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   27-MAR-2024, entry version 131.
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};
GN   OrderedLocusNames=TTHA0251;
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=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   DrugBank; DB04124; Aurodox.
DR   DrugBank; DB04315; Guanosine-5'-Diphosphate.
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   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   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.
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
//