FRP_SYNY3
ID FRP_SYNY3 Reviewed; 109 AA.
AC P74103;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2015, sequence version 2.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=Fluorescence recovery protein {ECO:0000303|PubMed:20534537};
DE Short=FRP {ECO:0000303|PubMed:20534537};
GN Name=frp; OrderedLocusNames=slr1964;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708 {ECO:0000312|Proteomes:UP000001425};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
RN [2]
RP FUNCTION, INTERACTION WITH OCP, SUBUNIT, SUBCELLULAR LOCATION, INDUCTION,
RP AND DISRUPTION PHENOTYPE.
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=20534537; DOI=10.1073/pnas.1002912107;
RA Boulay C., Wilson A., D'Haene S., Kirilovsky D.;
RT "Identification of a protein required for recovery of full antenna capacity
RT in OCP-related photoprotective mechanism in cyanobacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:11620-11625(2010).
RN [3]
RP FUNCTION, AND SUBUNIT.
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=21764991; DOI=10.1105/tpc.111.086884;
RA Gwizdala M., Wilson A., Kirilovsky D.;
RT "In vitro reconstitution of the cyanobacterial photoprotective mechanism
RT mediated by the orange carotenoid protein in Synechocystis PCC 6803.";
RL Plant Cell 23:2631-2643(2011).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 2-109, FUNCTION, INTERACTION WITH
RP OCP, SUBUNIT, AND MUTAGENESIS OF TRP-9; TRP-50; HIS-53; ASP-54 AND ARG-60.
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=23716688; DOI=10.1073/pnas.1303673110;
RA Sutter M., Wilson A., Leverenz R.L., Lopez-Igual R., Thurotte A.,
RA Salmeen A.E., Kirilovsky D., Kerfeld C.A.;
RT "Crystal structure of the FRP and identification of the active site for
RT modulation of OCP-mediated photoprotection in cyanobacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:10022-10027(2013).
CC -!- FUNCTION: Destabilizes orange carotenoid protein-R form (OCP-R), the
CC FRP-OCP interaction accelerates the OCP-R to OCP-O conversion
CC (PubMed:20534537, PubMed:23716688). Increases fluorescence recovery
CC following non-photochemical quenching (NPQ) by OCP, most probably by
CC destabilizing OCP-R binding to the phycobilisome core
CC (PubMed:21764991). {ECO:0000269|PubMed:20534537,
CC ECO:0000269|PubMed:21764991, ECO:0000269|PubMed:23716688}.
CC -!- SUBUNIT: Probably a dimer, interacts with the C-terminal domain of OCP-
CC R (PubMed:23716688). {ECO:0000269|PubMed:20534537,
CC ECO:0000269|PubMed:23716688, ECO:0000305|PubMed:21764991}.
CC -!- INTERACTION:
CC P74103; P74102: slr1963; NbExp=2; IntAct=EBI-1618115, EBI-1618104;
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane
CC {ECO:0000269|PubMed:20534537}; Peripheral membrane protein
CC {ECO:0000269|PubMed:20534537}; Cytoplasmic side
CC {ECO:0000305|PubMed:20534537}. Note=Very tightly associated with the
CC membrane. {ECO:0000269|PubMed:20534537}.
CC -!- INDUCTION: Transcribed from its own promoter, it may also be
CC cotranscribed with upstream ocp. {ECO:0000269|PubMed:20534537}.
CC -!- DISRUPTION PHENOTYPE: Decreased fluorescence recovery after non-
CC photochemical quenching (NPQ). {ECO:0000269|PubMed:20534537}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA18189.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305|PubMed:20534537};
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; BA000022; BAA18189.1; ALT_INIT; Genomic_DNA.
DR PIR; S75628; S75628.
DR PDB; 4JDQ; X-ray; 3.52 A; A/B/C/D/E/F=2-109.
DR PDB; 4JDX; X-ray; 2.50 A; A/B/C/D/E/F=2-109.
DR PDBsum; 4JDQ; -.
DR PDBsum; 4JDX; -.
DR AlphaFoldDB; P74103; -.
DR SASBDB; P74103; -.
DR SMR; P74103; -.
DR DIP; DIP-59344N; -.
DR IntAct; P74103; 3.
DR STRING; 1148.1653274; -.
DR PaxDb; P74103; -.
DR EnsemblBacteria; BAA18189; BAA18189; BAA18189.
DR KEGG; syn:slr1964; -.
DR eggNOG; ENOG5032S2M; Bacteria.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0031676; C:plasma membrane-derived thylakoid membrane; IEA:UniProtKB-SubCell.
DR InterPro; IPR041601; FRP.
DR Pfam; PF18032; FRP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Membrane; Reference proteome; Thylakoid.
FT CHAIN 1..109
FT /note="Fluorescence recovery protein"
FT /id="PRO_0000434475"
FT MUTAGEN 9
FT /note="W->L: Wild-type role in conversion of OCP-R to OCP-
FT O."
FT /evidence="ECO:0000269|PubMed:23716688"
FT MUTAGEN 50
FT /note="W->F: About 75% conversion of OCP-R to OCP-O."
FT /evidence="ECO:0000269|PubMed:23716688"
FT MUTAGEN 50
FT /note="W->L: About 25% conversion of OCP-R to OCP-O."
FT /evidence="ECO:0000269|PubMed:23716688"
FT MUTAGEN 53
FT /note="H->L: About 50% conversion of OCP-R to OCP-O."
FT /evidence="ECO:0000269|PubMed:23716688"
FT MUTAGEN 54
FT /note="D->E: About 75% conversion of OCP-R to OCP-O."
FT /evidence="ECO:0000269|PubMed:23716688"
FT MUTAGEN 54
FT /note="D->L: About 25% conversion of OCP-R to OCP-O."
FT /evidence="ECO:0000269|PubMed:23716688"
FT MUTAGEN 60
FT /note="R->K,L: Almost no conversion of OCP-R to OCP-O."
FT /evidence="ECO:0000269|PubMed:23716688"
FT HELIX 11..41
FT /evidence="ECO:0007829|PDB:4JDX"
FT HELIX 47..64
FT /evidence="ECO:0007829|PDB:4JDX"
FT TURN 71..73
FT /evidence="ECO:0007829|PDB:4JDX"
FT HELIX 74..83
FT /evidence="ECO:0007829|PDB:4JDX"
FT HELIX 89..92
FT /evidence="ECO:0007829|PDB:4JDX"
FT HELIX 97..108
FT /evidence="ECO:0007829|PDB:4JDX"
SQ SEQUENCE 109 AA; 12370 MW; 92B9948CECC838C8 CRC64;
MLQTAEAPWS QAETQSAHAL FRKAYQRELD GLLATVQAQA SQITQIDDLW KLHDFLSAKR
HEIDGKYDDR QSVIIFVFAQ LLKEGLVQAE ELTFLAADKQ SKIKALARL
