EFTU_CHACO
ID EFTU_CHACO Reviewed; 408 AA.
AC P50371;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Elongation factor Tu, chloroplastic;
DE Short=EF-Tu;
GN Name=tufA;
OS Chara connivens (Convergent stonewort).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Charophyceae; Charales; Characeae;
OC Chara.
OX NCBI_TaxID=13779;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7663757; DOI=10.1006/mpev.1995.1012;
RA Delwiche C.F., Kuhsel M., Palmer J.D.;
RT "Phylogenetic analysis of tufA sequences indicates a cyanobacterial origin
RT of all plastids.";
RL Mol. Phylogenet. Evol. 4:110-128(1995).
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}.
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; U09425; AAA87685.1; -; Genomic_DNA.
DR PIR; S62725; S62725.
DR AlphaFoldDB; P50371; -.
DR SMR; P50371; -.
DR PRIDE; P50371; -.
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..408
FT /note="Elongation factor Tu, chloroplastic"
FT /id="PRO_0000091447"
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 408 AA; 45321 MW; DAA452E42B0C3489 CRC64;
MAQEVFQRTK PHVNIGTIGH VDHGKTTLTA AITMTLAVNS TCTPKKYDEI DAAPEERARG
ITINTAHVEY ETALRHYAHV DCPGHADYIK NMITGAAQMD GAILVVSAAD GPMPQTKEHI
LLAKQVGVPS IVVFLNKEDQ VDDEEILQLV DLEVRESLIN YEFPGDKVPV VSGSALMALQ
ALTEKPNTSR GENKWVDKIY ELMDAVDSYI PTPKRDIEKP FLMPIEDVFS IQGRGTVATG
RIERGILKLG DIVELIGLNE KIRSTVVTGL EMFRRLLEQG FAGENIGVLL RGIEKKDIER
GMVIAQPGTI EPHTRFEAQV YILRKEEGGR HSPFFAGYRP QFFVRTADVT GVIEAFEYDN
GDKTRMVMPG DRVKMIVNLI CPIAIEKKMR FAIREGGRTI GAGVVYKY