ID EFTU_FUSNN Reviewed; 394 AA. AC Q8R603; DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2002, sequence version 1. DT 27-MAR-2024, entry version 125. 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=FN1555; OS Fusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / DSM 15643 / OS BCRC 10681 / CIP 101130 / JCM 8532 / KCTC 2640 / LMG 13131 / VPI 4355). OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Fusobacteriaceae; OC Fusobacterium. OX NCBI_TaxID=190304; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25586 / DSM 15643 / BCRC 10681 / CIP 101130 / JCM 8532 / RC KCTC 2640 / LMG 13131 / VPI 4355; RX PubMed=11889109; DOI=10.1128/jb.184.7.2005-2018.2002; RA Kapatral V., Anderson I., Ivanova N., Reznik G., Los T., Lykidis A., RA Bhattacharyya A., Bartman A., Gardner W., Grechkin G., Zhu L., Vasieva O., RA Chu L., Kogan Y., Chaga O., Goltsman E., Bernal A., Larsen N., D'Souza M., RA Walunas T., Pusch G., Haselkorn R., Fonstein M., Kyrpides N.C., RA Overbeek R.; RT "Genome sequence and analysis of the oral bacterium Fusobacterium nucleatum RT strain ATCC 25586."; RL J. Bacteriol. 184:2005-2018(2002). 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; AE009951; AAL93681.1; -; Genomic_DNA. DR RefSeq; NP_602382.1; NC_003454.1. DR RefSeq; WP_005903497.1; NZ_CP028101.1. DR AlphaFoldDB; Q8R603; -. DR SMR; Q8R603; -. DR STRING; 190304.FN1555; -. DR PaxDb; 190304-FN1555; -. DR EnsemblBacteria; AAL93681; AAL93681; FN1555. DR GeneID; 79782496; -. DR KEGG; fnu:FN1555; -. DR PATRIC; fig|190304.8.peg.58; -. DR eggNOG; COG0050; Bacteria. DR HOGENOM; CLU_007265_0_0_0; -. DR InParanoid; Q8R603; -. DR BioCyc; FNUC190304:G1FZS-59-MONOMER; -. DR Proteomes; UP000002521; Chromosome. 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..394 FT /note="Elongation factor Tu" FT /id="PRO_0000091328" 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; 43458 MW; 417DB9AAB2C18ECD CRC64; MAKEKYERSK PHVNIGTIGH VDHGKTTTTA AISKVLSDKG WASKVDFDQI DAAPEEKERG ITINTAHIEY ETEKRHYAHV DCPGHADYVK NMITGAAQMD GAILVVSAAD GPMPQTREHI LLSRQVGVPY IVVYLNKSDM VEDEELLELV EMEVRELLTE YGFPGDDIPV IRGSSLGALN GEEKWVEKIL ELMEAVDNYI PTPERAVDQP FLMPIEDVFT ITGRGTVVTG RVERGVIKVG EEIEIVGIKP TTKTTCTGVE MFRKLLDQGQ AGDNIGVLLR GTKKEEVERG QVLAKPGSIH PHTNFKGEVY VLTKDEGGRH TPFFTGYRPQ FYFRTTDITG AVTLPDGVEM VMPGDNITMT VELIHPIAME QGLRFAIREG GRTVASGVVS EITK //