ID   EFTU_PLAF7              Reviewed;         410 AA.
AC   Q25820;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Elongation factor Tu, apicoplast;
DE            Short=EF-Tu;
GN   Name=tufA;
OS   Plasmodium falciparum (isolate 3D7).
OG   Plastid; Apicoplast.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX   NCBI_TaxID=36329;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BW/C10;
RX   PubMed=8757284; DOI=10.1006/jmbi.1996.0449;
RA   Wilson R.J.M., Denny P.W., Preiser P.R., Rangachari K., Roberts K., Roy A.,
RA   Whyte A., Strath M., Moore D.J., Moore P.W., Williamson D.H.;
RT   "Complete gene map of the plastid-like DNA of the malaria parasite
RT   Plasmodium falciparum.";
RL   J. Mol. Biol. 261:155-172(1996).
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, apicoplast.
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; X95276; CAA64593.1; -; Genomic_DNA.
DR   EMBL; X87630; CAA60960.1; -; Genomic_DNA.
DR   PIR; S72277; S72277.
DR   AlphaFoldDB; Q25820; -.
DR   SMR; Q25820; -.
DR   STRING; 36329.Q25820; -.
DR   PRIDE; Q25820; -.
DR   VEuPathDB; PlasmoDB:PF3D7_API02900; -.
DR   InParanoid; Q25820; -.
DR   PhylomeDB; Q25820; -.
DR   Proteomes; UP000001450; Apicoplast B.
DR   GO; GO:0020011; C:apicoplast; 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; cd03697; EFTU_II; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_00118_B; EF_Tu_B; 1.
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; TIGR00231; small_GTP; 1.
DR   PROSITE; PS00301; G_TR_1; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   3: Inferred from homology;
KW   Apicoplast; Elongation factor; GTP-binding; Nucleotide-binding; Plastid;
KW   Protein biosynthesis; Reference proteome.
FT   CHAIN           1..410
FT                   /note="Elongation factor Tu, apicoplast"
FT                   /id="PRO_0000232686"
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;  46635 MW;  835629C7D5A2002D CRC64;
     MNNKLFLRNK QHINLGTIGH VDHGKTTLTT AISYLLNLQG LSKKYNYSDI DSAPEEKIRG
     ITINTTHIEY ETLTKHCAHI DCPGHSDYIK NMIIGATQMD IAILVISIID GIMPQTYEHL
     LLIKQIGIKN IIIFLNKEDL CDDVELIDFI KLEVNELLIK YNFDLNYIHI LTGSALNVIN
     IIQKNKDYEL IKSNIWIQKL NNLIQIIDNI IIPTRKINDY FLMSIEDVFS ITGRGTVVTG
     KIEQGCINLN DEIEILKFEK SSPNLTTVIG LEMFKKQLTQ AQSGDNVGIL LRNIQKKDIK
     RGMILATPNK LKVYKSFIAE TYILTKEEGG RHKPFNIGYK PQFFIRTVDV TGEIKNIYLN
     ENVQKVAIPG DKITLHIELK HYIVLTLNMK FSIREGGKTI GAGIITEIKN