CFTSY_ARATH
ID CFTSY_ARATH Reviewed; 366 AA.
AC O80842; F4IH43; Q9SWS7; Q9XFR1;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Cell division protein FtsY homolog, chloroplastic;
DE AltName: Full=Chloroplast SRP receptor homolog, alpha subunit CpFtsY;
DE AltName: Full=Fused signal recognition particle receptor;
DE Flags: Precursor;
GN Name=CPFTSY; Synonyms=FTSY; OrderedLocusNames=At2g45770; ORFNames=F4I18.25;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=10214972; DOI=10.1016/s0014-5793(99)00305-1;
RA Kogata N., Nishio K., Hirohashi T., Kikuchi S., Nakai M.;
RT "Involvement of a chloroplast homologue of the signal recognition particle
RT receptor protein, FtsY, in protein targeting to thylakoids.";
RL FEBS Lett. 447:329-333(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Wassilewskija;
RA Peterson E.C., Henry R.L.;
RT "CPFTSY signal recognition particle receptor homolog.";
RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=10480939; DOI=10.1074/jbc.274.38.27219;
RA Tu C.J., Schuenemann D., Hoffman N.E.;
RT "Chloroplast FtsY, chloroplast signal recognition particle, and GTP are
RT required to reconstitute the soluble phase of light-harvesting chlorophyll
RT protein transport into thylakoid membranes.";
RL J. Biol. Chem. 274:27219-27224(1999).
RN [7]
RP FUNCTION.
RX PubMed=12105232; DOI=10.1074/jbc.m206192200;
RA Yuan J., Kight A., Goforth R.L., Moore M., Peterson E.C., Sakon J.,
RA Henry R.;
RT "ATP stimulates signal recognition particle (SRP)/FtsY-supported protein
RT integration in chloroplasts.";
RL J. Biol. Chem. 277:32400-32404(2002).
RN [8]
RP INTERACTION WITH ALB3.
RX PubMed=14517205; DOI=10.1083/jcb.200307067;
RA Moore M., Goforth R.L., Mori H., Henry R.;
RT "Functional interaction of chloroplast SRP/FtsY with the ALB3 translocase
RT in thylakoids: substrate not required.";
RL J. Cell Biol. 162:1245-1254(2003).
RN [9]
RP MUTAGENESIS OF GLY-344, TISSUE SPECIFICITY, INDUCTION BY IRON, AND
RP SUBCELLULAR LOCATION.
RX PubMed=16813577; DOI=10.1111/j.1365-313x.2006.02803.x;
RA Durrett T.P., Connolly E.L., Rogers E.E.;
RT "Arabidopsis cpFtsY mutants exhibit pleiotropic defects including an
RT inability to increase iron deficiency-inducible root Fe(III) chelate
RT reductase activity.";
RL Plant J. 47:467-479(2006).
RN [10]
RP FUNCTION, MUTAGENESIS OF ASP-321, AND INTERACTION WITH CPSRP54/FFC.
RX PubMed=17475780; DOI=10.1091/mbc.e07-01-0037;
RA Jaru-Ampornpan P., Chandrasekar S., Shan S.O.;
RT "Efficient interaction between two GTPases allows the chloroplast SRP
RT pathway to bypass the requirement for an SRP RNA.";
RL Mol. Biol. Cell 18:2636-2645(2007).
RN [11]
RP FUNCTION, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE, INDUCTION, TISSUE
RP SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=18764927; DOI=10.1111/j.1365-313x.2008.03659.x;
RA Asakura Y., Kikuchi S., Nakai M.;
RT "Non-identical contributions of two membrane-bound cpSRP components, cpFtsY
RT and Alb3, to thylakoid biogenesis.";
RL Plant J. 56:1007-1017(2008).
RN [12]
RP FUNCTION, DOMAIN, MUTAGENESIS OF 48-PHE-PHE-49; ARG-51; LEU-52; ARG-54 AND
RP ILE-56, AND STRUCTURE BY NMR OF 39-56.
RX PubMed=19293157; DOI=10.1074/jbc.m900775200;
RA Marty N.J., Rajalingam D., Kight A.D., Lewis N.E., Fologea D., Kumar T.K.,
RA Henry R.L., Goforth R.L.;
RT "The membrane-binding motif of the chloroplast signal recognition particle
RT receptor (cpFtsY) regulates GTPase activity.";
RL J. Biol. Chem. 284:14891-14903(2009).
RN [13]
RP INTERACTION WITH CPSRP54/FFC, AND MUTAGENESIS OF PHE-71 AND GLY-326.
