ID EFTU_KORVE Reviewed; 395 AA. AC Q1IHG6; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 13-JUN-2006, sequence version 1. DT 27-MAR-2024, entry version 104. 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}; GN OrderedLocusNames=Acid345_1224; GN and GN Name=tuf2 {ECO:0000255|HAMAP-Rule:MF_00118}; GN OrderedLocusNames=Acid345_4684; OS Koribacter versatilis (strain Ellin345). OC Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae; OC Koribacter. OX NCBI_TaxID=204669; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ellin345; RX PubMed=19201974; DOI=10.1128/aem.02294-08; RA Ward N.L., Challacombe J.F., Janssen P.H., Henrissat B., Coutinho P.M., RA Wu M., Xie G., Haft D.H., Sait M., Badger J., Barabote R.D., Bradley B., RA Brettin T.S., Brinkac L.M., Bruce D., Creasy T., Daugherty S.C., RA Davidsen T.M., DeBoy R.T., Detter J.C., Dodson R.J., Durkin A.S., RA Ganapathy A., Gwinn-Giglio M., Han C.S., Khouri H., Kiss H., Kothari S.P., RA Madupu R., Nelson K.E., Nelson W.C., Paulsen I., Penn K., Ren Q., RA Rosovitz M.J., Selengut J.D., Shrivastava S., Sullivan S.A., Tapia R., RA Thompson L.S., Watkins K.L., Yang Q., Yu C., Zafar N., Zhou L., Kuske C.R.; RT "Three genomes from the phylum Acidobacteria provide insight into the RT lifestyles of these microorganisms in soils."; RL Appl. Environ. Microbiol. 75:2046-2056(2009). 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; CP000360; ABF40226.1; -; Genomic_DNA. DR EMBL; CP000360; ABF43684.1; -; Genomic_DNA. DR RefSeq; WP_011522028.1; NC_008009.1. DR AlphaFoldDB; Q1IHG6; -. DR SMR; Q1IHG6; -. DR STRING; 204669.Acid345_1224; -. DR EnsemblBacteria; ABF40226; ABF40226; Acid345_1224. DR EnsemblBacteria; ABF43684; ABF43684; Acid345_4684. DR KEGG; aba:Acid345_1224; -. DR KEGG; aba:Acid345_4684; -. DR eggNOG; COG0050; Bacteria. DR HOGENOM; CLU_007265_0_0_0; -. DR OrthoDB; 9804504at2; -. DR Proteomes; UP000002432; 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; Reference proteome. FT CHAIN 1..395 FT /note="Elongation factor Tu" FT /id="PRO_0000337297" FT DOMAIN 10..205 FT /note="tr-type G" FT REGION 19..26 FT /note="G1" FT /evidence="ECO:0000250" FT REGION 61..65 FT /note="G2" FT /evidence="ECO:0000250" FT REGION 82..85 FT /note="G3" FT /evidence="ECO:0000250" FT REGION 137..140 FT /note="G4" FT /evidence="ECO:0000250" FT REGION 175..177 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 82..86 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00118" FT BINDING 137..140 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00118" SQ SEQUENCE 395 AA; 43030 MW; 6A87FB78AC0A789C CRC64; MAKEKFDRSK PHVNVGTIGH IDHGKTTLTA AITKVLSKHN PKIAFRSFDS IDNAPEERER GITIATAHVE YETANRHYAH VDCPGHADYI KNMITGAAQM DGAILVVAAT DGPMPQTKEH VLLARQVGVP YVVVFLNKCD AVEDAELIDL VEMEVRELLN KYGFPGDDLP VVRGSALGAL NGEAQWEAKI DELMEAVDKN IPLPARDIDK PFLMPIEDIF SISGRGTVVT GRIERGKVKV GEEVEIVGFR ETRKTVVTGV EMFKKQLDEG LAGDNAGLLL RGIGKDDVER GMVLAKGGSI TPHTKFKGEV YVLSKEEGGR HTPFFKGYRP QFYFRTTDVT GVATLPAGTE MVMPGDNVAL EIELITPVAM EKGLRFAIRE GGRTVGAGTI SEIIA //