EFTU1_THETH
ID EFTU1_THETH Reviewed; 406 AA.
AC P60338; P07157;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 104.
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;
OS Thermus thermophilus.
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=274;
RN [1]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
RX PubMed=8371755; DOI=10.1038/365126a0;
RA Berchtold H., Reshetnikova L., Reiser C.O.A., Schirmer N.K., Sprinzl M.,
RA Hilgenfeld R.;
RT "Crystal structure of active elongation factor Tu reveals major domain
RT rearrangements.";
RL Nature 365:126-132(1993).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF COMPLEX WITH EF-TS.
RX PubMed=9253415; DOI=10.1038/nsb0897-650;
RA Wang Y., Jiang Y., Meyering-Voss M., Sprinzl M., Sigler P.B.;
RT "Crystal structure of the EF-Tu.EF-Ts complex from Thermus thermophilus.";
RL Nat. Struct. Biol. 4:650-656(1997).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
RX PubMed=10368282; DOI=10.1016/s0969-2126(99)80021-5;
RA Nissen P., Thirup S., Kjeldgaard M., Nyborg J.;
RT "The crystal structure of Cys-tRNACys-EF-Tu-GDPNP reveals general and
RT specific features in the ternary complex and in tRNA.";
RL Structure 7:143-156(1999).
CC -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-
CC tRNA to the A-site of ribosomes during protein biosynthesis.
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00118}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- PTM: Phosphorylated on a threonine. {ECO:0000250}.
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 -!- CAUTION: The sequence shown here has been extracted from PDB entry
CC 1EXM. {ECO:0000305}.
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 PIR; S00229; S00229.
DR PIR; S17146; S17146.
DR RefSeq; WP_011228847.1; NC_006461.1.
DR PDB; 1AIP; X-ray; 3.00 A; A/B/E/F=2-406.
DR PDB; 1EXM; X-ray; 1.70 A; A=2-406.
DR PDB; 4H9G; X-ray; 1.93 A; A=2-406.
DR PDB; 4LBV; X-ray; 2.03 A; A=3-406.
DR PDB; 4LBW; X-ray; 1.74 A; A=3-406.
DR PDB; 4LBY; X-ray; 2.69 A; A=3-406.
DR PDB; 4LBZ; X-ray; 2.22 A; A=3-406.
DR PDB; 4LC0; X-ray; 2.22 A; A=3-406.
DR PDBsum; 1AIP; -.
DR PDBsum; 1EXM; -.
DR PDBsum; 4H9G; -.
DR PDBsum; 4LBV; -.
DR PDBsum; 4LBW; -.
DR PDBsum; 4LBY; -.
DR PDBsum; 4LBZ; -.
DR PDBsum; 4LC0; -.
DR AlphaFoldDB; P60338; -.
DR SMR; P60338; -.
DR DIP; DIP-61168N; -.
DR IntAct; P60338; 1.
DR GeneID; 3167925; -.
DR BRENDA; 3.6.5.3; 2305.
DR EvolutionaryTrace; P60338; -.
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 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.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..406
FT /note="Elongation factor Tu-A"
FT /id="PRO_0000091422"
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 BINDING 82..86
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT BINDING 137..140
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT MOD_RES 395
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT STRAND 12..18
FT /evidence="ECO:0007829|PDB:1EXM"
FT HELIX 21..23
FT /evidence="ECO:0007829|PDB:1AIP"
FT HELIX 25..39
FT /evidence="ECO:0007829|PDB:1EXM"
FT HELIX 48..51
FT /evidence="ECO:0007829|PDB:1EXM"
FT HELIX 55..60
FT /evidence="ECO:0007829|PDB:1EXM"
FT STRAND 67..72
FT /evidence="ECO:0007829|PDB:1EXM"
FT STRAND 77..82
FT /evidence="ECO:0007829|PDB:1EXM"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:1EXM"
FT HELIX 90..97
FT /evidence="ECO:0007829|PDB:1EXM"
FT STRAND 101..108
FT /evidence="ECO:0007829|PDB:1EXM"
FT TURN 109..111
FT /evidence="ECO:0007829|PDB:1EXM"
FT HELIX 115..126
FT /evidence="ECO:0007829|PDB:1EXM"
FT STRAND 132..137
FT /evidence="ECO:0007829|PDB:1EXM"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:1EXM"
FT HELIX 145..161
FT /evidence="ECO:0007829|PDB:1EXM"
FT TURN 166..168
FT /evidence="ECO:0007829|PDB:1EXM"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:1EXM"
FT HELIX 176..185
FT /evidence="ECO:0007829|PDB:1EXM"
FT TURN 191..193
FT /evidence="ECO:0007829|PDB:4LBW"
FT HELIX 195..210
FT /evidence="ECO:0007829|PDB:1EXM"
FT STRAND 218..220
FT /evidence="ECO:0007829|PDB:4LBW"
FT STRAND 223..225
FT /evidence="ECO:0007829|PDB:1EXM"
FT STRAND 228..232
FT /evidence="ECO:0007829|PDB:1EXM"
FT TURN 233..235
FT /evidence="ECO:0007829|PDB:1EXM"
FT STRAND 236..242
FT /evidence="ECO:0007829|PDB:1EXM"
FT STRAND 245..249
FT /evidence="ECO:0007829|PDB:1EXM"
FT STRAND 253..262
FT /evidence="ECO:0007829|PDB:1EXM"
FT STRAND 264..273
FT /evidence="ECO:0007829|PDB:1EXM"
FT STRAND 279..282
FT /evidence="ECO:0007829|PDB:1EXM"
FT STRAND 286..291
FT /evidence="ECO:0007829|PDB:1EXM"
FT TURN 296..298
FT /evidence="ECO:0007829|PDB:1EXM"
FT STRAND 304..307
FT /evidence="ECO:0007829|PDB:1EXM"
FT STRAND 314..323
FT /evidence="ECO:0007829|PDB:1EXM"
FT HELIX 326..328
FT /evidence="ECO:0007829|PDB:1EXM"
FT STRAND 342..345
FT /evidence="ECO:0007829|PDB:1EXM"
FT STRAND 348..355
FT /evidence="ECO:0007829|PDB:1EXM"
FT STRAND 368..379
FT /evidence="ECO:0007829|PDB:1EXM"
FT STRAND 386..391
FT /evidence="ECO:0007829|PDB:1EXM"
FT STRAND 394..404
FT /evidence="ECO:0007829|PDB:1EXM"
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
