ID EFTU1_VIBVY Reviewed; 394 AA. AC Q7MH43; DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-2003, sequence version 1. DT 04-NOV-2026, entry version 132. 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}; OrderedLocusNames=VV3029; OS Vibrio vulnificus (strain YJ016). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=196600; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=YJ016; RX PubMed=14656965; DOI=10.1101/gr.1295503; RA Chen C.-Y., Wu K.-M., Chang Y.-C., Chang C.-H., Tsai H.-C., Liao T.-L., RA Liu Y.-M., Chen H.-J., Shen A.B.-T., Li J.-C., Su T.-L., Shao C.-P., RA Lee C.-T., Hor L.-I., Tsai S.-F.; RT "Comparative genome analysis of Vibrio vulnificus, a marine pathogen."; RL Genome Res. 13:2577-2587(2003). 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; BA000037; BAC95793.1; -; Genomic_DNA. DR RefSeq; WP_011151305.1; NC_005139.1. DR AlphaFoldDB; Q7MH43; -. DR SMR; Q7MH43; -. DR STRING; 672.VV93_v1c27570; -. DR KEGG; vvy:VV3029; -. DR PATRIC; fig|196600.6.peg.3006; -. DR HOGENOM; CLU_007265_0_0_6; -. DR OMA; AAITMTM; -. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule. 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. FT CHAIN 1..394 FT /note="Elongation factor Tu 1" FT /id="PRO_0000091435" 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; 43142 MW; 389C18A96E954BC2 CRC64; MSKEKFERTK PHVNVGTIGH VDHGKTTLTA AICTVLSKVY GGTARDFASI DNAPEERERG ITISTSHVEY DTPSRHYAHV DCPGHADYVK NMITGAAQMD GGILVVAATD GPMPQTREHI LLGRQVGIPY IIVFMNKCDM VDDEELLELV EMEVRELLSE YDFPGDDLPV IQGSALGALN GEEQWEAKIV ELAEALDSYI PEPERAVDMP FLMPIEDVFS IQGRGTVVTG RIERGILKVG DEVAIVGIKD TTTTTCTGVE MFRKLLDEGR AGENVGALLR GTKRDEVERG QVLAKPGSIT PHTKFESEVY VLSKDEGGRH TPFFKGYRPQ FYFRTTDVTG DISLPEGVEM VMPGDNIQMV VELISPIAMD EGLRFAIREG GRTVGAGVVA KIFA //