ID   EFTU_CHAVU              Reviewed;         419 AA.
AC   Q1ACI3;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=Elongation factor Tu, chloroplastic;
DE            Short=EF-Tu;
GN   Name=tufA;
OS   Chara vulgaris (Common stonewort).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Charophyceae; Charales; Characeae;
OC   Chara.
OX   NCBI_TaxID=55564;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16611644; DOI=10.1093/molbev/msk018;
RA   Turmel M., Otis C., Lemieux C.;
RT   "The chloroplast genome sequence of Chara vulgaris sheds new light into the
RT   closest green algal relatives of land plants.";
RL   Mol. Biol. Evol. 23:1324-1338(2006).
CC   -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-
CC       tRNA to the A-site of ribosomes during protein biosynthesis.
CC       {ECO:0000250}.
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; DQ229107; ABA61966.1; -; Genomic_DNA.
DR   RefSeq; YP_635764.1; NC_008097.1.
DR   AlphaFoldDB; Q1ACI3; -.
DR   SMR; Q1ACI3; -.
DR   PRIDE; Q1ACI3; -.
DR   GeneID; 4100337; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
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.
FT   CHAIN           1..419
FT                   /note="Elongation factor Tu, chloroplastic"
FT                   /id="PRO_0000275376"
FT   DOMAIN          10..214
FT                   /note="tr-type G"
FT   REGION          19..26
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          60..64
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          81..84
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          136..139
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          174..176
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   BINDING         19..26
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         81..85
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         136..139
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   419 AA;  46449 MW;  7A805A60DB78625D CRC64;
     MAQEVFQRTK PHVNIGTIGH VDHGKTTLTA AITMTLAVNS TCTPKKYDEI DAAPEERARG
     ITINTAHVEY ETASRHYAHV DCPGHADYIK NMITGAAQMD GAILVVSAAD GPMPQTKEHI
     LLAKQVGVPS IVVFLNKEDQ VDDEEILQLV DLEVRESLIN YEFPGDKVPV VAGSALMALQ
     ALTEKPNTLR GENKWVDKIY ELMDAVDSYI PTPKRDIEKP FLMPIEDVFS IQGRGTVATG
     RIERGILKLG DIVELIGLNE KIRSTVVTGL EMFRRLLEQG FAGENIGVLL RGIEKKDIER
     GMVIAQPGTI EPHTRFEAQV YILRKEEGGR HSPFFAGYRP QFFVRTADVT GVIEAFEYDN
     GDKTRMVMPG DRVKMIVNLI CPIAIEKKMR FAIREGGRTI GAGVVLQILD STQLKSKNK