ID EFTU_EHRRG Reviewed; 395 AA. AC Q5FFE6; Q5FFT8; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2005, sequence version 1. DT 24-JAN-2024, entry version 117. 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=ERGA_CDS_01580; GN and GN Name=tuf2 {ECO:0000255|HAMAP-Rule:MF_00118}; Synonyms=tuf; GN OrderedLocusNames=ERGA_CDS_06310; OS Ehrlichia ruminantium (strain Gardel). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales; OC Anaplasmataceae; Ehrlichia. OX NCBI_TaxID=302409; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Gardel; RX PubMed=16547041; DOI=10.1128/jb.188.7.2533-2542.2006; RA Frutos R., Viari A., Ferraz C., Morgat A., Eychenie S., Kandassamy Y., RA Chantal I., Bensaid A., Coissac E., Vachiery N., Demaille J., Martinez D.; RT "Comparative genomic analysis of three strains of Ehrlichia ruminantium RT reveals an active process of genome size plasticity."; RL J. Bacteriol. 188:2533-2542(2006). 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 -!- SEQUENCE CAUTION: CC Sequence=CAI28083.1; Type=Erroneous initiation; Evidence={ECO:0000305}; 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; CR925677; CAI27610.1; -; Genomic_DNA. DR EMBL; CR925677; CAI28083.1; ALT_INIT; Genomic_DNA. DR RefSeq; WP_011154850.1; NC_006831.1. DR AlphaFoldDB; Q5FFE6; -. DR SMR; Q5FFE6; -. DR GeneID; 56785369; -. DR KEGG; erg:ERGA_CDS_01580; -. DR KEGG; erg:ERGA_CDS_06310; -. DR HOGENOM; CLU_007265_0_1_5; -. DR OrthoDB; 9803139at2; -. DR Proteomes; UP000000533; 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: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..395 FT /note="Elongation factor Tu" FT /id="PRO_0000337376" FT DOMAIN 6..205 FT /note="tr-type G" FT REGION 15..22 FT /note="G1" FT /evidence="ECO:0000250" FT REGION 59..63 FT /note="G2" FT /evidence="ECO:0000250" FT REGION 80..83 FT /note="G3" FT /evidence="ECO:0000250" FT REGION 135..138 FT /note="G4" FT /evidence="ECO:0000250" FT REGION 173..175 FT /note="G5" FT /evidence="ECO:0000250" FT BINDING 15..22 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00118" FT BINDING 80..84 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00118" FT BINDING 135..138 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00118" SQ SEQUENCE 395 AA; 43282 MW; C2B3B98AD64B94F0 CRC64; MVDGRKPHIN VGTIGHVDHG KTTLTAALTT VLAKRLSGEG NKSVKYDEID KAPEEKARGI TISTAHVEYE TENRHYAHVD CPGHADYIKN MITGAAQMDA AILVVSATDG AMPQTREHIL LAKQVGVKDI VVWMNKCDVV DDEEMLSLVE MEIRELLTKY GYPGDDIDVV KGSAVKALEE ESADGVWSEK IMELMNALEK IDLPIREKDK PFLMSIEDVF SIPGRGTVVT GRIERGVIKV GDKIDIVGLR DIQSTVCTGV EMFHKALDAG EAGDNAGILL RGIKKEDVER GQVLSAPGQI HSYKGFKAEV YVLKKEEGGR HTPFFSNYQP QFYVRTTDVT GNIKLPDGVE MVMPGDNISI EVNLDKPVAI DKGLRFAIRE GGRTIGSGII TEILE //