EFTU1_THET8
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 03-AUG-2022, entry version 121.
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; Deinococcus-Thermus; 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}.
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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 SMR; Q5SHN6; -.
DR IntAct; Q5SHN6; 50.
DR STRING; 300852.55773076; -.
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 OMA; ERPHCNV; -.
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 Gene3D; 3.40.50.300; -; 1.
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 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; SSF50447; SSF50447; 1.
DR SUPFAM; SSF50465; SSF50465; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00485; EF-Tu; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 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