RX PubMed=19587121; DOI=10.1091/mbc.e08-10-0989;
RA Jaru-Ampornpan P., Nguyen T.X., Shan S.O.;
RT "A distinct mechanism to achieve efficient signal recognition particle
RT (SRP)-SRP receptor interaction by the chloroplast srp pathway.";
RL Mol. Biol. Cell 20:3965-3973(2009).
RN [14]
RP 3D-STRUCTURE MODELING.
RX PubMed=20682346; DOI=10.1016/j.jsb.2010.07.013;
RA Yang M.J., Pang X.Q., Zhang X., Han K.L.;
RT "Molecular dynamics simulation reveals preorganization of the chloroplast
RT FtsY towards complex formation induced by GTP binding.";
RL J. Struct. Biol. 173:57-66(2011).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 65-366.
RX PubMed=18022392; DOI=10.1016/j.febslet.2007.11.024;
RA Stengel K.F., Holdermann I., Wild K., Sinning I.;
RT "The structure of the chloroplast signal recognition particle (SRP)
RT receptor reveals mechanistic details of SRP GTPase activation and a
RT conserved membrane targeting site.";
RL FEBS Lett. 581:5671-5676(2007).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 41-366, AND MUTAGENESIS OF PHE-71
RP AND PHE-109.
RX PubMed=18035371; DOI=10.1016/j.jmb.2007.09.061;
RA Chandrasekar S., Chartron J., Jaru-Ampornpan P., Shan S.O.;
RT "Structure of the chloroplast signal recognition particle (cpSRP) receptor:
RT domain arrangement modulates SRP-receptor interaction.";
RL J. Mol. Biol. 375:425-436(2008).
CC -!- FUNCTION: Signal recognition particle receptor protein. Binds GTP
CC specifically. The GTPase activity is inhibited by the N-terminus of the
CC protein until binding to the thylakoid membrane. Activates the GTPase
CC activity of FFC/cpSRP54 when bound to the cpSRP complex. Required for
CC light-harvesting chlorophyll a/b-binding protein (LHCP) integration
CC into thylakoids. Might be also functionally linked to the Sec
CC translocation machinery. {ECO:0000269|PubMed:10214972,
CC ECO:0000269|PubMed:10480939, ECO:0000269|PubMed:12105232,
CC ECO:0000269|PubMed:17475780, ECO:0000269|PubMed:18764927,
CC ECO:0000269|PubMed:19293157}.
CC -!- SUBUNIT: Monomer. Interacts with FFC/cpSRP54, a component of the cpSRP
CC complex, composed of a FFC/cpSRP54 monomer and a CAO/cpSRP43 dimer. The
CC complex with FFC/cpSRP54 is formed when both proteins are bound with
CC GTP. {ECO:0000269|PubMed:10480939, ECO:0000269|PubMed:14517205,
CC ECO:0000269|PubMed:17475780, ECO:0000269|PubMed:19587121}.
CC -!- INTERACTION:
CC O80842; Q8LBP4: ALB3; NbExp=2; IntAct=EBI-2353373, EBI-1806831;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma. Plastid, chloroplast
CC thylakoid membrane; Peripheral membrane protein; Stromal side. Note=The
CC membrane-binding domain is capable of partial insertion into the lipid
CC bilayer.
CC -!- TISSUE SPECIFICITY: Expressed in green tissues. Low levels in roots and
CC seeds. {ECO:0000269|PubMed:16813577, ECO:0000269|PubMed:18764927}.
CC -!- DEVELOPMENTAL STAGE: Peak of expression 20 days after germination.
CC {ECO:0000269|PubMed:18764927}.
CC -!- INDUCTION: Not induced by light or iron. {ECO:0000269|PubMed:16813577,
CC ECO:0000269|PubMed:18764927}.
CC -!- DOMAIN: The N-terminal domain (39-56) is necessary and sufficient for
CC thylakoid binding. {ECO:0000269|PubMed:19293157}.
CC -!- DISRUPTION PHENOTYPE: Seedling lethal. {ECO:0000269|PubMed:18764927}.
CC -!- MISCELLANEOUS: Unlike eukaryotic or prokaryotic signal recognition
CC particle (SRP), the chloroplast SRP from higher plants lacks an SRP-RNA
CC component. It targets both chloroplast-encoded and nucleus-encoded
CC substrates to the thylakoid membrane, post-translationally for the
CC nucleus-encoded proteins and co-translationally for the chloroplast-
CC encoded proteins.
CC -!- SIMILARITY: Belongs to the GTP-binding SRP family. {ECO:0000305}.
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DR EMBL; AJ010820; CAB40382.1; -; mRNA.
DR EMBL; AF120112; AAD47910.1; -; mRNA.
