PETS_ARATH
ID PETS_ARATH Reviewed; 953 AA.
AC Q9SZD6; F4JMU5; Q0WVD2; Q0WWF9; Q5QEA9; Q93ZG6;
DT 26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 175.
DE RecName: Full=Polyprotein of EF-Ts, chloroplastic {ECO:0000303|PubMed:15548736};
DE Short=150 kDa pro-protein {ECO:0000305|PubMed:16980539};
DE AltName: Full=Protein EMBRYO DEFECTIVE 2726 {ECO:0000303|PubMed:15266054, ECO:0000303|PubMed:31334862};
DE Contains:
DE RecName: Full=Plastid-specific ribosomal protein-7, chloroplastic {ECO:0000303|PubMed:15548736};
DE Contains:
DE RecName: Full=Elongation factor Ts, chloroplastic {ECO:0000303|PubMed:15548736};
DE Short=EF-Ts {ECO:0000303|PubMed:15548736};
DE Flags: Precursor;
GN Name=PETs {ECO:0000303|PubMed:15548736};
GN Synonyms=EFTS {ECO:0000303|PubMed:15548736},
GN EMB2726 {ECO:0000303|PubMed:15266054, ECO:0000303|PubMed:31334862},
GN PSRP-7 {ECO:0000303|PubMed:15548736};
GN OrderedLocusNames=At4g29060 {ECO:0000312|Araport:AT4G29060};
GN ORFNames=F19B15.90 {ECO:0000312|EMBL:CAB43920.1};
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] (ISOFORM 2), ALTERNATIVE SPLICING, AND GENE
RP FAMILY.
RC STRAIN=cv. Columbia;
RX PubMed=15548736; DOI=10.1105/tpc.104.026708;
RA Beligni M.V., Yamaguchi K., Mayfield S.P.;
RT "Chloroplast elongation factor ts pro-protein is an evolutionarily
RT conserved fusion with the s1 domain-containing plastid-specific ribosomal
RT protein-7.";
RL Plant Cell 16:3357-3369(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION [LARGE SCALE ANALYSIS], AND DISRUPTION PHENOTYPE [LARGE SCALE
RP ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=15266054; DOI=10.1104/pp.104.045179;
RA Tzafrir I., Pena-Muralla R., Dickerman A., Berg M., Rogers R., Hutchens S.,
RA Sweeney T.C., McElver J., Aux G., Patton D., Meinke D.;
RT "Identification of genes required for embryo development in Arabidopsis.";
RL Plant Physiol. 135:1206-1220(2004).
RN [7]
RP PTM, IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=16980539; DOI=10.1105/tpc.106.044594;
RA Sjoegren L.L.E., Stanne T.M., Zheng B., Sutinen S., Clarke A.K.;
RT "Structural and functional insights into the chloroplast ATP-dependent Clp
RT protease in Arabidopsis.";
RL Plant Cell 18:2635-2649(2006).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=21139083; DOI=10.1104/pp.110.168120;
RA Bryant N., Lloyd J., Sweeney C., Myouga F., Meinke D.;
RT "Identification of nuclear genes encoding chloroplast-localized proteins
RT required for embryo development in Arabidopsis.";
RL Plant Physiol. 155:1678-1689(2011).
RN [9]
RP FUNCTION [LARGE SCALE ANALYSIS], AND DISRUPTION PHENOTYPE [LARGE SCALE
RP ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=31334862; DOI=10.1111/nph.16071;
RA Meinke D.W.;
RT "Genome-wide identification of EMBRYO-DEFECTIVE (EMB) genes required for
RT growth and development in Arabidopsis.";
RL New Phytol. 226:306-325(2020).
CC -!- FUNCTION: [Elongation factor Ts, chloroplastic]: Associates with the
CC EF-Tu.GDP complex and induces the exchange of GDP to GTP (By
CC similarity). It remains bound to the aminoacyl-tRNA.EF-Tu.GTP complex
CC up to the GTP hydrolysis stage on the ribosome (By similarity).
CC {ECO:0000250|UniProtKB:A8J637}.
CC -!- FUNCTION: [Plastid-specific ribosomal protein-7, chloroplastic]: Binds
CC to psbD and psbA 5'-untranslated regions (UTRs) in vitro.
CC {ECO:0000250|UniProtKB:A8J637}.
CC -!- SUBUNIT: [Plastid-specific ribosomal protein-7, chloroplastic]:
CC Component of the chloroplast ribosome 30S and 70S subunits, as well as
CC polysomes. {ECO:0000250|UniProtKB:A8J637}.
