SR54C_ARATH
ID SR54C_ARATH Reviewed; 564 AA.
AC P37107; O82570;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Signal recognition particle 54 kDa protein, chloroplastic;
DE Short=54 chloroplast protein;
DE Short=54CP;
DE Short=SRP54;
DE Short=cpSRP54;
DE AltName: Full=FFC;
DE Flags: Precursor;
GN Name=FFC; Synonyms=CPSRP54; OrderedLocusNames=At5g03940; ORFNames=F8F6_150;
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].
RC STRAIN=cv. Columbia;
RX PubMed=8408079; DOI=10.1016/s0021-9258(20)80664-4;
RA Franklin A.E., Hoffman N.E.;
RT "Characterization of a chloroplast homologue of the 54-kDa subunit of the
RT signal recognition particle.";
RL J. Biol. Chem. 268:22175-22180(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Amin P., Sy D., Pilgrim M., Parry D.H., Hoffman N.E.;
RT "Isolation of two Arabidopsis mutants in the nuclear gene ffc, encoding the
RT 54 kDa subunit of chloroplast signal recognition particle.";
RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
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 INTERACTION WITH PSBA.
RX PubMed=9927433; DOI=10.1093/emboj/18.3.733;
RA Nilsson R., Brunner J., Hoffman N.E., van Wijk K.J.;
RT "Interactions of ribosome nascent chain complexes of the chloroplast-
RT encoded D1 thylakoid membrane protein with cpSRP54.";
RL EMBO J. 18:733-742(1999).
RN [7]
RP FUNCTION, AND INTERACTION WITH CAO/CPSRP43.
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 [8]
RP FUNCTION, AND INTERACTION WITH CAO/CPSRP43 AND LHCP.
RX PubMed=11356852; DOI=10.1074/jbc.m103470200;
RA Groves M.R., Mant A., Kuhn A., Koch J., Duebel S., Robinson C., Sinning I.;
RT "Functional characterization of recombinant chloroplast signal recognition
RT particle.";
RL J. Biol. Chem. 276:27778-27786(2001).
RN [9]
RP INTERACTION WITH CAO/CPSRP43, AND MUTAGENESIS OF ARG-536; ARG-537; LYS-538;
RP ARG-539 AND LYS-540.
RX PubMed=15632183; DOI=10.1074/jbc.m409992200;
RA Funke S., Knechten T., Ollesch J., Schunemann D.;
RT "A unique sequence motif in the 54-kDa subunit of the chloroplast signal
RT recognition particle mediates binding to the 43-kDa subunit.";
RL J. Biol. Chem. 280:8912-8917(2005).
RN [10]
RP TISSUE SPECIFICITY.
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 [11]
RP FUNCTION, AND INTERACTION WITH CPFTSY.
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 [12]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18633119; DOI=10.1104/pp.108.124545;
RA Rutschow H., Ytterberg A.J., Friso G., Nilsson R., van Wijk K.J.;
RT "Quantitative proteomics of a chloroplast SRP54 sorting mutant and its
RT genetic interactions with CLPC1 in Arabidopsis.";
RL Plant Physiol. 148:156-175(2008).
RN [13]
RP INTERACTION WITH CPFTSY.
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 STRUCTURE BY NMR OF 530-543.
RX PubMed=18586266; DOI=10.1016/j.jmb.2008.05.065;
RA Kathir K.M., Rajalingam D., Sivaraja V., Kight A., Goforth R.L., Yu C.,
RA Henry R., Kumar T.K.;
RT "Assembly of chloroplast signal recognition particle involves structural
RT rearrangement in cpSRP43.";
RL J. Mol. Biol. 381:49-60(2008).
CC -!- FUNCTION: Involved in cotranslational and post-translational sorting of
CC thylakoid proteins. Binds GTP specifically. Activates the GTPase
CC activity of CPFTSY when bound together. Required for light-harvesting
CC chlorophyll a/b-binding protein (LHCP) integration into thylakoids.
CC {ECO:0000269|PubMed:10480939, ECO:0000269|PubMed:11356852,
CC ECO:0000269|PubMed:17475780, ECO:0000269|PubMed:18633119}.
CC -!- SUBUNIT: Component of the cpSRP complex, composed of a FFC/cpSRP54
CC monomer and a CAO/cpSRP43 dimer. Interacts (via C-terminus) with
CC CAO/cpSRP43 and with CPFTSY. Interacts with the third transmembrane
CC domain of LHCP. Interacts with the PSBA/D1 nascent chain, but only when
CC it is attached to the 70S ribosome and if it is shorter than 189 amino
CC acid residues. {ECO:0000269|PubMed:10480939,
CC ECO:0000269|PubMed:11356852, ECO:0000269|PubMed:15632183,
CC ECO:0000269|PubMed:17475780, ECO:0000269|PubMed:19587121,
CC ECO:0000269|PubMed:9927433}.
