L->Q: Absorbs blue light; slower photocycle."
FT /evidence="ECO:0000269|PubMed:12682005"
FT MUTAGEN 107
FT /note="C->S: Lower molecular weight on SDS gels potentially
FT due to failure to bind either sugar or lipid; when
FT associated with S-156 and S-175."
FT /evidence="ECO:0000269|PubMed:11943070"
FT MUTAGEN 108
FT /note="E->Q: Changes in the photocycle."
FT /evidence="ECO:0000269|PubMed:11969395"
FT MUTAGEN 156
FT /note="C->S: Lower molecular weight on SDS gels potentially
FT due to failure to bind either sugar or lipid; when
FT associated with S-107 and S-175."
FT /evidence="ECO:0000269|PubMed:11943070"
FT MUTAGEN 175
FT /note="C->S: Lower molecular weight on SDS gels potentially
FT due to failure to bind either sugar or lipid; when
FT associated with S-107 and S-156."
FT /evidence="ECO:0000269|PubMed:11943070"
FT HELIX 25..49
FT /evidence="ECO:0007829|PDB:2L6X"
FT HELIX 50..52
FT /evidence="ECO:0007829|PDB:2L6X"
FT HELIX 59..86
FT /evidence="ECO:0007829|PDB:2L6X"
FT HELIX 91..114
FT /evidence="ECO:0007829|PDB:2L6X"
FT TURN 115..117
FT /evidence="ECO:0007829|PDB:2L6X"
FT HELIX 122..143
FT /evidence="ECO:0007829|PDB:2L6X"
FT TURN 148..150
FT /evidence="ECO:0007829|PDB:2L6X"
FT HELIX 151..166
FT /evidence="ECO:0007829|PDB:2L6X"
FT TURN 171..173
FT /evidence="ECO:0007829|PDB:2L6X"
FT STRAND 174..177
FT /evidence="ECO:0007829|PDB:2L6X"
FT HELIX 180..208
FT /evidence="ECO:0007829|PDB:2L6X"
FT STRAND 210..213
FT /evidence="ECO:0007829|PDB:2L6X"
FT HELIX 216..229
FT /evidence="ECO:0007829|PDB:2L6X"
FT HELIX 232..247
FT /evidence="ECO:0007829|PDB:2L6X"
SQ SEQUENCE 249 AA; 27251 MW; 5D6B54FB36C237EA CRC64;
MKLLLILGSV IALPTFAAGG GDLDASDYTG VSFWLVTAAL LASTVFFFVE RDRVSAKWKT
SLTVSGLVTG IAFWHYMYMR GVWIETGDSP TVFRYIDWLL TVPLLICEFY LILAAATNVA
GSLFKKLLVG SLVMLVFGYM GEAGIMAAWP AFIIGCLAWV YMIYELWAGE GKSACNTASP
AVQSAYNTMM YIIIFGWAIY PVGYFTGYLM GDGGSALNLN LIYNLADFVN KILFGLIIWN
VAVKESSNA
