ID   EFTU_PEA                Reviewed;         488 AA.
AC   O24310;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Elongation factor Tu, chloroplastic;
DE            Short=EF-Tu;
DE   Flags: Precursor;
GN   Name=tufA;
OS   Pisum sativum (Garden pea).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX   NCBI_TaxID=3888;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaf;
RA   Reddy M.K., Nair S., Tewari K.K.;
RL   Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, AND INDUCTION.
RX   PubMed=15219860; DOI=10.1016/j.bbrc.2004.05.192;
RA   Singh B.N., Mishra R.N., Agarwal P.K., Goswami M., Nair S., Sopory S.K.,
RA   Reddy M.K.;
RT   "A pea chloroplast translation elongation factor that is regulated by
RT   abiotic factors.";
RL   Biochem. Biophys. Res. Commun. 320:523-530(2004).
CC   -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-
CC       tRNA to the A-site of ribosomes during protein biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC       {ECO:0000269|PubMed:15219860}.
CC   -!- TISSUE SPECIFICITY: Higher expression in leaves than in roots.
CC       {ECO:0000269|PubMed:15219860}.
CC   -!- INDUCTION: Induced by light, low temperature and salicylic acid (SA).
CC       Repressed by high salt and abscisic acid (ABA).
CC       {ECO:0000269|PubMed:15219860}.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; Y14561; CAA74893.1; -; mRNA.
DR   EMBL; AY083613; AAM01198.1; -; Genomic_DNA.
DR   PIR; T06821; T06821.
DR   PRIDE; O24310; -.
DR   GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
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; TAS:UniProtKB.
DR   GO; GO:0006414; P:translational elongation; TAS:UniProtKB.
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   2: Evidence at transcript level;
KW   Chloroplast; Elongation factor; GTP-binding; Nucleotide-binding; Plastid;
KW   Protein biosynthesis; Transit peptide.
FT   TRANSIT         1..79
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           80..488
FT                   /note="Elongation factor Tu, chloroplastic"
FT                   /id="PRO_0000007457"
FT   DOMAIN          89..293
FT                   /note="tr-type G"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          98..105
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          139..143
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          160..163
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          215..218
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          253..255
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   BINDING         98..105
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         160..164
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         215..218
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   488 AA;  53050 MW;  8C8D694B846A4897 CRC64;
     MALSSTAATT SSKLKLSNPP SLSHTFTASA SASVSNSTSF RPKLTLTRLS SSFLNPSTIL
     HLTPSQRTNR PSSSPFTVRA ARGKFERKKP HLNIGTIGHV DHGKTTLTAA LTMALACLGN
     SAPKKYDEID AAPEERARGI TINTATVEYE TETRHYAHVD CPGHADYVKN MITGAAQMDG
     AILVVSGADG PMPQTKEHIL LAKQVGVPSV VVFLNKQDQV DDEELLELVE LEVRELLSSY
     EFPGDDIPIV SGSALLALEA LMANPTLKRG NNQWVDKIYQ LMDEVDKYIP IPQRQTELPF
     LLAIEDVFSI TXRGTVATGR IERGLVKVGD VVDLVGLRET RNTTVTGVEM FQKILDDAMA
     GDNVGLLLRG IQKIDIQRGM VLAKPGTITP HSKFSAIVYV LKKEEGGRHS PFFAGYRPQF
     YMRTTDVTGK VTSIMNDKDE ESKMVMPGDR VKIVVELIVP VAIEQGMRFA IREGGKTVGA
     GVIGAIIE