ID EFTU_VIBC3 Reviewed; 394 AA. AC A5F3K0; C3M3X9; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 12-JUN-2007, sequence version 1. DT 27-MAR-2024, entry version 94. DE RecName: Full=Elongation factor Tu {ECO:0000255|HAMAP-Rule:MF_00118}; DE Short=EF-Tu {ECO:0000255|HAMAP-Rule:MF_00118}; GN Name=tuf1 {ECO:0000255|HAMAP-Rule:MF_00118}; Synonyms=tufA; GN OrderedLocusNames=VC0395_A2723, VC395_0364; GN and GN Name=tuf2 {ECO:0000255|HAMAP-Rule:MF_00118}; Synonyms=tufB; GN OrderedLocusNames=VC0395_A2774, VC395_0405; OS Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 / OS O395). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae; OC Vibrio. OX NCBI_TaxID=345073; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395; RA Heidelberg J.; RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395; RX PubMed=19115014; DOI=10.1371/journal.pone.0004053; RA Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J., RA Wang W., Wang J., Qian W., Li D., Wang L.; RT "A recalibrated molecular clock and independent origins for the cholera RT pandemic clones."; RL PLoS ONE 3:E4053-E4053(2008). 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; CP000627; ABQ21011.1; -; Genomic_DNA. DR EMBL; CP000627; ABQ21384.1; -; Genomic_DNA. DR EMBL; CP001235; ACP08387.1; -; Genomic_DNA. DR EMBL; CP001235; ACP08428.1; -; Genomic_DNA. DR RefSeq; WP_000031644.1; NZ_CP045719.1. DR AlphaFoldDB; A5F3K0; -. DR SMR; A5F3K0; -. DR GeneID; 69720944; -. DR KEGG; vco:VC0395_A2723; -. DR KEGG; vco:VC0395_A2774; -. DR KEGG; vcr:VC395_0364; -. DR KEGG; vcr:VC395_0405; -. DR PATRIC; fig|345073.21.peg.352; -. DR eggNOG; COG0050; Bacteria. DR HOGENOM; CLU_007265_0_0_6; -. DR OrthoDB; 9803139at2; -. DR Proteomes; UP000000249; Chromosome 2. 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:0097216; F:guanosine tetraphosphate binding; IEA:UniProt. 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 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. FT CHAIN 1..394 FT /note="Elongation factor Tu" FT /id="PRO_0000337567" 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 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; 43126 MW; BF0DE31A00618B36 CRC64; MSKEKFERTK PHVNVGTIGH VDHGKTTLTA AICTVLAKVY GGKARDFASI DNAPEERERG ITINTSHVEY DTPNRHYAHV DCPGHADYVK NMITGAAQMD GGILVVAATD GPMPQTREHI LLGRQVGIPY IIVFMNKCDM VDDEELLELV EMEVRELLSE YDFPGDDLPV IQGSALGALN GEAQWEAKIV ELAEALDTYI PEPERAVDMA FLMPIEDVFS IQGRGTVVTG RIERGILKVG DEVAIVGIKE TVKTTCTGVE MFRKLLDEGR AGENVGALLR GTKREEVERG QVLAKPGSIT PHTKFESEVY VLSKDEGGRH TPFFKGYRPQ FYFRTTDVTG SIELPEGVEM VMPGDNVKMV VDLIAPIAMD EGLRFAIREG GRTVGAGVVA KIIA //