ID   EFTU1_SOYBN             Reviewed;         479 AA.
AC   Q43467;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Elongation factor Tu, chloroplastic;
DE            Short=EF-Tu;
DE   Flags: Precursor;
GN   Name=TUFA;
OS   Glycine max (Soybean) (Glycine hispida).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC   Glycine subgen. Soja.
OX   NCBI_TaxID=3847;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Maple Arrow; TISSUE=Leaf;
RA   Bonny C., Stutz E.;
RT   "Soybean (Glycine max l.) nuclear DNA contains four tuf genes conding for
RT   the chloroplast specific translation elongation factor EF-Tu.";
RL   Chimia 47:247-249(1993).
CC   -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-
CC       tRNA to the A-site of ribosomes during protein biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
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; X66062; CAA46864.1; -; Genomic_DNA.
DR   PIR; S21567; S21567.
DR   AlphaFoldDB; Q43467; -.
DR   SMR; Q43467; -.
DR   STRING; 3847.GLYMA06G18640.1; -.
DR   PRIDE; Q43467; -.
DR   ProMEX; Q43467; -.
DR   eggNOG; KOG0460; Eukaryota.
DR   InParanoid; Q43467; -.
DR   Proteomes; UP000008827; Unplaced.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0003746; F:translation elongation factor activity; IBA:GO_Central.
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   3: Inferred from homology;
KW   Chloroplast; Elongation factor; Glycoprotein; GTP-binding;
KW   Nucleotide-binding; Plastid; Protein biosynthesis; Reference proteome;
KW   Transit peptide.
FT   TRANSIT         1..71
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           72..479
FT                   /note="Elongation factor Tu, chloroplastic"
FT                   /id="PRO_0000007458"
FT   DOMAIN          80..284
FT                   /note="tr-type G"
FT   REGION          19..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          89..96
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          130..134
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          151..154
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          206..209
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          244..246
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   BINDING         89..96
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         151..155
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         206..209
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        333
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   479 AA;  52096 MW;  43C97B99EACF4971 CRC64;
     MAVSSATASS KLILLPHASS SSSLNSTPFR SSTTNTHKLT PLSSSFLHPT TVLRRTPSST
     TTPRRTFTVR AARGKFERKK PHVNIGTIGH VDHGKTTLTA ALTMALAALG NSAPKKYDEI
     DAAPEERARG ITINTATVEY ETENRHYAHV DCPGHADYVK NMITGAAQMD GAILVVSGAD
     GPMPQTKEHI ILAKQVGVPN MVVFLNKQDQ VDDEELLQLV EIEVRDLLSS YEFPGDDTPI
     VSGSALLALE ALMANPAIKR GDNEWVDKIF QLMDEVDNYI PIPQRQTDLP FLLAVEDVFS
     ITGRGTVATG RVERGTIKVG ETVDLVGLRE TRNTTVTGVE MFQKILDEAL AGDNVGLLLR
     GVQKTDIQRG MVLAKPGTIT PHTKFSAIVY VLKKEEGGRH SPFFAGYRPQ FYMRTTDVTG
     KVTSIMNDKD EESTMVLPGD RVKMVVELIV PVACEQGMRF AIREGGKTVG AGVIQSIIE