ID EFTU1_THET8 Reviewed; 406 AA. AC Q5SHN6; DT 24-MAY-2005, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 127. DE RecName: Full=Elongation factor Tu-A {ECO:0000255|HAMAP-Rule:MF_00118}; DE Short=EF-Tu-A {ECO:0000255|HAMAP-Rule:MF_00118}; GN Name=tufA {ECO:0000255|HAMAP-Rule:MF_00118}; Synonyms=tuf; GN OrderedLocusNames=TTHA1694; OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8). OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus. OX NCBI_TaxID=300852; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=3317278; DOI=10.1093/nar/15.22.9263; RA Seidler L., Peter M., Meissner F., Sprinzl M.; RT "Sequence and identification of the nucleotide binding site for the RT elongation factor Tu from Thermus thermophilus HB8."; RL Nucleic Acids Res. 15:9263-9277(1987). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2826164; DOI=10.1111/j.1432-1033.1987.tb13671.x; RA Kushiro A., Shimizu M., Tomita K.; RT "Molecular cloning and sequence determination of the tuf gene coding for RT the elongation factor Tu of Thermus thermophilus HB8."; RL Eur. J. Biochem. 170:93-98(1987). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27634 / DSM 579 / HB8; RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T., RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.; RT "Complete genome sequence of Thermus thermophilus HB8."; RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases. RN [4] RP PHOSPHORYLATION. RX PubMed=8416965; DOI=10.1016/s0021-9258(18)54193-4; RA Lippmann C., Lindschau C., Vijgenboom E., Schroeder W., Bosch L., RA Erdmann V.A.; RT "Prokaryotic elongation factor Tu is phosphorylated in vivo."; RL J. Biol. Chem. 268:601-607(1993). RN [5] RP FUNCTION. RX PubMed=27224426; DOI=10.1371/journal.pbio.1002465; RA Routh S.B., Pawar K.I., Ahmad S., Singh S., Suma K., Kumar M., Kuncha S.K., RA Yadav K., Kruparani S.P., Sankaranarayanan R.; RT "Elongation factor Tu prevents misediting of Gly-tRNA(Gly) caused by the RT design behind the chiral proofreading site of D-aminoacyl-tRNA deacylase."; RL PLoS Biol. 14:E1002465-E1002465(2016). RN [6] {ECO:0007744|PDB:1HA3} RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF COMPLEX WITH GDP AND AURODOX. RX PubMed=11278992; DOI=10.1074/jbc.m100017200; RA Vogeley L., Palm G.J., Mesters J.R., Hilgenfeld R.; RT "Conformational change of elongation factor Tu (EF-Tu) induced by RT antibiotic binding. Crystal structure of the complex between EF-Tu.GDP and RT aurodox."; RL J. Biol. Chem. 276:17149-17155(2001). RN [7] {ECO:0007744|PDB:1ZC8} RP STRUCTURE BY ELECTRON MICROSCOPY (13.00 ANGSTROMS), FUNCTION, SUBUNIT, AND RP TMRNA-BINDING. RC STRAIN=ATCC 27634 / DSM 579 / HB8; RX PubMed=12677067; DOI=10.1126/science.1081798; RA Valle M., Gillet R., Kaur S., Henne A., Ramakrishnan V., Frank J.; RT "Visualizing tmRNA entry into a stalled ribosome."; RL Science 300:127-130(2003). CC -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl- CC tRNA to the A-site of ribosomes during protein biosynthesis. CC -!