ID EFTU_BACFR Reviewed; 394 AA. AC P33165; DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1993, sequence version 1. DT 27-MAR-2024, entry version 135. 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=BF4199; OS Bacteroides fragilis (strain YCH46). OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=295405; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2110445; DOI=10.1007/bf00249075; RA Ludwig W., Weizenegger M., Betzl D., Leidel E., Lenz T., Ludvigsen A., RA Moellenhoff D., Wenzig P., Schleifer K.H.; RT "Complete nucleotide sequences of seven eubacterial genes coding for the RT elongation factor Tu: functional, structural and phylogenetic RT evaluations."; RL Arch. Microbiol. 153:241-247(1990). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=YCH46; RX PubMed=15466707; DOI=10.1073/pnas.0404172101; RA Kuwahara T., Yamashita A., Hirakawa H., Nakayama H., Toh H., Okada N., RA Kuhara S., Hattori M., Hayashi T., Ohnishi Y.; RT "Genomic analysis of Bacteroides fragilis reveals extensive DNA inversions RT regulating cell surface adaptation."; RL Proc. Natl. Acad. Sci. U.S.A. 101:14919-14924(2004). 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; AP006841; BAD50942.1; -; Genomic_DNA. DR PIR; B60663; B60663. DR RefSeq; WP_005782155.1; NZ_UYXF01000007.1. DR RefSeq; YP_101476.1; NC_006347.1. DR AlphaFoldDB; P33165; -. DR SMR; P33165; -. DR STRING; 295405.BF4199; -. DR GeneID; 66331177; -. DR KEGG; bfr:BF4199; -. DR PATRIC; fig|295405.11.peg.4054; -. DR HOGENOM; CLU_007265_0_0_10; -. DR OrthoDB; 9804504at2; -. DR Proteomes; UP000002197; 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; 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_0000091288" FT DOMAIN 10..205 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; 43580 MW; 7B4C6FD208323149 CRC64; MAKEKFERTK PHVNIGTIGH VDHGKTTLTA AITTVLAKKG LSELRSFDSI DNAPEEKERG ITINTSHVEY ETANRHYAHV DCPGHADYVK NMVTGAAQMD GAIIVVAATD GPMPQTREHI LLARQVNVPK LVVFMNKCDM VEDAEMLELV EMEMRELLSF YDFDGDNTPI IQGSALGALN GVEKWEDKVM ELMEAVDTWI PLPPRDVDKP FLMPVEDVFS ITGRGTVATG RIETGVIHVG DEIEILGLGE DKKSVVTGVE MFRKLLDQGE AGDNVGLLLR GVDKNEIKRG MVLCKPGQIK PHSKFKAEVY ILKKEEGGRH TPFHNKYRPQ FYLRTMDCTG EITLPEGTEM VMPGDNVTIT VELIYPVALN IGLRFAIREG GRTVGAGQIT EIID //