ID   EFTU2_SOYBN             Reviewed;         479 AA.
AC   P46280;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Elongation factor Tu, chloroplastic;
DE            Short=EF-Tu;
DE   Flags: Precursor;
GN   Name=TUFB1;
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. Ceresia;
RA   Maurer F., Murone M., Stutz E.;
RT   "The tuf gene family of soybean: structure and differential expression.";
RL   Plant Sci. 117:83-92(1996).
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; X89058; CAA61444.1; -; Genomic_DNA.
DR   PIR; S60659; S60659.
DR   AlphaFoldDB; P46280; -.
DR   SMR; P46280; -.
DR   STRING; 3847.GLYMA05G02670.2; -.
DR   PRIDE; P46280; -.
DR   eggNOG; KOG0460; Eukaryota.
DR   InParanoid; P46280; -.
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; GTP-binding; Nucleotide-binding; Plastid;
KW   Protein biosynthesis; Reference proteome; Transit peptide.
FT   TRANSIT         1..70
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           71..479
FT                   /note="Elongation factor Tu, chloroplastic"
FT                   /id="PRO_0000007459"
FT   DOMAIN          80..284
FT                   /note="tr-type G"
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"
SQ   SEQUENCE   479 AA;  52509 MW;  CD65F0E262BBD77B CRC64;
     MAISWAAATT SKLAYPPHVH FSPSPSSNYL FLKTHKPSAT HLSSSFIHPT TILHLAAANT
     TTRRRSFTVR AARGKFERKK PHVNIGTIGH VDHGKTTLTA ALTMALASLG NSAPKKYDEI
     DAAPEERARG ITINTATVEY ETENRHYAHV DCPGHADYVK NMITGAAQMD GAILVVSGAD
     GPMPQTKEHI LLAKQVGVPN IVVFLNKQDQ VDDEELLQLV ELEVRELLSK YEFPGDDVPI
     ISGSALLSLE ALMANPSIKR GENQWVDKIY ELMEAVDDYI PIPQRQTELP FLLAIEDVFT
     ITGRGTVATG RVERGTIRVG ETVDIVGVKD TRNTTVTGVE MFQKILDEAL AGDNVGLLLR
     GIQKTDIQRG MVLAKPGTIT PHTKFSAIVY VLKKEEGGRH SPFFSGYRPQ FYMRTTDVTG
     KVTEIMNDKD EESKMVMPGD RVKLVVELIV PVACEQGMRF AIREGGKTVG AGVIQSIIE