- FUNCTION: EF-Tu-GDP binds to the acceptor arm of tmRNA by interacting CC with its acceptor arm, suggesting that GTP hydrolysis by EF-Tu is CC essential for tmRNA function. {ECO:0000269|PubMed:12677067}. CC -!- FUNCTION: Protects glycyl-tRNA(Gly) from hydrolysis by E.coli D- CC aminoacyl-tRNA deacylase (dtd) (PubMed:27224426). CC {ECO:0000269|PubMed:27224426}. CC -!- SUBUNIT: Monomer (By similarity). Binds to the 70S ribosome, contacts CC tmRNA during trans-translation (PubMed:12677067). {ECO:0000255|HAMAP- CC Rule:MF_00118, ECO:0000269|PubMed:12677067}. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- PTM: Phosphorylated on a threonine. {ECO:0000269|PubMed:8416965}. 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; X05977; CAA29397.1; -; Genomic_DNA. DR EMBL; X06657; CAA29856.1; -; Genomic_DNA. DR EMBL; AP008226; BAD71517.1; -; Genomic_DNA. DR PIR; S00229; S00229. DR PIR; S17146; S17146. DR RefSeq; WP_011228847.1; NC_006461.1. DR RefSeq; YP_144960.1; NC_006461.1. DR PDB; 1HA3; X-ray; 2.00 A; A/B=2-406. DR PDB; 1ZC8; EM; 13.00 A; Y=2-406. DR PDB; 2C78; X-ray; 1.40 A; A=2-406. DR PDB; 4V5G; X-ray; 3.60 A; AZ/CZ=1-406. DR PDB; 4V5P; X-ray; 3.10 A; AZ/CZ=2-406. DR PDB; 4V5Q; X-ray; 3.10 A; AZ/CZ=2-406. DR PDB; 4V5R; X-ray; 3.10 A; AZ/CZ=2-406. DR PDB; 4V5S; X-ray; 3.10 A; AZ/CZ=2-406. DR PDB; 4V8Q; X-ray; 3.10 A; BZ=2-406. DR PDBsum; 1HA3; -. DR PDBsum; 1ZC8; -. DR PDBsum; 2C78; -. DR PDBsum; 4V5G; -. DR PDBsum; 4V5P; -. DR PDBsum; 4V5Q; -. DR PDBsum; 4V5R; -. DR PDBsum; 4V5S; -. DR PDBsum; 4V8Q; -. DR AlphaFoldDB; Q5SHN6; -. DR EMDB; EMD-1122; -. DR SMR; Q5SHN6; -. DR IntAct; Q5SHN6; 50. DR EnsemblBacteria; BAD71517; BAD71517; BAD71517. DR GeneID; 3167925; -. DR KEGG; ttj:TTHA1694; -. DR PATRIC; fig|300852.9.peg.1664; -. DR eggNOG; COG0050; Bacteria. DR HOGENOM; CLU_007265_0_1_0; -. DR PhylomeDB; Q5SHN6; -. DR EvolutionaryTrace; Q5SHN6; -. DR Proteomes; UP000000532; 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:0003723; F:RNA binding; IEA:UniProtKB-KW. 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 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Elongation factor; GTP-binding; KW Nucleotide-binding; Phosphoprotein; Protein biosynthesis; KW Reference proteome; RNA-binding. FT INIT_MET 1 FT /note="Removed" FT CHAIN 2..406 FT /note="Elongation factor Tu-A" FT /id="PRO_0000091423" FT DOMAIN 10..215 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:0000269|PubMed:11278992, FT ECO:0007744|PDB:1HA3, ECO:0007744|PDB:2C78, FT ECO:0007744|PDB:4V5G, ECO:0007744|PDB:4V5P, FT ECO:0007744|PDB:4V5Q, ECO:0007744|PDB:4V5R, FT ECO:0007744|PDB:4V5S, ECO:0007744|PDB:4V8Q" FT BINDING 82..86 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0007744|PDB:2C78" FT BINDING 137..140 