DR EMBL; AC004665; AAC28547.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC10599.1; -; Genomic_DNA.
DR EMBL; AF360125; AAK25835.1; -; mRNA.
DR EMBL; AY051026; AAK93703.1; -; mRNA.
DR PIR; T02470; T02470.
DR PIR; T52612; T52612.
DR RefSeq; NP_566056.1; NM_130140.3.
DR PDB; 2OG2; X-ray; 2.00 A; A=41-366.
DR PDB; 3B9Q; X-ray; 1.75 A; A=65-366.
DR PDB; 5L3R; X-ray; 2.50 A; B/D=80-366.
DR PDBsum; 2OG2; -.
DR PDBsum; 3B9Q; -.
DR PDBsum; 5L3R; -.
DR AlphaFoldDB; O80842; -.
DR SMR; O80842; -.
DR BioGRID; 4521; 5.
DR IntAct; O80842; 6.
DR MINT; O80842; -.
DR STRING; 3702.AT2G45770.2; -.
DR TCDB; 3.A.5.1.2; the general secretory pathway (sec) family.
DR PaxDb; O80842; -.
DR PRIDE; O80842; -.
DR ProteomicsDB; 220474; -.
DR EnsemblPlants; AT2G45770.1; AT2G45770.1; AT2G45770.
DR GeneID; 819185; -.
DR Gramene; AT2G45770.1; AT2G45770.1; AT2G45770.
DR KEGG; ath:AT2G45770; -.
DR Araport; AT2G45770; -.
DR eggNOG; KOG0780; Eukaryota.
DR InParanoid; O80842; -.
DR OMA; GISDQFQ; -.
DR OrthoDB; 804839at2759; -.
DR PhylomeDB; O80842; -.
DR EvolutionaryTrace; O80842; -.
DR PRO; PR:O80842; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O80842; baseline and differential.
DR GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005047; F:signal recognition particle binding; IBA:GO_Central.
DR GO; GO:0006605; P:protein targeting; IBA:GO_Central.
DR GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; IEA:InterPro.
DR Gene3D; 1.20.120.140; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR013822; Signal_recog_particl_SRP54_hlx.
DR InterPro; IPR004390; SR_rcpt_FtsY.
DR InterPro; IPR036225; SRP/SRP_N.
DR InterPro; IPR000897; SRP54_GTPase_dom.
DR InterPro; IPR042101; SRP54_N_sf.
DR Pfam; PF00448; SRP54; 1.
DR Pfam; PF02881; SRP54_N; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00962; SRP54; 1.
DR SMART; SM00963; SRP54_N; 1.
DR SUPFAM; SSF47364; SSF47364; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00064; ftsY; 1.
DR PROSITE; PS00300; SRP54; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chloroplast; GTP-binding; Membrane; Metal-binding;
KW Nucleotide-binding; Plastid; Receptor; Reference proteome; Thylakoid;
KW Transit peptide.
FT TRANSIT 1..40
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 41..366
FT /note="Cell division protein FtsY homolog, chloroplastic"
FT /id="PRO_0000413416"
FT BINDING 171..178
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 254..258
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 318..321
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MUTAGEN 48
FT /note="F->A: Reduced binding to the thylakoid and 80%
FT reduction of LHCP integration in thylakoids, but no effect
FT on GTP binding. Reduced binding to the thylakoid and 80%
FT reduction of LHCP integration in thylakoids; when
FT associated with A-49."
FT MUTAGEN 48
FT /note="F->G,E,Q,K: Severe reduction of LHCP integration in
FT thylakoids."
FT MUTAGEN 48
FT /note="F->L,V,Y,W: No or limited reduction of LHCP
FT integration in thylakoids."
FT MUTAGEN 49
FT /note="F->A: Reduced binding to the thylakoid and 40%
FT reduction of LHCP integration in thylakoids. Reduced
FT binding to the thylakoid and 80% reduction of LHCP
FT integration in thylakoids; when associated with A-48."
FT MUTAGEN 51
FT /note="R->A: Reduced binding to the thylakoid and LHCP
FT integration in thylakoids; when associated with A-54."
FT /evidence="ECO:0000269|PubMed:19293157"
FT MUTAGEN 52
FT /note="L->A,Q: Reduced binding to the thylakoid and LHCP
FT integration in thylakoids."
FT /evidence="ECO:0000269|PubMed:19293157"
FT MUTAGEN 54
FT /note="R->A: Reduced binding to the thylakoid and LHCP
FT integration in thylakoids; when associated with A-51."
FT /evidence="ECO:0000269|PubMed:19293157"
FT MUTAGEN 56
FT /note="I->A: Reduced binding to the thylakoid and LHCP
FT integration in thylakoids."