CC -!- INTERACTION:
CC P37107; O22265: CAO; NbExp=21; IntAct=EBI-780642, EBI-780656;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma.
CC -!- TISSUE SPECIFICITY: Most abundant in green shoot tissue and lower
CC levels seen in the roots and etiolated buds.
CC {ECO:0000269|PubMed:16813577}.
CC -!- DOMAIN: The M-domain stimulates the interaction between CPFTSY and the
CC chloroplast signal recognition particle (cpSRP).
CC -!- DOMAIN: The C-terminal residues (539-564) are required for interaction
CC with CAO/cpSRP43.
CC -!- DISRUPTION PHENOTYPE: Pale green with delayed development.
CC {ECO:0000269|PubMed:18633119}.
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. SRP54 subfamily.
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; Z21970; CAA79981.1; -; mRNA.
DR EMBL; AF092168; AAC64139.1; -; Genomic_DNA.
DR EMBL; AL162873; CAB85514.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90674.1; -; Genomic_DNA.
DR EMBL; AY050999; AAK93676.1; -; mRNA.
DR EMBL; BT000976; AAN41376.1; -; mRNA.
DR PIR; S36637; S36637.
DR RefSeq; NP_196014.1; NM_120476.5.
DR PDB; 2HUG; NMR; -; B=530-543.
DR PDB; 3UI2; X-ray; 3.18 A; B=528-540.
DR PDB; 5L3R; X-ray; 2.50 A; A/C=77-371.
DR PDBsum; 2HUG; -.
DR PDBsum; 3UI2; -.
DR PDBsum; 5L3R; -.
DR AlphaFoldDB; P37107; -.
DR SMR; P37107; -.
DR BioGRID; 15553; 4.
DR DIP; DIP-752N; -.
DR IntAct; P37107; 5.
DR MINT; P37107; -.
DR STRING; 3702.AT5G03940.1; -.
DR TCDB; 3.A.5.1.2; the general secretory pathway (sec) family.
DR iPTMnet; P37107; -.
DR PaxDb; P37107; -.
DR PRIDE; P37107; -.
DR ProteomicsDB; 226862; -.
DR EnsemblPlants; AT5G03940.1; AT5G03940.1; AT5G03940.
DR GeneID; 830273; -.
DR Gramene; AT5G03940.1; AT5G03940.1; AT5G03940.
DR KEGG; ath:AT5G03940; -.
DR Araport; AT5G03940; -.
DR TAIR; locus:2150620; AT5G03940.
DR eggNOG; KOG0780; Eukaryota.
DR HOGENOM; CLU_009301_6_0_1; -.
DR InParanoid; P37107; -.
DR OMA; IDKTMMD; -.
DR OrthoDB; 463152at2759; -.
DR PhylomeDB; P37107; -.
DR BRENDA; 3.6.5.4; 399.
DR EvolutionaryTrace; P37107; -.
DR PRO; PR:P37107; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; P37107; baseline and differential.
DR Genevisible; P37107; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0032991; C:protein-containing complex; IDA:CAFA.
DR GO; GO:0005786; C:signal recognition particle, endoplasmic reticulum targeting; IEA:UniProtKB-KW.
DR GO; GO:0008312; F:7S RNA binding; IEA:InterPro.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
DR GO; GO:0070208; P:protein heterotrimerization; IMP:CAFA.
DR GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; IEA:InterPro.
DR Gene3D; 1.10.260.30; -; 1.
DR Gene3D; 1.20.120.140; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00306; SRP54; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR036891; Signal_recog_part_SRP54_M_sf.
DR InterPro; IPR013822; Signal_recog_particl_SRP54_hlx.
DR InterPro; IPR004125; Signal_recog_particle_SRP54_M.
DR InterPro; IPR004780; SRP.
DR InterPro; IPR022941; SRP54.
DR InterPro; IPR000897; SRP54_GTPase_dom.
DR InterPro; IPR042101; SRP54_N_sf.
DR PANTHER; PTHR11564; PTHR11564; 1.
DR Pfam; PF00448; SRP54; 1.
DR Pfam; PF02881; SRP54_N; 1.
DR Pfam; PF02978; SRP_SPB; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00962; SRP54; 1.
DR SMART; SM00963; SRP54_N; 1.
DR SUPFAM; SSF47446; SSF47446; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00959; ffh; 1.
DR PROSITE; PS00300; SRP54; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chloroplast; GTP-binding; Nucleotide-binding; Plastid;
KW Reference proteome; Ribonucleoprotein; RNA-binding;
KW Signal recognition particle; Transit peptide.
