EFTU_ARATH
ID EFTU_ARATH Reviewed; 476 AA.
AC P17745; Q8GTE7;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Elongation factor Tu, chloroplastic;
DE Short=EF-Tu;
DE AltName: Full=Ras-related protein RABE1b;
DE Short=AtRABE1b;
DE AltName: Full=Ras-related protein Rab8D;
DE Short=AtRab8D;
DE Flags: Precursor;
GN Name=TUFA; Synonyms=RAB8D, RABE1B; OrderedLocusNames=At4g20360;
GN ORFNames=F9F13.10;
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 [GENOMIC DNA].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=2314461; DOI=10.1038/344262a0;
RA Baldauf S.L., Palmer J.D.;
RT "Evolutionary transfer of the chloroplast tufA gene to the nucleus.";
RL Nature 344:262-265(1990).
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].
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT "Multidimensional protein identification technology (MudPIT) analysis of
RT ubiquitinated proteins in plants.";
RL Mol. Cell. Proteomics 6:601-610(2007).
RN [6]
RP INTERACTION WITH PI5K2.
RX PubMed=19903693; DOI=10.1242/jcs.053488;
RA Camacho L., Smertenko A.P., Perez-Gomez J., Hussey P.J., Moore I.;
RT "Arabidopsis Rab-E GTPases exhibit a novel interaction with a plasma-
RT membrane phosphatidylinositol-4-phosphate 5-kinase.";
RL J. Cell Sci. 122:4383-4392(2009).
RN [7]
RP INTERACTION WITH APD2.
RC STRAIN=cv. Columbia;
RX PubMed=22897245; DOI=10.1111/j.1744-7909.2012.01152.x;
RA Luo G., Gu H., Liu J., Qu L.-J.;
RT "Four closely-related RING-type E3 ligases, APD1-4, are involved in pollen
RT mitosis II regulation in Arabidopsis.";
RL J. Integr. Plant Biol. 54:814-827(2012).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-94, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22092075; DOI=10.1021/pr200917t;
RA Aryal U.K., Krochko J.E., Ross A.R.;
RT "Identification of phosphoproteins in Arabidopsis thaliana leaves using
RT polyethylene glycol fractionation, immobilized metal-ion affinity
RT chromatography, two-dimensional gel electrophoresis and mass
RT spectrometry.";
RL J. Proteome Res. 11:425-437(2012).
CC -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-
CC tRNA to the A-site of ribosomes during protein biosynthesis.
CC -!- SUBUNIT: Interacts with PI5K2 (PubMed:19903693). Interacts with APD2
CC (PubMed:22897245). {ECO:0000269|PubMed:19903693,
CC ECO:0000269|PubMed:22897245}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A
CC subfamily. {ECO:0000305}.
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DR EMBL; X52256; CAA36498.1; -; Genomic_DNA.
DR EMBL; AL080253; CAB45802.2; -; Genomic_DNA.
DR EMBL; AL161552; CAB79036.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84313.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM67987.1; -; Genomic_DNA.
DR EMBL; AF410329; AAK95315.1; -; mRNA.
DR EMBL; AF419609; AAL31941.1; -; mRNA.
DR EMBL; AY074355; AAL67051.1; -; mRNA.
DR EMBL; BT000687; AAN31832.1; -; mRNA.
DR EMBL; BT000699; AAN31843.1; -; mRNA.
DR EMBL; BT000998; AAN41398.1; -; mRNA.
DR EMBL; BT002642; AAO11558.1; -; mRNA.
DR PIR; S09152; S09152.
DR RefSeq; NP_001329775.1; NM_001341435.1.
DR RefSeq; NP_193769.1; NM_118155.2.
DR AlphaFoldDB; P17745; -.
DR SMR; P17745; -.
DR BioGRID; 13075; 15.
DR IntAct; P17745; 1.
DR MINT; P17745; -.
DR STRING; 3702.AT4G20360.1; -.
DR iPTMnet; P17745; -.
DR MetOSite; P17745; -.
DR SWISS-2DPAGE; P17745; -.
