ID C6AUY0_RHILS Unreviewed; 391 AA. AC C6AUY0; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 27-MAR-2024, entry version 88. DE RecName: Full=Elongation factor Tu {ECO:0000256|ARBA:ARBA00029554, ECO:0000256|HAMAP-Rule:MF_00118}; DE Short=EF-Tu {ECO:0000256|HAMAP-Rule:MF_00118}; GN Name=tuf {ECO:0000256|HAMAP-Rule:MF_00118}; GN OrderedLocusNames=Rleg_1413 {ECO:0000313|EMBL:ACS55705.1}, Rleg_1428 GN {ECO:0000313|EMBL:ACS55720.1}; OS Rhizobium leguminosarum bv. trifolii (strain WSM1325). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium. OX NCBI_TaxID=395491 {ECO:0000313|EMBL:ACS55705.1, ECO:0000313|Proteomes:UP000002256}; RN [1] {ECO:0000313|EMBL:ACS55705.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=WSM1325 {ECO:0000313|EMBL:ACS55705.1}; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., RA Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., Detter J.C., Han C., RA Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova H., Reeve W.G.; RT "Complete sequence of chromosome of Rhizobium leguminosarum bv. trifolii RT WSM1325."; RL Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ACS55705.1, ECO:0000313|Proteomes:UP000002256} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=WSM1325 {ECO:0000313|EMBL:ACS55705.1, RC ECO:0000313|Proteomes:UP000002256}; RX PubMed=21304718; RA Reeve W., O'Hara G., Chain P., Ardley J., Brau L., Nandesena K., Tiwari R., RA Copeland A., Nolan M., Han C., Brettin T., Land M., Ovchinikova G., RA Ivanova N., Mavromatis K., Markowitz V., Kyrpides N., Melino V., Denton M., RA Yates R., Howieson J.; RT "Complete genome sequence of Rhizobium leguminosarum bv. trifolii strain RT WSM1325, an effective microsymbiont of annual Mediterranean clovers."; RL Stand. Genomic Sci. 2:347-356(2010). CC -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl- CC tRNA to the A-site of ribosomes during protein biosynthesis. CC {ECO:0000256|HAMAP-Rule:MF_00118}. CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00118}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|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:0000256|ARBA:ARBA00007249, ECO:0000256|HAMAP- CC 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; CP001622; ACS55705.1; -; Genomic_DNA. DR EMBL; CP001622; ACS55720.1; -; Genomic_DNA. DR RefSeq; WP_012757012.1; NC_012850.1. DR AlphaFoldDB; C6AUY0; -. DR GeneID; 67484945; -. DR KEGG; rlg:Rleg_1413; -. DR KEGG; rlg:Rleg_1428; -. DR HOGENOM; CLU_007265_0_1_5; -. DR OrthoDB; 9803139at2; -. DR Proteomes; UP000002256; 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 {ECO:0000256|HAMAP-Rule:MF_00118}; KW Elongation factor {ECO:0000256|ARBA:ARBA00022768, ECO:0000256|HAMAP- KW Rule:MF_00118}; KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP- KW Rule:MF_00118}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_00118}; KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP- KW Rule:MF_00118}. FT DOMAIN 10..201 FT /note="Tr-type G" FT /evidence="ECO:0000259|PROSITE:PS51722" FT BINDING 19..26 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00118" FT BINDING 76..80 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00118" FT BINDING 131..134 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00118" SQ SEQUENCE 391 AA; 42596 MW; B55D6BDE0D715A82 CRC64; MGKSKFERNK PHVNIGTIGH VDHGKTSLTA AITKYFGEYK AYDQIDAAPE EKARGITIST AHVEYETPAR HYAHVDCPGH ADYVKNMITG AAQMDGAILV CSAADGPMPQ TREHILLARQ VGVPAIVVFL NKVDQVDDAE LLELVELEVR ELLSSYDFPG DDIPIVKGSA LAALEDSDKK IGEDSIRELM AAVDAYIPTP ERPINLPFLL PIEDVFSISG RGTVVTGRVE RGIVKVGEEV EIVGIRPTTK TTVTGVEMFR KLLDQGQAGD NIGALIRGVT RDGVERGQIL CKPGSVKPHK KFMAEAYILT KEEGGRHTPF FTNYRPQFYF RTTDVTGIVT LPEGTEMVMP GDNVTVSVEL IVPIAMEEKL RFAIREGGRT VGAGIVASIV E //