CC -!- SUBUNIT: [Polyprotein of EF-Ts, chloroplastic]: Component of the
CC chloroplast ribosome 70S subunit, and at low levels, present in
CC polysomes. {ECO:0000250|UniProtKB:A8J637}.
CC -!- SUBUNIT: [Elongation factor Ts, chloroplastic]: Associates transiently
CC with chloroplast polysomes. {ECO:0000250|UniProtKB:A8J637}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:16980539, ECO:0000269|PubMed:21139083}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9SZD6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9SZD6-2; Sequence=VSP_060533;
CC Name=3;
CC IsoId=Q9SZD6-3; Sequence=VSP_060531, VSP_060532;
CC -!- PTM: [Polyprotein of EF-Ts, chloroplastic]: Probable substrate for the
CC chloroplast protease ClpP6. {ECO:0000269|PubMed:16980539}.
CC -!- DISRUPTION PHENOTYPE: Defective embryo arrested at globular stage.
CC {ECO:0000250|UniProtKB:A8J637}.
CC -!- SIMILARITY: [Elongation factor Ts, chloroplastic]: Belongs to the EF-Ts
CC family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Seed defective Arabidopsis mutants;
CC URL="http://seedgenes.org/MutantList";
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DR EMBL; AY661462; AAU93601.1; -; mRNA.
DR EMBL; AL078470; CAB43920.1; -; Genomic_DNA.
DR EMBL; AL161574; CAB79664.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85580.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85581.1; -; Genomic_DNA.
DR EMBL; AY056792; AAL10483.1; -; mRNA.
DR EMBL; AY057550; AAL09789.1; -; mRNA.
DR EMBL; AY074270; AAL66967.1; -; mRNA.
DR EMBL; AY096654; AAM20288.1; -; mRNA.
DR EMBL; AK226393; BAE98539.1; -; mRNA.
DR EMBL; AK226820; BAE98916.1; -; mRNA.
DR PIR; T08961; T08961.
DR RefSeq; NP_001031743.1; NM_001036666.1. [Q9SZD6-2]
DR RefSeq; NP_567820.1; NM_119050.3. [Q9SZD6-1]
DR AlphaFoldDB; Q9SZD6; -.
DR SMR; Q9SZD6; -.
DR IntAct; Q9SZD6; 1.
DR STRING; 3702.AT4G29060.1; -.
DR iPTMnet; Q9SZD6; -.
DR MetOSite; Q9SZD6; -.
DR PaxDb; Q9SZD6; -.
DR PRIDE; Q9SZD6; -.
DR ProMEX; Q9SZD6; -.
DR ProteomicsDB; 191473; -. [Q9SZD6-1]
DR ProteomicsDB; 204388; -.
DR EnsemblPlants; AT4G29060.1; AT4G29060.1; AT4G29060. [Q9SZD6-1]
DR EnsemblPlants; AT4G29060.2; AT4G29060.2; AT4G29060. [Q9SZD6-2]
DR GeneID; 829027; -.
DR Gramene; AT4G29060.1; AT4G29060.1; AT4G29060. [Q9SZD6-1]
DR Gramene; AT4G29060.2; AT4G29060.2; AT4G29060. [Q9SZD6-2]
DR KEGG; ath:AT4G29060; -.
DR Araport; AT4G29060; -.
DR TAIR; locus:2119946; AT4G29060.
DR eggNOG; KOG1071; Eukaryota.
DR HOGENOM; CLU_012395_0_0_1; -.
DR InParanoid; Q9SZD6; -.
DR OMA; MQVAAYP; -.
DR OrthoDB; 1048278at2759; -.
DR PhylomeDB; Q9SZD6; -.
DR PRO; PR:Q9SZD6; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SZD6; baseline and differential.
DR GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0043253; C:chloroplast ribosome; ISS:UniProtKB.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-UniRule.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:1905538; F:polysome binding; ISS:UniProtKB.
DR GO; GO:0003746; F:translation elongation factor activity; IBA:GO_Central.
DR GO; GO:0061770; F:translation elongation factor binding; ISS:UniProtKB.
DR GO; GO:0006414; P:translational elongation; IBA:GO_Central.
DR Gene3D; 2.40.50.140; -; 2.
DR Gene3D; 3.30.479.20; -; 2.
DR HAMAP; MF_00050; EF_Ts; 2.
DR InterPro; IPR036402; EF-Ts_dimer_sf.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR022967; S1_dom.
DR InterPro; IPR003029; S1_domain.
DR InterPro; IPR001816; Transl_elong_EFTs/EF1B.
