EFTU_EUGGR
ID EFTU_EUGGR Reviewed; 409 AA.
AC P02991;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Elongation factor Tu, chloroplastic;
DE Short=EF-Tu;
GN Name=tufA;
OS Euglena gracilis.
OG Plastid; Chloroplast.
OC Eukaryota; Discoba; Euglenozoa; Euglenida; Spirocuta; Euglenophyceae;
OC Euglenales; Euglenaceae; Euglena.
OX NCBI_TaxID=3039;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Z / UTEX 753;
RX PubMed=6310519; DOI=10.1093/nar/11.17.5877;
RA Montandon P.-E., Stutz E.;
RT "Nucleotide sequence of a Euglena gracilis chloroplast genome region coding
RT for the elongation factor Tu; evidence for a spliced mRNA.";
RL Nucleic Acids Res. 11:5877-5892(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Z / UTEX 753;
RX PubMed=3118328; DOI=10.1093/nar/15.19.7809;
RA Montandon P.-E., Knuchel-Aegerter C., Stutz E.;
RT "Euglena gracilis chloroplast DNA: the untranslated leader of tufA-ORF206
RT gene contains an intron.";
RL Nucleic Acids Res. 15:7809-7822(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Z / UTEX 753;
RX PubMed=8346031; DOI=10.1093/nar/21.15.3537;
RA Hallick R.B., Hong L., Drager R.G., Favreau M.R., Monfort A., Orsat B.,
RA Spielmann A., Stutz E.;
RT "Complete sequence of Euglena gracilis chloroplast DNA.";
RL Nucleic Acids Res. 21:3537-3544(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28.
RX PubMed=6324129; DOI=10.1093/nar/12.6.2851;
RA Montandon P.-E., Stutz E.;
RT "The genes for the ribosomal proteins S12 and S7 are clustered with the
RT gene for the EF-Tu protein on the chloroplast genome of Euglena gracilis.";
RL Nucleic Acids Res. 12:2851-2859(1984).
RN [5]
RP METHYLATION AT LYS-57.
RX PubMed=2125570; DOI=10.1016/0378-1097(90)90227-h;
RA Toledo H., Jerez C.A.;
RT "In vivo and in vitro methylation of the elongation factor EF-Tu from
RT Euglena gracilis chloroplast.";
RL FEMS Microbiol. Lett. 59:241-246(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 -!- 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; Z11874; CAA77904.1; -; Genomic_DNA.
DR EMBL; X00044; CAA24925.1; -; Genomic_DNA.
DR EMBL; X06254; CAA29599.1; -; Genomic_DNA.
DR EMBL; X70810; CAA50087.1; -; Genomic_DNA.
DR EMBL; X00480; CAA25159.1; -; Genomic_DNA.
DR PIR; S34508; EFEGT.
DR RefSeq; NP_041900.1; NC_001603.2.
DR AlphaFoldDB; P02991; -.
DR SMR; P02991; -.
DR iPTMnet; P02991; -.
DR GeneID; 807509; -.
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 1: Evidence at protein level;
KW Chloroplast; Elongation factor; GTP-binding; Methylation;
KW Nucleotide-binding; Plastid; Protein biosynthesis.
FT CHAIN 1..409
FT /note="Elongation factor Tu, chloroplastic"
FT /id="PRO_0000091458"
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"
FT MOD_RES 57
FT /note="N6-methyllysine"
FT /evidence="ECO:0000305|PubMed:2125570"
SQ SEQUENCE 409 AA; 45062 MW; C803740422FFEB84 CRC64;
MARQKFERTK PHINIGTIGH VDHGKTTLTA AITMALAATG NSKAKRYEDI DSAPEEKARG
ITINTAHVEY ETKNRHYAHV DCPGHADYVK NMITGAAQMD GAILVVSAAD GPMPQTKEHI
LLAKQVGVPN IVVFLNKEDQ VDDSELLELV ELEIRETLSN YEFPGDDIPV IPGSALLSVE
ALTKNPKITK GENKWVDKIL NLMDQVDSYI PTPTRDTEKD FLMAIEDVLS ITGRGTVATG
RVERGTIKVG ETVELVGLKD TRSTTITGLE MFQKSLDEAL AGDNVGVLLR GIQKNDVERG
MVLAKPRTIN PHTKFDSQVY ILTKEEGGRH TPFFEGYRPQ FYVRTTDVTG KIESFRSDND
NPAQMVMPGD RIKMKVELIQ PIAIEKGMRF AIREGGRTVG AGVVLSIIQ
