EFTU_THEAQ
ID EFTU_THEAQ Reviewed; 406 AA.
AC Q01698;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Elongation factor Tu {ECO:0000255|HAMAP-Rule:MF_00118};
DE Short=EF-Tu {ECO:0000255|HAMAP-Rule:MF_00118};
GN Name=tuf {ECO:0000255|HAMAP-Rule:MF_00118}; Synonyms=tufA;
OS Thermus aquaticus.
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=271;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-10.
RC STRAIN=EP 00276;
RX PubMed=1499561; DOI=10.1111/j.1432-1033.1992.tb17115.x;
RA Voss R.H., Hartmann R.K., Lippmann C., Alexander C., Jahn O., Erdmann V.;
RT "Sequence of the tufA gene encoding elongation factor EF-Tu from Thermus
RT aquaticus and overproduction of the protein in Escherichia coli.";
RL Eur. J. Biochem. 207:839-846(1992).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RC STRAIN=ATCC 25104 / DSM 625 / JCM 10724 / NBRC 103206 / NCIMB 11243 / YT-1;
RX PubMed=8069622; DOI=10.1016/0969-2126(93)90007-4;
RA Kjeldgaard M., Nissen P., Thirup S., Nyborg J.;
RT "The crystal structure of elongation factor EF-Tu from Thermus aquaticus in
RT the GTP conformation.";
RL Structure 1:35-50(1993).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
RC STRAIN=ATCC 25104 / DSM 625 / JCM 10724 / NBRC 103206 / NCIMB 11243 / YT-1;
RX PubMed=7491491; DOI=10.1126/science.270.5241.1464;
RA Nissen P., Kjeldgaard M., Thirup S., Polekhina G., Reshetnikova L.,
RA Clark B.F.C., Nyborg J.;
RT "Crystal structure of the ternary complex of Phe-tRNAPhe, EF-Tu, and a GTP
RT analog.";
RL Science 270:1464-1472(1995).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
RX PubMed=8939739; DOI=10.1016/s0969-2126(96)00122-0;
RA Polekhina G., Thirup S., Kjeldgaard M., Nissen P., Lippmann C., Nyborg J.;
RT "Helix unwinding in the effector region of elongation factor EF-Tu-GDP.";
RL Structure 4:1141-1151(1996).
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 -!- 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; X66322; CAA46998.1; -; Genomic_DNA.
DR PIR; S29293; S29293.
DR RefSeq; WP_003043841.1; NZ_LHCI01000106.1.
DR PDB; 1B23; X-ray; 2.60 A; P=2-406.
DR PDB; 1EFT; X-ray; 2.50 A; A=2-406.
DR PDB; 1MJ1; EM; 13.00 A; A=2-406.
DR PDB; 1OB5; X-ray; 3.10 A; A/C/E=2-406.
DR PDB; 1TTT; X-ray; 2.70 A; A/B/C=2-406.
DR PDB; 1TUI; X-ray; 2.70 A; A/B/C=2-406.
DR PDBsum; 1B23; -.
DR PDBsum; 1EFT; -.
DR PDBsum; 1MJ1; -.
DR PDBsum; 1OB5; -.
DR PDBsum; 1TTT; -.
DR PDBsum; 1TUI; -.
DR AlphaFoldDB; Q01698; -.
DR SMR; Q01698; -.
DR DrugBank; DB08185; 2-METHYLTHIO-N6-ISOPENTENYL-ADENOSINE-5'-MONOPHOSPHATE.
DR DrugBank; DB04315; Guanosine-5'-Diphosphate.
DR PRIDE; Q01698; -.
DR BRENDA; 3.6.5.3; 6334.
DR EvolutionaryTrace; Q01698; -.