DR InterPro; IPR014039; Transl_elong_EFTs/EF1B_dimer.
DR InterPro; IPR018101; Transl_elong_Ts_CS.
DR InterPro; IPR009060; UBA-like_sf.
DR PANTHER; PTHR11741; PTHR11741; 3.
DR Pfam; PF00889; EF_TS; 2.
DR Pfam; PF00575; S1; 2.
DR SMART; SM00316; S1; 2.
DR SUPFAM; SSF46934; SSF46934; 2.
DR SUPFAM; SSF50249; SSF50249; 2.
DR SUPFAM; SSF54713; SSF54713; 2.
DR TIGRFAMs; TIGR00116; tsf; 3.
DR PROSITE; PS01126; EF_TS_1; 2.
DR PROSITE; PS01127; EF_TS_2; 1.
DR PROSITE; PS50126; S1; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Chloroplast; Elongation factor; Plastid;
KW Protein biosynthesis; Reference proteome; Repeat; Transit peptide.
FT TRANSIT 1..80
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 81..953
FT /note="Polyprotein of EF-Ts, chloroplastic"
FT /id="PRO_0000449222"
FT CHAIN 81..518
FT /note="Plastid-specific ribosomal protein-7, chloroplastic"
FT /id="PRO_0000449223"
FT CHAIN 519..953
FT /note="Elongation factor Ts, chloroplastic"
FT /id="PRO_0000449224"
FT DOMAIN 136..205
FT /note="S1 motif 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT DOMAIN 248..318
FT /note="S1 motif 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT REGION 93..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 201..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 359..514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 731..750
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..234
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..431
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..469
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 473..487
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..514
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 732..746
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 450..455
FT /note="EEEIVE -> KLTKNH (in isoform 3)"
FT /id="VSP_060531"
FT VAR_SEQ 456..953
FT /note="Missing (in isoform 3)"
FT /id="VSP_060532"
FT VAR_SEQ 617..860
FT /note="Missing (in isoform 2)"
FT /id="VSP_060533"
FT CONFLICT 583
FT /note="D -> V (in Ref. 5; BAE98539)"
FT /evidence="ECO:0000305"
FT CONFLICT Q9SZD6-2:616
FT /note="V -> VA (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 953 AA; 103782 MW; 5CA860B9F7A4A7CE CRC64;
MATITPSSIS NAWLIPGASF TVKKSDCSIK CSFSRKAGKQ ILSSTQRLVL PLSTSLRLFP
THGRQFVLHP HRRATGTDVV AAVEEQDSTP VVAEDKETVA SEKSDAPAPT SQSRGTARPG
RKSEMPAVKN EELVPGATFT GKVRAIQPFG AFVDFGAFTD GLVHVSQLSD NFVKDVSSVV
TIGQEVKVRL VEADIESKRI SLTMRENDDP PKRQSGGSDK PRSGGKRDGS KGGGQRKGEG
FNSKFAKGQM LDGVVKNLTR SGAFITIGEG EEGFLPTAEE ADDGIGSMMM GGSSLQAGQE
VKVRVLRIAR GRVTLTMKEE DDGKFDETTT QGVVHTATNP FMLAFRKNEE IAAFLDKREE
EAEKPPVETP VEPEAEASVT SAEVEESVCV PAEVTSEEVP SSETPKVVEE EVIATKAEDD
SPEKEEQTET LAAAAEAEEV VPPIPETKSE EEIVENSIPP NSATDEVSSP EALASEEVEK
EQVVAETPVD EVKTPAPVVT EASSEESGNT ATAESIKGIS PALVKQLREE TGAGMMDCKN
ALSESEGDMV KAQEYLRKKG LASADKKASR ATSEGRIGAY IHDSRIGVLL EVNCETDFVS
RGDIFKELVD DLAMQVAACP QVEYLVTEDV SEEIVKKEKE IEMQKEDLLS KPEQIREKIV
DGRIKKRLDS LALLEQPYIK DDKVIVKDLV KQRIATIGEN IKVKRFVRYT LGEGLEKKSQ
DFAAEVAAQT AAKPKAKEEP KAEEAKEAVA SPPTTVVSAA LVKQLREETG AGMMDCKKAL
AATGGDLEKA QEFLRKKGLS SADKKSSRLA SEGRIGSYIH DSRIGVLIEV NCETDFVGRS
EKFKELVDDL AMQAVANPQV QYVSIEDIPE EIKQKEKEIE MQREDLLSKP ENIREKIVEG
RISKRLGEWA LLEQPYIKDD SVLVKDLVKQ TVATLGENIK VRRFVKFTLG EDN