FT TRANSIT 1..75
FT /note="Chloroplast"
FT CHAIN 76..564
FT /note="Signal recognition particle 54 kDa protein,
FT chloroplastic"
FT /id="PRO_0000033232"
FT REGION 76..370
FT /note="G-domain"
FT REGION 371..564
FT /note="M-domain"
FT REGION 460..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 525..564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..482
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 183..190
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 265..269
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 323..326
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MUTAGEN 536
FT /note="R->G,K: Strongly reduced binding to CAO/cpSRP43."
FT /evidence="ECO:0000269|PubMed:15632183"
FT MUTAGEN 537
FT /note="R->G,Q,K,N: Loss of binding to CAO/cpSRP43."
FT /evidence="ECO:0000269|PubMed:15632183"
FT MUTAGEN 538..540
FT /note="Missing: No effect on binding to CAO/cpSRP43."
FT MUTAGEN 538
FT /note="K->M: No effect on binding to CAO/cpSRP43."
FT /evidence="ECO:0000269|PubMed:15632183"
FT MUTAGEN 539
FT /note="R->G,K: Reduced binding to CAO/cpSRP43."
FT /evidence="ECO:0000269|PubMed:15632183"
FT MUTAGEN 540
FT /note="K->M: No effect on binding to CAO/cpSRP43."
FT /evidence="ECO:0000269|PubMed:15632183"
FT CONFLICT 76
FT /note="E -> V (in Ref. 2; AAC64139)"
FT /evidence="ECO:0000305"
FT HELIX 104..116
FT /evidence="ECO:0007829|PDB:5L3R"
FT HELIX 121..138
FT /evidence="ECO:0007829|PDB:5L3R"
FT HELIX 146..161
FT /evidence="ECO:0007829|PDB:5L3R"
FT STRAND 173..175
FT /evidence="ECO:0007829|PDB:5L3R"
FT STRAND 177..182
FT /evidence="ECO:0007829|PDB:5L3R"
FT HELIX 189..201
FT /evidence="ECO:0007829|PDB:5L3R"
FT TURN 202..204
FT /evidence="ECO:0007829|PDB:5L3R"
FT STRAND 207..212
FT /evidence="ECO:0007829|PDB:5L3R"
FT HELIX 219..230
FT /evidence="ECO:0007829|PDB:5L3R"
FT HELIX 243..256
FT /evidence="ECO:0007829|PDB:5L3R"
FT STRAND 260..266
FT /evidence="ECO:0007829|PDB:5L3R"
FT HELIX 274..287
FT /evidence="ECO:0007829|PDB:5L3R"
FT STRAND 290..297
FT /evidence="ECO:0007829|PDB:5L3R"
FT HELIX 304..314
FT /evidence="ECO:0007829|PDB:5L3R"
FT STRAND 318..323
FT /evidence="ECO:0007829|PDB:5L3R"
FT HELIX 333..341
FT /evidence="ECO:0007829|PDB:5L3R"
FT STRAND 345..349
FT /evidence="ECO:0007829|PDB:5L3R"
FT STRAND 351..353
FT /evidence="ECO:0007829|PDB:5L3R"
FT STRAND 357..359
FT /evidence="ECO:0007829|PDB:5L3R"
FT HELIX 362..369
FT /evidence="ECO:0007829|PDB:5L3R"
FT STRAND 534..538
FT /evidence="ECO:0007829|PDB:3UI2"
SQ SEQUENCE 564 AA; 61232 MW; 423F7285FB9063E4 CRC64;
MEALQFSSVN RVPCTLSCTG NRRIKAAFSS AFTGGTINSA SLSSSRNLST REIWSWVKSK
TVVGHGRYRR SQVRAEMFGQ LTGGLEAAWS KLKGEEVLTK DNIAEPMRDI RRALLEADVS
LPVVRRFVQS VSDQAVGMGV IRGVKPDQQL VKIVHDELVK LMGGEVSELQ FAKSGPTVIL
LAGLQGVGKT TVCAKLACYL KKQGKSCMLI AGDVYRPAAI DQLVILGEQV GVPVYTAGTD
VKPADIAKQG LKEAKKNNVD VVIMDTAGRL QIDKGMMDEL KDVKKFLNPT EVLLVVDAMT
GQEAAALVTT FNVEIGITGA ILTKLDGDSR GGAALSVKEV SGKPIKLVGR GERMEDLEPF
YPDRMAGRIL GMGDVLSFVE KATEVMRQED AEDLQKKIMS AKFDFNDFLK QTRAVAKMGS
MTRVLGMIPG MGKVSPAQIR EAEKNLLVME AMIEVMTPEE RERPELLAES PERRKRIAKD
SGKTEQQVSA LVAQIFQMRV KMKNLMGVME GGSIPALSGL EDALKAEQKA PPGTARRKRK
ADSRKKFVES ASSKPGPRGF GSGN