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; Direct protein sequencing; Elongation factor;
KW GTP-binding; Nucleotide-binding; Protein biosynthesis.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1499561"
FT CHAIN 2..406
FT /note="Elongation factor Tu"
FT /id="PRO_0000091420"
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 STRAND 12..18
FT /evidence="ECO:0007829|PDB:1EFT"
FT HELIX 25..37
FT /evidence="ECO:0007829|PDB:1EFT"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:1OB5"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:1EFT"
FT HELIX 55..60
FT /evidence="ECO:0007829|PDB:1EFT"
FT STRAND 67..72
FT /evidence="ECO:0007829|PDB:1EFT"
FT STRAND 77..82
FT /evidence="ECO:0007829|PDB:1EFT"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:1EFT"
FT HELIX 90..97
FT /evidence="ECO:0007829|PDB:1EFT"
FT STRAND 101..108
FT /evidence="ECO:0007829|PDB:1EFT"
FT TURN 109..111
FT /evidence="ECO:0007829|PDB:1EFT"
FT HELIX 115..125
FT /evidence="ECO:0007829|PDB:1EFT"
FT TURN 126..128
FT /evidence="ECO:0007829|PDB:1EFT"
FT STRAND 132..137
FT /evidence="ECO:0007829|PDB:1EFT"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:1EFT"
FT HELIX 147..160
FT /evidence="ECO:0007829|PDB:1EFT"
FT TURN 161..163
FT /evidence="ECO:0007829|PDB:1EFT"
FT TURN 166..168
FT /evidence="ECO:0007829|PDB:1EFT"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:1EFT"
FT HELIX 176..185
FT /evidence="ECO:0007829|PDB:1EFT"
FT TURN 191..193
FT /evidence="ECO:0007829|PDB:1EFT"
FT HELIX 195..210
FT /evidence="ECO:0007829|PDB:1EFT"
FT STRAND 218..220
FT /evidence="ECO:0007829|PDB:1EFT"
FT STRAND 223..232
FT /evidence="ECO:0007829|PDB:1EFT"
FT TURN 233..235
FT /evidence="ECO:0007829|PDB:1EFT"
FT STRAND 236..242
FT /evidence="ECO:0007829|PDB:1EFT"
FT STRAND 245..249
FT /evidence="ECO:0007829|PDB:1EFT"
FT STRAND 253..256
FT /evidence="ECO:0007829|PDB:1EFT"
FT STRAND 258..262
FT /evidence="ECO:0007829|PDB:1EFT"
FT STRAND 264..273
FT /evidence="ECO:0007829|PDB:1EFT"
FT STRAND 276..282
FT /evidence="ECO:0007829|PDB:1EFT"
FT STRAND 286..291
FT /evidence="ECO:0007829|PDB:1EFT"
FT TURN 296..298
FT /evidence="ECO:0007829|PDB:1B23"
FT STRAND 304..307
FT /evidence="ECO:0007829|PDB:1EFT"
FT TURN 308..310
FT /evidence="ECO:0007829|PDB:1B23"
FT STRAND 314..323
FT /evidence="ECO:0007829|PDB:1EFT"
FT HELIX 326..328
FT /evidence="ECO:0007829|PDB:1EFT"
FT STRAND 342..345
FT /evidence="ECO:0007829|PDB:1EFT"
FT STRAND 348..355
FT /evidence="ECO:0007829|PDB:1EFT"
FT STRAND 368..379
FT /evidence="ECO:0007829|PDB:1EFT"
FT STRAND 386..391
FT /evidence="ECO:0007829|PDB:1EFT"
FT STRAND 394..404
FT /evidence="ECO:0007829|PDB:1EFT"
SQ SEQUENCE 406 AA; 44814 MW; A5E642800075E5D1 CRC64;
MAKGEFIRTK PHVNVGTIGH VDHGKTTLTA ALTYVAAAEN PNVEVKDYGD IDKAPEERAR
GITINTAHVE YETAKRHYSH VDCPGHADYI KNMITGAAQM DGAILVVSAA DGPMPQTREH
ILLARQVGVP YIVVFMNKVD MVDDPELLDL VEMEVRDLLN QYEFPGDEVP VIRGSALLAL
EEMHKNPKTK RGENEWVDKI WELLDAIDEY IPTPVRDVDK PFLMPVEDVF TITGRGTVAT
GRIERGKVKV GDEVEIVGLA PETRKTVVTG VEMHRKTLQE GIAGDNVGLL LRGVSREEVE
RGQVLAKPGS ITPHTKFEAS VYILKKEEGG RHTGFFTGYR PQFYFRTTDV TGVVRLPQGV
EMVMPGDNVT FTVELIKPVA LEEGLRFAIR EGGRTVGAGV VTKILE
