ID G8N9L1_9DEIN Unreviewed; 406 AA. AC G8N9L1; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 24-JAN-2024, entry version 63. 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 ORFNames=TCCBUS3UF1_21190 {ECO:0000313|EMBL:AEV17157.1}, GN TCCBUS3UF1_4610 {ECO:0000313|EMBL:AEV15509.1}; OS Thermus sp. CCB_US3_UF1. OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus. OX NCBI_TaxID=1111069 {ECO:0000313|EMBL:AEV15509.1, ECO:0000313|Proteomes:UP000005635}; RN [1] {ECO:0000313|EMBL:AEV15509.1, ECO:0000313|Proteomes:UP000005635} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CCB_US3_UF1 {ECO:0000313|EMBL:AEV15509.1, RC ECO:0000313|Proteomes:UP000005635}; RA Teh B.S., Abdul Rahman A.Y., Saito J.A., Hou S., Alam M.; RT "Complete genome sequence of thermophilic Thermus sp. CCB_US3_UF1."; RL Submitted (NOV-2011) 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; CP003126; AEV15509.1; -; Genomic_DNA. DR EMBL; CP003126; AEV17157.1; -; Genomic_DNA. DR RefSeq; WP_014514872.1; NC_017278.1. DR AlphaFoldDB; G8N9L1; -. DR STRING; 1111069.TCCBUS3UF1_21190; -. DR KEGG; thc:TCCBUS3UF1_21190; -. DR KEGG; thc:TCCBUS3UF1_4610; -. DR PATRIC; fig|1111069.3.peg.2084; -. DR eggNOG; COG0050; Bacteria. DR HOGENOM; CLU_007265_0_1_0; -. DR OrthoDB; 9804504at2; -. DR Proteomes; UP000005635; 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..215 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 406 AA; 44765 MW; 8E94595D25FFE58C CRC64; MAKGEFIRTK PHVNVGTIGH VDHGKTTLTA ALTFVAAAEN PNVEVKDYGE IDKAPEERAR GITINTAHVE YETAARHYSH VDCPGHADYI KNMITGAAQM DGAILVVSAA DGPMPQTREH ILLARQVGVP YIVVFMNKVD MVDDPELLDL VEMEVRDLLN QYEFPGDEVP VIRGSALLAL EQMHKNPQTK RGENEWVDRI WELLDAIDRY IPTPQRDVDK PFLMPVEDVF TITGRGTVAT GRIERGKVKV GDEVEIVGLA PETRKTVVTG VEMHRKTLQE GIAGDNVGLL LRGVGRDEVE RGQVLAKPGS ITPHTKFEAS VYILKKEEGG RHTGFFTGYR PQFYFRTTDV TGVVELPQGV EMVMPGDNVT FVVELIKPVA LEEGLRFAIR EGGRTVGAGV VTKILE //