DR PaxDb; P17745; -.
DR PRIDE; P17745; -.
DR ProteomicsDB; 221922; -.
DR EnsemblPlants; AT4G20360.1; AT4G20360.1; AT4G20360.
DR EnsemblPlants; AT4G20360.2; AT4G20360.2; AT4G20360.
DR GeneID; 827784; -.
DR Gramene; AT4G20360.1; AT4G20360.1; AT4G20360.
DR Gramene; AT4G20360.2; AT4G20360.2; AT4G20360.
DR KEGG; ath:AT4G20360; -.
DR Araport; AT4G20360; -.
DR TAIR; locus:2128615; AT4G20360.
DR eggNOG; KOG0460; Eukaryota.
DR HOGENOM; CLU_007265_0_1_1; -.
DR InParanoid; P17745; -.
DR OMA; TTHIEYE; -.
DR OrthoDB; 491836at2759; -.
DR PhylomeDB; P17745; -.
DR PRO; PR:P17745; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; P17745; differential.
DR Genevisible; P17745; AT.
DR GO; GO:0048046; C:apoplast; HDA:TAIR.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0042644; C:chloroplast nucleoid; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0009534; C:chloroplast thylakoid; HDA:TAIR.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0003746; F:translation elongation factor activity; IBA:GO_Central.
DR GO; GO:0009658; P:chloroplast organization; IGI:TAIR.
DR GO; GO:0048366; P:leaf development; IGI:TAIR.
DR GO; GO:0070125; P:mitochondrial translational elongation; IBA:GO_Central.
DR GO; GO:0006414; P:translational elongation; IBA:GO_Central.
DR CDD; cd01884; EF_Tu; 1.
DR CDD; cd03697; EFTU_II; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00118_B; EF_Tu_B; 1.
DR InterPro; IPR041709; EF-Tu_GTP-bd.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR033720; EFTU_2.
DR InterPro; IPR031157; G_TR_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR InterPro; IPR004541; Transl_elong_EFTu/EF1A_bac/org.
DR InterPro; IPR004160; Transl_elong_EFTu/EF1A_C.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR Pfam; PF03143; GTP_EFTU_D3; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF50465; SSF50465; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00485; EF-Tu; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Elongation factor; GTP-binding; Nucleotide-binding;
KW Phosphoprotein; Plastid; Protein biosynthesis; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..67
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 68..476
FT /note="Elongation factor Tu, chloroplastic"
FT /id="PRO_0000007454"
FT DOMAIN 77..281
FT /note="tr-type G"
FT REGION 86..93
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 127..131
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 148..151
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 203..206
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 241..243
FT /note="G5"
FT /evidence="ECO:0000250"
FT BINDING 86..93
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 148..152
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 203..206
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 94
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22092075"
FT CONFLICT 2
FT /note="A -> P (in Ref. 4; AAN31832)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 476 AA; 51630 MW; 6041F540224A1738 CRC64;
MAISAPAACS SSSRILCSYS SPSPSLCPAI STSGKLKTLT LSSSFLPSYS LTTTSASQST
RRSFTVRAAR GKFERKKPHV NIGTIGHVDH GKTTLTAALT MALASIGSSV AKKYDEIDAA
PEERARGITI NTATVEYETE NRHYAHVDCP GHADYVKNMI TGAAQMDGAI LVVSGADGPM
PQTKEHILLA KQVGVPDMVV FLNKEDQVDD AELLELVELE VRELLSSYEF NGDDIPIISG
SALLAVETLT ENPKVKRGDN KWVDKIYELM DAVDDYIPIP QRQTELPFLL AVEDVFSITG
RGTVATGRVE RGTVKVGETV DLVGLRETRS YTVTGVEMFQ KILDEALAGD NVGLLLRGIQ
KADIQRGMVL AKPGSITPHT KFEAIIYVLK KEEGGRHSPF FAGYRPQFYM RTTDVTGKVT
KIMNDKDEES KMVMPGDRVK IVVELIVPVA CEQGMRFAIR EGGKTVGAGV IGTILE