FT /evidence="ECO:0000269|PubMed:19293157"
FT MUTAGEN 71
FT /note="F->V,A,L: Reduced interaction with FFC, but no
FT effect on the basal GTPase activity."
FT /evidence="ECO:0000269|PubMed:18035371,
FT ECO:0000269|PubMed:19587121"
FT MUTAGEN 109
FT /note="F->V: Reduced interaction with FFC."
FT /evidence="ECO:0000269|PubMed:18035371"
FT MUTAGEN 321
FT /note="D->N: Loss of GTP binding specificity."
FT /evidence="ECO:0000269|PubMed:17475780"
FT MUTAGEN 326
FT /note="G->W: Reduced interaction with FFC, but no effect on
FT the basal GTPase activity."
FT /evidence="ECO:0000269|PubMed:19587121"
FT MUTAGEN 344
FT /note="G->D: In frd4-2; chlorotic and reduction in
FT thylakoid membrane content and stacking."
FT /evidence="ECO:0000269|PubMed:16813577"
FT CONFLICT 8
FT /note="L -> F (in Ref. 2 and 15; AAD47910)"
FT /evidence="ECO:0000305"
FT HELIX 66..70
FT /evidence="ECO:0007829|PDB:3B9Q"
FT HELIX 72..78
FT /evidence="ECO:0007829|PDB:3B9Q"
FT HELIX 80..85
FT /evidence="ECO:0007829|PDB:3B9Q"
FT HELIX 90..92
FT /evidence="ECO:0007829|PDB:3B9Q"
FT HELIX 93..106
FT /evidence="ECO:0007829|PDB:3B9Q"
FT HELIX 111..126
FT /evidence="ECO:0007829|PDB:3B9Q"
FT HELIX 133..148
FT /evidence="ECO:0007829|PDB:3B9Q"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:3B9Q"
FT STRAND 165..170
FT /evidence="ECO:0007829|PDB:3B9Q"
FT HELIX 177..190
FT /evidence="ECO:0007829|PDB:3B9Q"
FT STRAND 195..198
FT /evidence="ECO:0007829|PDB:3B9Q"
FT HELIX 205..218
FT /evidence="ECO:0007829|PDB:3B9Q"
FT STRAND 221..223
FT /evidence="ECO:0007829|PDB:3B9Q"
FT STRAND 226..229
FT /evidence="ECO:0007829|PDB:2OG2"
FT HELIX 232..245
FT /evidence="ECO:0007829|PDB:3B9Q"
FT STRAND 249..253
FT /evidence="ECO:0007829|PDB:3B9Q"
FT HELIX 263..277
FT /evidence="ECO:0007829|PDB:3B9Q"
FT STRAND 285..292
FT /evidence="ECO:0007829|PDB:3B9Q"
FT HELIX 293..299
FT /evidence="ECO:0007829|PDB:3B9Q"
FT HELIX 300..309
FT /evidence="ECO:0007829|PDB:3B9Q"
FT STRAND 314..318
FT /evidence="ECO:0007829|PDB:3B9Q"
FT HELIX 327..336
FT /evidence="ECO:0007829|PDB:3B9Q"
FT STRAND 340..344
FT /evidence="ECO:0007829|PDB:3B9Q"
FT STRAND 346..348
FT /evidence="ECO:0007829|PDB:3B9Q"
FT HELIX 349..351
FT /evidence="ECO:0007829|PDB:3B9Q"
FT STRAND 352..354
FT /evidence="ECO:0007829|PDB:3B9Q"
FT HELIX 357..365
FT /evidence="ECO:0007829|PDB:3B9Q"
SQ SEQUENCE 366 AA; 39679 MW; 8986F431A6A3BE12 CRC64;
MATSSAHLSF LAGRISPFSS ERIGLFPLRG EFRPRMTRFR CSAGPSGFFT RLGRLIKEKA
KSDVEKVFSG FSKTRENLAV IDELLLFWNL AETDRVLDEL EEALLVSDFG PKITVRIVER
LREDIMSGKL KSGSEIKDAL KESVLEMLAK KNSKTELQLG FRKPAVIMIV GVNGGGKTTS
LGKLAHRLKN EGTKVLMAAG DTFRAAASDQ LEIWAERTGC EIVVAEGDKA KAATVLSKAV
KRGKEEGYDV VLCDTSGRLH TNYSLMEELI ACKKAVGKIV SGAPNEILLV LDGNTGLNML
PQAREFNEVV GITGLILTKL DGSARGGCVV SVVEELGIPV KFIGVGEAVE DLQPFDPEAF
VNAIFS
