ID   EFTU_CHLRE              Reviewed;         418 AA.
AC   P17746; B7U1E8;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   03-AUG-2022, entry version 147.
DE   RecName: Full=Elongation factor Tu, chloroplastic;
DE            Short=EF-Tu;
GN   Name=tufA;
OS   Chlamydomonas reinhardtii (Chlamydomonas smithii).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX   NCBI_TaxID=3055;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cw15;
RX   PubMed=2314461; DOI=10.1038/344262a0;
RA   Baldauf S.L., Palmer J.D.;
RT   "Evolutionary transfer of the chloroplast tufA gene to the nucleus.";
RL   Nature 344:262-265(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CC-503;
RX   PubMed=19473533; DOI=10.1186/1471-2148-9-120;
RA   Smith D.R., Lee R.W.;
RT   "Nucleotide diversity of the Chlamydomonas reinhardtii plastid genome:
RT   addressing the mutational-hazard hypothesis.";
RL   BMC Evol. Biol. 9:120-120(2009).
RN   [3]
RP   IDENTIFICATION, AND COMPLETE PLASTID GENOME.
RX   PubMed=12417694; DOI=10.1105/tpc.006155;
RA   Maul J.E., Lilly J.W., Cui L., dePamphilis C.W., Miller W., Harris E.H.,
RA   Stern D.B.;
RT   "The Chlamydomonas reinhardtii plastid chromosome: islands of genes in a
RT   sea of repeats.";
RL   Plant Cell 14:2659-2679(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   -!- 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; X52257; CAA36499.1; -; Genomic_DNA.
DR   EMBL; FJ423446; ACJ50095.1; -; Genomic_DNA.
DR   EMBL; BK000554; DAA00908.1; -; Genomic_DNA.
DR   PIR; S09153; S09153.
DR   RefSeq; NP_958362.1; NC_005353.1.
DR   AlphaFoldDB; P17746; -.
DR   SMR; P17746; -.
DR   STRING; 3055.DAA00908; -.
DR   PaxDb; P17746; -.
DR   PRIDE; P17746; -.
DR   ProMEX; P17746; -.
DR   GeneID; 2716979; -.
DR   KEGG; cre:ChreCp005; -.
DR   eggNOG; KOG0460; Eukaryota.
DR   HOGENOM; CLU_007265_0_0_1; -.
DR   InParanoid; P17746; -.
DR   OrthoDB; 491836at2759; -.
DR   Proteomes; UP000006906; Chloroplast.
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-UniRule.
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.
FT   CHAIN           1..418
FT                   /note="Elongation factor Tu, chloroplastic"
FT                   /id="PRO_0000091448"
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   418 AA;  45743 MW;  9CBEBBE11EE36632 CRC64;
     MSRAKFERKK PHVNIGTIGH VDHGKTTLTA AITMTLAAAG GSVGKKYDEI DSAPEEKARG
     ITINTAHVEY ETEKRHYAHV DCPGHADYVK NMITGAAQMD GAILVVSGAD GPMPQTKEHI
     LLAKQVGVPN VVVFLNKEDQ VDDKELLELV ELEVRETLDK YEFPGDEIPV VPGSALLALE
     ALIENPKTQR GENKWVDKIY QLMDNVDSYI PTPQRETDKP FLLAVEDVLS ITGRGTVATG
     RVERGALRIS DNVEIVGLRP TQTAVVTGLE MFKKTLDETL AGDNVGVLLR GVQKKDIERG
     MVIAKPGTIT PHTKFEAQVY VLTKEEGGRH SAFMIGYQPQ FYVRTTDVTG KVVGFNHIQM
     RNPSSVAEEH SNKMAMPGDR ISMTVELINP IAIEKGMRFA IREGGRTVGA GVVTNIVQ