ID EFTU_LEPIN Reviewed; 401 AA. AC Q9XD38; Q7CM62; DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 27-MAR-2024, entry version 132. DE RecName: Full=Elongation factor Tu {ECO:0000255|HAMAP-Rule:MF_00118}; DE Short=EF-Tu {ECO:0000255|HAMAP-Rule:MF_00118}; GN Name=tuf {ECO:0000255|HAMAP-Rule:MF_00118}; OrderedLocusNames=LA_0737; OS Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain OS 56601). OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae; OC Leptospira. OX NCBI_TaxID=189518; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=Lai / Serogroup Icterohaemorrhagiae / Serovar lai; RX PubMed=10620683; DOI=10.1111/j.1574-6968.2000.tb08912.x; RA Zuerner R.L., Hartskeerl R.A., van de Kemp H., Bal A.E.; RT "Characterization of the Leptospira interrogans S10-spc-alpha operon."; RL FEMS Microbiol. Lett. 182:303-308(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=56601; RX PubMed=12712204; DOI=10.1038/nature01597; RA Ren S.-X., Fu G., Jiang X.-G., Zeng R., Miao Y.-G., Xu H., Zhang Y.-X., RA Xiong H., Lu G., Lu L.-F., Jiang H.-Q., Jia J., Tu Y.-F., Jiang J.-X., RA Gu W.-Y., Zhang Y.-Q., Cai Z., Sheng H.-H., Yin H.-F., Zhang Y., Zhu G.-F., RA Wan M., Huang H.-L., Qian Z., Wang S.-Y., Ma W., Yao Z.-J., Shen Y., RA Qiang B.-Q., Xia Q.-C., Guo X.-K., Danchin A., Saint Girons I., RA Somerville R.L., Wen Y.-M., Shi M.-H., Chen Z., Xu J.-G., Zhao G.-P.; RT "Unique physiological and pathogenic features of Leptospira interrogans RT revealed by whole-genome sequencing."; RL Nature 422:888-893(2003). CC -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl- CC tRNA to the A-site of ribosomes during protein biosynthesis. CC {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; AF115283; AAD40614.1; -; Genomic_DNA. DR EMBL; AE010300; AAN47936.1; -; Genomic_DNA. DR RefSeq; NP_710918.1; NC_004342.2. DR RefSeq; WP_001040571.1; NC_004342.2. DR AlphaFoldDB; Q9XD38; -. DR SMR; Q9XD38; -. DR STRING; 189518.LA_0737; -. DR PaxDb; 189518-LA_0737; -. DR EnsemblBacteria; AAN47936; AAN47936; LA_0737. DR GeneID; 61142749; -. DR KEGG; lil:LA_0737; -. DR PATRIC; fig|189518.3.peg.741; -. DR HOGENOM; CLU_007265_0_1_12; -. DR InParanoid; Q9XD38; -. DR OrthoDB; 9804504at2; -. DR Proteomes; UP000001408; Chromosome I. DR GO; GO:0005737; C:cytoplasm; 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; IBA:GO_Central. DR GO; GO:0006414; P:translational elongation; IBA:GO_Central. DR CDD; cd01884; EF_Tu; 1. DR CDD; cd03697; EFTU_II; 1. DR CDD; cd03707; EFTU_III; 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; 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 NCBIfam; TIGR00485; EF-Tu; 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; Nucleotide-binding; KW Protein biosynthesis; Reference proteome. FT CHAIN 1..401 FT /note="Elongation factor Tu" FT /id="PRO_0000091340" FT DOMAIN 10..211 FT /note="tr-type G" FT REGION 19..26 FT /note="G1" FT /evidence="ECO:0000250" FT REGION 62..66 FT /note="G2" FT /evidence="ECO:0000250" FT REGION 83..86 FT /note="G3" FT /evidence="ECO:0000250" FT REGION 138..141 FT /note="G4" FT /evidence="ECO:0000250" FT REGION 179..181 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 83..87 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00118" FT BINDING 138..141 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00118" SQ SEQUENCE 401 AA; 43574 MW; B8ED827C1A717BA0 CRC64; MAKEKFDRSK PHLNVGTIGH VDHGKTTLTA AITTTLAKAI GGKNKAVAYD QIDNAPEEKA RGITIATSHQ EYETANRHYA HVDCPGHADY VKNMITGAAQ MDAAILVVSA TDGPMPQTKE HILLARQVGV PYVIVFINKA DMLAADERAE MIEMVEMDVR ELLNKYSFPG DTTPIVHGSA VKALEGDESE IGMPAILKLM EALDTFVPNP KRVIDKPFLM PVEDVFSITG RGTVATGRVE QGVLKVNDEV EIIGIRPTTK TVVTGIEMFR KLLDQAEAGD NIGALLRGTK KEEIERGQVL AKPGSITPHK KFAAEVYVLT KDEGGRHTPF INNYRPQFYF RTTDVTGVCN LPNGVEMVMP GDNVSLTVEL ISPIAMDKGL KFAIREGGRT IGSGVVAEIT E //