ID EFTU1_ECO24 Reviewed; 394 AA. AC A7ZSL4; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 23-OCT-2007, sequence version 1. DT 28-JAN-2026, entry version 96. DE RecName: Full=Elongation factor Tu 1 {ECO:0000255|HAMAP-Rule:MF_00118}; DE Short=EF-Tu 1 {ECO:0000255|HAMAP-Rule:MF_00118}; DE EC=3.6.5.3 {ECO:0000255|HAMAP-Rule:MF_00118}; GN Name=tuf1 {ECO:0000255|HAMAP-Rule:MF_00118}; GN OrderedLocusNames=EcE24377A_3808; OS Escherichia coli O139:H28 (strain E24377A / ETEC). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; Enterobacteriaceae; Escherichia. OX NCBI_TaxID=331111; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=E24377A / ETEC; RX PubMed=18676672; DOI=10.1128/jb.00619-08; RA Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F., RA Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R., RA Henderson I.R., Sperandio V., Ravel J.; RT "The pangenome structure of Escherichia coli: comparative genomic analysis RT of E. coli commensal and pathogenic isolates."; RL J. Bacteriol. 190:6881-6893(2008). CC -!- FUNCTION: GTP hydrolase that promotes the GTP-dependent binding of CC aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_00118}. CC -!- CATALYTIC ACTIVITY: CC Reaction=GTP + H2O = GDP + phosphate + H(+); Xref=Rhea:RHEA:19669, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.3; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00118}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00118}; CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00118}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00118}. CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase CC superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00118}. 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; CP000800; ABV16458.1; -; Genomic_DNA. DR RefSeq; WP_000031783.1; NC_009801.1. DR AlphaFoldDB; A7ZSL4; -. DR BMRB; A7ZSL4; -. DR SMR; A7ZSL4; -. DR GeneID; 89518171; -. DR KEGG; ecw:EcE24377A_3808; -. DR HOGENOM; CLU_007265_0_2_6; -. DR Proteomes; UP000001122; Chromosome. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0032045; C:guanyl-nucleotide exchange factor complex; IEA:UniProtKB-ARBA. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule. DR GO; GO:0097216; F:guanosine tetraphosphate binding; IEA:UniProtKB-ARBA. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. 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 CDD; cd03707; EFTU_III; 1. DR FunFam; 2.40.30.10:FF:000001; Elongation factor Tu; 1. DR FunFam; 3.40.50.300:FF:000003; Elongation factor Tu; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR Gene3D; 2.40.30.10; Translation factors; 2. DR HAMAP; MF_00118_B; EF_Tu_B; 1. DR InterPro; IPR041709; EF-Tu_GTP-bd. DR InterPro; IPR050055; EF-Tu_GTPase. 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. 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 NCBIfam; TIGR00485; EF-Tu; 1. DR NCBIfam; NF000766; PRK00049.1; 1. DR NCBIfam; NF009372; PRK12735.1; 1. DR NCBIfam; NF009373; PRK12736.1; 1. DR NCBIfam; TIGR00231; small_GTP; 1. DR PANTHER; PTHR43721:SF22; ELONGATION FACTOR TU, MITOCHONDRIAL; 1. DR PANTHER; PTHR43721; ELONGATION FACTOR TU-RELATED; 1. 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; SSF50465; EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR SUPFAM; SSF50447; Translation proteins; 1. DR PROSITE; PS00301; G_TR_1; 1. DR PROSITE; PS51722; G_TR_2; 1. PE 3: Inferred from homology; KW Cytoplasm; Elongation factor; GTP-binding; Hydrolase; Magnesium; KW Metal-binding; Nucleotide-binding; Protein biosynthesis; KW Reference proteome. FT CHAIN 1..394 FT /note="Elongation factor Tu 1" FT /id="PRO_0000337386" FT DOMAIN 10..204 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:0000255|HAMAP-Rule:MF_00118" FT BINDING 26 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00118" FT BINDING 81..85 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00118" FT BINDING 136..139 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00118" SQ SEQUENCE 394 AA; 43284 MW; 731A60255F43358F CRC64; MSKEKFERTK PHVNVGTIGH VDHGKTTLTA AITTVLAKTY GGAARAFDQI DNAPEEKARG ITINTSHVEY DTPTRHYAHV DCPGHADYVK NMITGAAQMD GAILVVAATD GPMPQTREHI LLGRQVGVPY IIVFLNKCDM VDDEELLELV EMEVRELLSQ YDFPGDDTPI VRGSALKALE GDAEWEAKIL ELAGFLDSYI PEPERAIDKP FLLPIEDVFS ISGRGTVVTG RVERGIIKVG EEVEIVGIKE TQKSTCTGVE MFRKLLDEGR AGENVGVLLR GIKREEIERG QVLAKPGTIK PHTKFESEVY ILSKDEGGRH TPFFKGYRPQ FYFRTTDVTG TIELPEGVEM VMPGDNIKMV VTLIHPIAMD DGLRFAIREG GRTVGAGVVA KVLG //