ID   EFTU_TOBAC              Reviewed;         478 AA.
AC   P68158; P41342;
DT   25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Elongation factor Tu, chloroplastic;
DE            Short=EF-Tu;
DE   Flags: Precursor;
GN   Name=TUFA;
OS   Nicotiana tabacum (Common tobacco).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=4097;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=cv. NK 326;
RX   PubMed=8278500; DOI=10.1104/pp.101.1.333;
RA   Ursin V.M., Becker C.K., Shewmaker C.K.;
RT   "Cloning and nucleotide sequence of a tobacco chloroplast translational
RT   elongation factor, EF-Tu.";
RL   Plant Physiol. 101:333-334(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; M94204; AAA18546.1; -; Unassigned_DNA.
DR   PIR; JQ2240; JQ2240.
DR   PIR; S39153; S39153.
DR   RefSeq; XP_016478946.1; XM_016623460.1.
DR   AlphaFoldDB; P68158; -.
DR   SMR; P68158; -.
DR   STRING; 4097.P68158; -.
DR   PRIDE; P68158; -.
DR   GeneID; 107800308; -.
DR   KEGG; nta:107800308; -.
DR   OMA; TTHIEYE; -.
DR   OrthoDB; 491836at2759; -.
DR   Proteomes; UP000084051; 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..69
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           70..478
FT                   /note="Elongation factor Tu, chloroplastic"
FT                   /id="PRO_0000007460"
FT   DOMAIN          79..283
FT                   /note="tr-type G"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          88..95
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          129..133
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          150..153
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          205..208
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          243..245
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   BINDING         88..95
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         150..154
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         205..208
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   478 AA;  51957 MW;  98116E09E5FAC001 CRC64;
     MASISAATAT SSTKLVSSNS TNPLLPSSTK PSKLILSSSF TPNCSTLFLH SPATPSSTAT
     HRHRRFTVRA ARGKFERKKP HVNIGTIGHV DHGKTTLTAA LTMALASMGN SAPKKYDEID
     AAPEERARGI TINTATVEYE TENRHYAHVD CPGHADYVKN MITGAAQMDG AILVCSGADG
     PMPQTKEHIL LAKQVGVPNM VVFLNKQDQV DDEELLQLVE LEVRELLSSY EFPGDDIPII
     SGSALLALEA LMANPSIKRG ENQWVDKIYE LMDAVDSYIP IPVRQTELPF LMAIEDVFSI
     TGRGTVATGR VERGTVRIGD TVDIVGLKDT RSTTVTGVEM FQKILDEAMA GDNVGLLLRG
     IQKIDIQRGM VLAKPGTITP HTKFEAIVYV LKKEEGGRHS PFFSGYRPQF YMRTTDVTGK
     VTSITTDKGE ESKMVMPGDR VNLVVELIMP VACEQGMRFA IREGGKTVGA GVIQKIIE