ID D5H7Z9_SALRM Unreviewed; 396 AA. AC D5H7Z9; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 24-JAN-2024, entry version 69. 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=tufA {ECO:0000313|EMBL:CBH24154.1}; GN Synonyms=tuf {ECO:0000256|HAMAP-Rule:MF_00118}; GN OrderedLocusNames=SRM_01233 {ECO:0000313|EMBL:CBH24154.1}; OS Salinibacter ruber (strain M8). OC Bacteria; Rhodothermota; Rhodothermia; Rhodothermales; Salinibacteraceae; OC Salinibacter. OX NCBI_TaxID=761659 {ECO:0000313|EMBL:CBH24154.1, ECO:0000313|Proteomes:UP000000933}; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=M8; RA Pena A., Teeling H., Huerta-Cepas J., Santos F., Yarza P., RA Brito-Echeverria J., Lucio M., Schmitt-Kopplin P., Meseguer I., RA Schenowitz C., Dossat C., Barbe V., Dopazo J., Rossello-Mora R., RA Schuler M., Glockner F.O., Amann R., Gabaldon T., Anton J.; RT "Fine-scale evolution: genomic, phenotypic and ecological differentiation RT in two coexisting Salinibacter ruber strains."; RL ISME J. 4:882-95(2010). RN [2] {ECO:0000313|EMBL:CBH24154.1, ECO:0000313|Proteomes:UP000000933} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=M8 {ECO:0000313|EMBL:CBH24154.1, RC ECO:0000313|Proteomes:UP000000933}; RX PubMed=20164864; DOI=10.1038/ismej.2010.6; RA Pena A., Teeling H., Huerta-Cepas J., Santos F., Yarza P., RA Brito-Echeverria J., Lucio M., Schmitt-Kopplin P., Meseguer I., RA Schenowitz C., Dossat C., Barbe V., Dopazo J., Rossello-Mora R., RA Schuler M., Glockner F.O., Amann R., Gabaldon T., Anton J.; RT "Fine-scale evolution: genomic, phenotypic and ecological differentiation RT in two coexisting Salinibacter ruber strains."; RL ISME J. 4:882-895(2010). RN [3] {ECO:0000313|Proteomes:UP000000933} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=M8 {ECO:0000313|Proteomes:UP000000933}; RG Genoscope; RT "Genome sequence of Salinibacter ruber M8."; RL Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases. 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; FP565814; CBH24154.1; -; Genomic_DNA. DR RefSeq; WP_011403793.1; NC_014032.1. DR AlphaFoldDB; D5H7Z9; -. DR SMR; D5H7Z9; -. DR GeneID; 83727962; -. DR KEGG; srm:SRM_01233; -. DR PATRIC; fig|761659.10.peg.1360; -. DR HOGENOM; CLU_007265_0_1_10; -. DR Proteomes; UP000000933; 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 {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..205 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 82..86 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00118" FT BINDING 137..140 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00118" SQ SEQUENCE 396 AA; 43729 MW; 64D19E50888E7698 CRC64; MAKEEFAREK PHVNVGTIGH VDHGKTTLTA AITKVLAERV GGAAEQTFEA IDNAPEERER GITIATSHVE YETENRHYAH VDCPGHADYV KNMVTGAAQM DGAILVVGSD DGPMPQTREH ILLARQVGVP YLVVFMNKTD LVDDAELLEL VEMEVRELLT EYEFPGDEVP VVRGSALQAL ESSEEHEEKI MELMEAVDEY IPTPERDVEK PFLMPVEDIF SITGRGTVVT GRIERGRVQL QDEIEIVGMQ EEKMDSVVTG IEMFNKTLEE GEAGDNAGIL LRGIEKEEVK RGMVLAEPGT VTPHKEFECE VYVLSKEEGG RHTPFFDGYQ PQFYFRTTDV TGSIELPEGV EMVMPGDNAT FEGSLIEPVA LEEGLRFAIR EGGHTVGAGV VTDILD //