ID G9A4S8_RHIFH Unreviewed; 391 AA. AC G9A4S8; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 27-MAR-2024, entry version 61. 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=tufa3 {ECO:0000313|EMBL:CCE95572.1}; GN Synonyms=tuf {ECO:0000256|HAMAP-Rule:MF_00118}, tufa1 GN {ECO:0000313|EMBL:CCE95558.1}; GN OrderedLocusNames=SFHH103_01059 {ECO:0000313|EMBL:CCE95558.1}, GN SFHH103_01073 {ECO:0000313|EMBL:CCE95572.1}; OS Rhizobium fredii (strain HH103) (Sinorhizobium fredii). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium. OX NCBI_TaxID=1117943 {ECO:0000313|EMBL:CCE95572.1, ECO:0000313|Proteomes:UP000007735}; RN [1] {ECO:0000313|EMBL:CCE95572.1, ECO:0000313|Proteomes:UP000007735} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HH103 {ECO:0000313|EMBL:CCE95572.1, RC ECO:0000313|Proteomes:UP000007735}; RX PubMed=22374952; DOI=10.1128/JB.06729-11; RA Weidner S., Becker A., Bonilla I., Jaenicke S., Lloret J., Margaret I., RA Puhler A., Ruiz-Sainz J.E., Schneiker-Bekel S., Szczepanowski R., RA Vinardell J.M., Zehner S., Gottfert M.; RT "Genome sequence of the soybean symbiont Sinorhizobium fredii HH103."; RL J. Bacteriol. 194:1617-1618(2012). 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; HE616890; CCE95558.1; -; Genomic_DNA. DR EMBL; HE616890; CCE95572.1; -; Genomic_DNA. DR RefSeq; WP_012707739.1; NC_016812.1. DR AlphaFoldDB; G9A4S8; -. DR STRING; 1117943.SFHH103_01059; -. DR GeneID; 48972679; -. DR KEGG; sfh:SFHH103_01059; -. DR KEGG; sfh:SFHH103_01073; -. DR PATRIC; fig|380.5.peg.1129; -. DR eggNOG; COG0050; Bacteria. DR HOGENOM; CLU_007265_0_1_5; -. DR Proteomes; UP000007735; 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}; Hydrolase {ECO:0000313|EMBL:CCE95572.1}; 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; 42663 MW; 65D5D3E550C50658 CRC64; MAKSKFERNK PHVNIGTIGH VDHGKTSLTA AITKYFGEFK AYDQIDAAPE EKARGITIST AHVEYETPAR HYAHVDCPGH ADYVKNMITG AAQMDGAILV VSAADGPMPQ TREHILLARQ VGVPAIVVFL NKVDQVDDAE LLELVELEVR ELLSSYEFPG DDIPIVKGSA LAALEDSDKK IGEDAIRELM AAVDAYIPTP ERPVDLPFLM PIEDVFSISG RGTVVTGRVE RGIVKVGEEI EIVGIRPTTK TTCTGVEMFR KLLDQGQAGD NIGALLRGVD RNGVERGQVL CKPGSVKPHR KFKAEAYILT KEEGGRHTPF FTNYRPQFYF RTTDVTGIVT LPEGTEMVMP GDNVTVDVEL IVPIAMEEKL RFAIREGGRT VGAGIVASIV E //