ID   EFTU_CHAGL              Reviewed;         406 AA.
AC   Q8M9W7;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Elongation factor Tu, chloroplastic;
DE            Short=EF-Tu;
GN   Name=tufA;
OS   Chaetosphaeridium globosum (Charophycean green alga) (Herposteiron
OS   globosum).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Coleochaetophyceae; Coleochaetales;
OC   Chaetosphaeridiaceae; Chaetosphaeridium.
OX   NCBI_TaxID=96477;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12161560; DOI=10.1073/pnas.162203299;
RA   Turmel M., Otis C., Lemieux C.;
RT   "The chloroplast and mitochondrial genome sequences of the charophyte
RT   Chaetosphaeridium globosum: insights into the timing of the events that
RT   restructured organelle DNAs within the green algal lineage that led to land
RT   plants.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:11275-11280(2002).
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   -!- SUBUNIT: Monomer. {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:0000255|PROSITE-ProRule:PRU01059}.
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DR   EMBL; AF494278; AAM96580.1; -; Genomic_DNA.
DR   RefSeq; NP_683822.1; NC_004115.1.
DR   AlphaFoldDB; Q8M9W7; -.
DR   SMR; Q8M9W7; -.
DR   GeneID; 860736; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-KW.
DR   CDD; cd01884; EF_Tu; 1.
DR   CDD; cd03697; EFTU_II; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR041709; EF-Tu_GTP-bd.
DR   InterPro; IPR004161; EFTu-like_2.
DR   InterPro; IPR033720; EFTU_2.
DR   InterPro; IPR027417; P-loop_NTPase.
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; 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   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..406
FT                   /note="Elongation factor Tu, chloroplastic"
FT                   /id="PRO_0000337593"
FT   DOMAIN          8..210
FT                   /note="tr-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT   BINDING         17..24
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         77..81
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         132..135
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   406 AA;  45950 MW;  7EB56F1605CEE8F1 CRC64;
     MNIFRDKKTH INIATIGHFN HGKTTLSAAI AMTLANKKYR LDKKSIKVTL EEKNQGIGIY
     THHFQYETTL RHYSHTDCPG HTDYINNMIA GISQVDSTIL VVSAVDGSMS QTKEHLLIAK
     LLGISSFIVF INKEDQLDDD KFVYLVQKEI SQFLMSHGFQ TNKIPIVSGS ALLALETLIQ
     QPNVLRGENY WVDKIYTLIE LLDSYIPKPK RKKDKHFLMW IDSVKFLPNI GPIAMGRIEQ
     GTIKVGEFID IVGFRETRTA KIISLEFFNQ SCMQVLAGDD IGVSIEGTKN HNDIKKGMII
     STPGTIKSWL EFEAQVYILK REEGGRTSPF FKGYCPQFFF KTTCVTGRIE AIEYTTGSKT
     WMIMPGDKLK IQVNLVYPIG IKKRMRFLIR EGGVLVGVGI ISNLIK