ID   EFTU_COLOB              Reviewed;         415 AA.
AC   P18905;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Elongation factor Tu, chloroplastic;
DE            Short=EF-Tu;
GN   Name=tufA;
OS   Coleochaete orbicularis (Charophycean green alga).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Coleochaetophyceae; Coleochaetales;
OC   Coleochaetaceae; Coleochaete.
OX   NCBI_TaxID=3124;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2371274; DOI=10.1073/pnas.87.14.5317;
RA   Baldauf S.L., Manhart J.R., Palmer J.D.;
RT   "Different fates of the chloroplast tufA gene following its transfer to the
RT   nucleus in green algae.";
RL   Proc. Natl. Acad. Sci. U.S.A. 87:5317-5321(1990).
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   -!- MISCELLANEOUS: This is a very divergent elongation factor, it is
CC       probably no longer completely functional.
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; M34286; AAA84135.1; -; Genomic_DNA.
DR   PIR; A35773; A35773.
DR   AlphaFoldDB; P18905; -.
DR   SMR; P18905; -.
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; 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; 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   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..415
FT                   /note="Elongation factor Tu, chloroplastic"
FT                   /id="PRO_0000091451"
FT   DOMAIN          13..217
FT                   /note="tr-type G"
FT   REGION          22..29
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          63..67
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          84..87
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          139..142
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          177..179
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   BINDING         22..29
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         84..88
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         139..142
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   415 AA;  46753 MW;  F532FA1408FBF9AB CRC64;
     MERLLHMTFR NKKIHLNVGT IGHFSHGKTT LTAAITAVLA GIGYTQPKQN DAIDSTSEEK
     ARNMSIYVHH VEYETAARHY SHLDCPGHVN YINNMITGVS QMDGAILVVS AVDGPMAQTK
     EHILLAKLLG ISSILVFINK EDELDDQEVL PMLIQNMRQI LIYYGFPGHT SPILCGSALL
     ALEAMNENPN FNRGKNKWVD KISSLIDHLD LYLPTPRRKL NKPFLMPIER VILIPSFGLV
     GTGTIEKGHI NIGESVEIVG FKDTQHSKVI SLKMFNKTLE QAIAGDDIGI FLEGTNKNNF
     QKGMVIAKPN TIQSWNHFEA QIYILRREEG GRRSPFFQGY CPQFYFRTIQ ITGRMESFEY
     EIGGKTWMVM PGEKIKAIIQ LIFPIALKKK MRFVIREGGF TIGVGIILEL IKIKN