ID   EFTU_MESVI              Reviewed;         410 AA.
AC   Q9MUP0;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Elongation factor Tu, chloroplastic;
DE            Short=EF-Tu;
GN   Name=tufA;
OS   Mesostigma viride (Green alga).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Mesostigmatophyceae;
OC   Mesostigmatales; Mesostigmataceae; Mesostigma.
OX   NCBI_TaxID=41882;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-296 / KY-14 / CCMP 2046;
RX   PubMed=10688199; DOI=10.1038/35001059;
RA   Lemieux C., Otis C., Turmel M.;
RT   "Ancestral chloroplast genome in Mesostigma viride reveals an early branch
RT   of green plant evolution.";
RL   Nature 403:649-652(2000).
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; AF166114; AAF43860.1; -; Genomic_DNA.
DR   RefSeq; NP_038420.1; NC_002186.1.
DR   AlphaFoldDB; Q9MUP0; -.
DR   SMR; Q9MUP0; -.
DR   PRIDE; Q9MUP0; -.
DR   GeneID; 800881; -.
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..410
FT                   /note="Elongation factor Tu, chloroplastic"
FT                   /id="PRO_0000091465"
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   410 AA;  44854 MW;  9000DD2DB49800DF CRC64;
     MAREKFERKK PHINIGTIGH VDHGKTTLTA AITMALAVGT GKSGKRYDEI DAAPEEKARG
     ITINTAHVEY ETETRHYAHV DCPGHADYVK NMITGAAQMD GAILVVSGAD GPMPQTKEHI
     LLAKQVGVPN MVVFLNKEDQ VDDPELLELV ELEVRETLNS YDFPGDEIPV VAGSALMALE
     ALTQDSKLAR GSNPWVDKIY ALMDQVDKYI PTPQRDTDKP FLMAIEDVFS ITGRGTVATG
     RVERGKVVVG ENVDIVGLAN IPQNTTVTGL EMFQKTLEES VAGDNVGVLL RGIQKDQVER
     GMVLAKPNTI KPHIRFESEV YVLAKEEGGR HTPFFPGYRP QFYVRTTDVT GKIDSFKADD
     GSDTQMVMPG DRVKMVVSLI QPIAIEKGMR FAIREGGRTV GAGIVSEILE