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000269|PubMed:11278992, FT ECO:0007744|PDB:1HA3, ECO:0007744|PDB:2C78, FT ECO:0007744|PDB:4V5G, ECO:0007744|PDB:4V5P, FT ECO:0007744|PDB:4V5Q, ECO:0007744|PDB:4V5R, FT ECO:0007744|PDB:4V5S, ECO:0007744|PDB:4V8Q" FT MOD_RES 395 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P0CE47" FT CONFLICT 380 FT /note="A -> G (in Ref. 1; CAA29397)" FT /evidence="ECO:0000305" FT STRAND 12..18 FT /evidence="ECO:0007829|PDB:2C78" FT HELIX 25..38 FT /evidence="ECO:0007829|PDB:2C78" FT HELIX 48..51 FT /evidence="ECO:0007829|PDB:2C78" FT HELIX 55..60 FT /evidence="ECO:0007829|PDB:2C78" FT STRAND 67..72 FT /evidence="ECO:0007829|PDB:2C78" FT STRAND 77..82 FT /evidence="ECO:0007829|PDB:2C78" FT HELIX 87..89 FT /evidence="ECO:0007829|PDB:2C78" FT HELIX 90..97 FT /evidence="ECO:0007829|PDB:2C78" FT STRAND 101..108 FT /evidence="ECO:0007829|PDB:2C78" FT TURN 109..111 FT /evidence="ECO:0007829|PDB:2C78" FT HELIX 115..126 FT /evidence="ECO:0007829|PDB:2C78" FT STRAND 132..137 FT /evidence="ECO:0007829|PDB:2C78" FT HELIX 139..141 FT /evidence="ECO:0007829|PDB:2C78" FT HELIX 145..161 FT /evidence="ECO:0007829|PDB:2C78" FT TURN 166..168 FT /evidence="ECO:0007829|PDB:2C78" FT STRAND 171..173 FT /evidence="ECO:0007829|PDB:2C78" FT HELIX 176..185 FT /evidence="ECO:0007829|PDB:2C78" FT HELIX 195..210 FT /evidence="ECO:0007829|PDB:2C78" FT STRAND 223..225 FT /evidence="ECO:0007829|PDB:2C78" FT STRAND 228..232 FT /evidence="ECO:0007829|PDB:2C78" FT TURN 233..235 FT /evidence="ECO:0007829|PDB:2C78" FT STRAND 236..242 FT /evidence="ECO:0007829|PDB:2C78" FT STRAND 245..249 FT /evidence="ECO:0007829|PDB:2C78" FT STRAND 253..262 FT /evidence="ECO:0007829|PDB:2C78" FT STRAND 264..273 FT /evidence="ECO:0007829|PDB:2C78" FT STRAND 276..282 FT /evidence="ECO:0007829|PDB:2C78" FT STRAND 286..293 FT /evidence="ECO:0007829|PDB:2C78" FT TURN 296..298 FT /evidence="ECO:0007829|PDB:2C78" FT STRAND 304..307 FT /evidence="ECO:0007829|PDB:2C78" FT STRAND 310..323 FT /evidence="ECO:0007829|PDB:2C78" FT HELIX 326..328 FT /evidence="ECO:0007829|PDB:2C78" FT STRAND 342..345 FT /evidence="ECO:0007829|PDB:2C78" FT STRAND 348..355 FT /evidence="ECO:0007829|PDB:2C78" FT STRAND 368..381 FT /evidence="ECO:0007829|PDB:2C78" FT STRAND 386..391 FT /evidence="ECO:0007829|PDB:2C78" FT STRAND 394..404 FT /evidence="ECO:0007829|PDB:2C78" SQ SEQUENCE 406 AA; 44782 MW; BA597518358269E4 CRC64; MAKGEFVRTK PHVNVGTIGH VDHGKTTLTA ALTYVAAAEN PNVEVKDYGD IDKAPEERAR GITINTAHVE YETAKRHYSH VDCPGHADYI KNMITGAAQM DGAILVVSAA DGPMPQTREH ILLARQVGVP YIVVFMNKVD MVDDPELLDL VEMEVRDLLN QYEFPGDEVP VIRGSALLAL EQMHRNPKTR RGENEWVDKI WELLDAIDEY IPTPVRDVDK PFLMPVEDVF TITGRGTVAT GRIERGKVKV GDEVEIVGLA PETRRTVVTG VEMHRKTLQE GIAGDNVGVL LRGVSREEVE RGQVLAKPGS ITPHTKFEAS VYVLKKEEGG RHTGFFSGYR PQFYFRTTDV TGVVQLPPGV EMVMPGDNVT FTVELIKPVA LEEGLRFAIR EGGRTVGAGV VTKILE //