EFTU2_THET8
ID EFTU2_THET8 Reviewed; 406 AA.
AC P60339; P07157; Q5SLP2;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Elongation factor Tu-B {ECO:0000255|HAMAP-Rule:MF_00118};
DE Short=EF-Tu-B {ECO:0000255|HAMAP-Rule:MF_00118};
GN Name=tufB {ECO:0000255|HAMAP-Rule:MF_00118}; OrderedLocusNames=TTHA0251;
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=1908798; DOI=10.1016/0014-5793(91)81011-v;
RA Satoh M., Tanaka T., Kushiro A., Hakoshima T., Tomita K.;
RT "Molecular cloning, nucleotide sequence and expression of the tufB gene
RT encoding elongation factor Tu from Thermus thermophilus HB8.";
RL FEBS Lett. 288:98-100(1991).
RN [2]
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 [3]
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).
CC -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-
CC tRNA to the A-site of ribosomes during protein biosynthesis.
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. {ECO:0000255|HAMAP-Rule:MF_00118}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- PTM: Phosphorylated on a threonine. {ECO:0000250|UniProtKB:Q5SHN6}.
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; X61957; CAA43956.1; -; Genomic_DNA.
DR EMBL; AP008226; BAD70074.1; -; Genomic_DNA.
DR PIR; S00229; S00229.
DR PIR; S17146; S17146.
DR RefSeq; WP_011227805.1; NC_006461.1.
DR RefSeq; YP_143517.1; NC_006461.1.
DR PDB; 2C77; X-ray; 1.60 A; A=2-406.
DR PDB; 2P8W; EM; 11.30 A; S=36-70.
DR PDB; 2P8X; EM; 9.70 A; S=36-70.
DR PDB; 2P8Z; EM; 8.90 A; S=36-70.
DR PDB; 3DWU; EM; 12.60 A; A=21-66.
DR PDB; 4V5L; X-ray; 3.10 A; AZ=2-406.
DR PDB; 4V68; EM; 6.40 A; AZ=2-406.
DR PDBsum; 2C77; -.
DR PDBsum; 2P8W; -.
DR PDBsum; 2P8X; -.
DR PDBsum; 2P8Z; -.
DR PDBsum; 3DWU; -.
DR PDBsum; 4V5L; -.
DR PDBsum; 4V68; -.
DR AlphaFoldDB; P60339; -.
DR SMR; P60339; -.
DR STRING; 300852.55771633; -.
DR DrugBank; DB04124; Aurodox.
DR DrugBank; DB04315; Guanosine-5'-Diphosphate.
DR PRIDE; P60339; -.
DR EnsemblBacteria; BAD70074; BAD70074; BAD70074.
DR GeneID; 3168327; -.
DR KEGG; ttj:TTHA0251; -.
DR PATRIC; fig|300852.9.peg.251; -.
DR eggNOG; COG0050; Bacteria.
DR HOGENOM; CLU_007265_0_1_0; -.
DR OMA; EGDKEWG; -.
DR PhylomeDB; P60339; -.
DR EvolutionaryTrace; P60339; -.
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: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.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..406
FT /note="Elongation factor Tu-B"
FT /id="PRO_0000091424"
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:0000255|HAMAP-Rule:MF_00118"
FT BINDING 82..86
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT BINDING 137..140
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT MOD_RES 395
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P0CE47"
FT STRAND 12..18
FT /evidence="ECO:0007829|PDB:2C77"
FT HELIX 25..39
FT /evidence="ECO:0007829|PDB:2C77"
FT HELIX 48..51
FT /evidence="ECO:0007829|PDB:2C77"
FT HELIX 55..60
FT /evidence="ECO:0007829|PDB:2C77"
FT STRAND 67..72
FT /evidence="ECO:0007829|PDB:2C77"
FT STRAND 77..82
FT /evidence="ECO:0007829|PDB:2C77"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:2C77"
FT HELIX 90..97
FT /evidence="ECO:0007829|PDB:2C77"
FT STRAND 101..108
FT /evidence="ECO:0007829|PDB:2C77"
FT TURN 109..111
FT /evidence="ECO:0007829|PDB:2C77"
FT HELIX 115..127
FT /evidence="ECO:0007829|PDB:2C77"
FT STRAND 132..137
FT /evidence="ECO:0007829|PDB:2C77"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:2C77"
FT HELIX 145..161
FT /evidence="ECO:0007829|PDB:2C77"
FT TURN 166..168
FT /evidence="ECO:0007829|PDB:2C77"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:2C77"
FT HELIX 176..185
FT /evidence="ECO:0007829|PDB:2C77"
FT HELIX 195..210
FT /evidence="ECO:0007829|PDB:2C77"
FT STRAND 223..225
FT /evidence="ECO:0007829|PDB:2C77"
FT STRAND 228..232
FT /evidence="ECO:0007829|PDB:2C77"
FT TURN 233..235
FT /evidence="ECO:0007829|PDB:2C77"
FT STRAND 236..242
FT /evidence="ECO:0007829|PDB:2C77"
FT STRAND 245..248
FT /evidence="ECO:0007829|PDB:2C77"
FT STRAND 253..262
FT /evidence="ECO:0007829|PDB:2C77"
FT STRAND 264..273
FT /evidence="ECO:0007829|PDB:2C77"
FT STRAND 286..293
FT /evidence="ECO:0007829|PDB:2C77"
FT HELIX 296..298
FT /evidence="ECO:0007829|PDB:2C77"
FT STRAND 304..307
FT /evidence="ECO:0007829|PDB:2C77"
FT STRAND 310..323
FT /evidence="ECO:0007829|PDB:2C77"
FT HELIX 326..328
FT /evidence="ECO:0007829|PDB:2C77"
FT STRAND 342..345
FT /evidence="ECO:0007829|PDB:2C77"
FT STRAND 348..355
FT /evidence="ECO:0007829|PDB:2C77"
FT STRAND 368..381
FT /evidence="ECO:0007829|PDB:2C77"
FT STRAND 386..391
FT /evidence="ECO:0007829|PDB:2C77"
FT STRAND 394..404
FT /evidence="ECO:0007829|PDB:2C77"
SQ SEQUENCE 406 AA; 44782 MW; 38D5E2D8F1B645DD CRC64;
MAKGEFIRTK PHVNVGTIGH VDHGKTTLTA ALTFVTAAEN PNVEVKDYGD IDKAPEERAR
GITINTAHVE YETAKRHYSH VDCPGHADYI KNMITGAAQM DGAILVVSAA DGPMPQTREH
ILLARQVGVP YIVVFMNKVD MVDDPELLDL VEMEVRDLLN QYEFPGDEVP VIRGSALLAL
EQMHRNPKTR RGENEWVDKI WELLDAIDEY IPTPVRDVDK PFLMPVEDVF TITGRGTVAT
GRIERGKVKV GDEVEIVGLA PETRKTVVTG VEMHRKTLQE GIAGDNVGVL LRGVSREEVE
RGQVLAKPGS ITPHTKFEAS VYVLKKEEGG RHTGFFSGYR PQFYFRTTDV TGVVQLPPGV
EMVMPGDNVT FTVELIKPVA LEEGLRFAIR EGGRTVGAGV VTKILE
