ID   EFTU_AQUAE              Reviewed;         405 AA.
AC   O66429; O67755;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 140.
DE   RecName: Full=Elongation factor Tu {ECO:0000255|HAMAP-Rule:MF_00118};
DE            Short=EF-Tu {ECO:0000255|HAMAP-Rule:MF_00118};
GN   Name=tufA {ECO:0000255|HAMAP-Rule:MF_00118}; OrderedLocusNames=aq_005;
GN   and
GN   Name=tufB {ECO:0000255|HAMAP-Rule:MF_00118}; OrderedLocusNames=aq_1928;
OS   Aquifex aeolicus (strain VF5).
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=224324;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5;
RX   PubMed=9537320; DOI=10.1038/32831;
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL   Nature 392:353-358(1998).
CC   -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-
CC       tRNA to the A-site of ribosomes during protein biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00118}.
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00118}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00118}.
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; AE000657; AAC06403.1; -; Genomic_DNA.
DR   EMBL; AE000657; AAC07714.1; -; Genomic_DNA.
DR   PIR; B70300; B70300.
DR   PIR; G70465; G70465.
DR   RefSeq; NP_212987.1; NC_000918.1.
DR   RefSeq; NP_214323.1; NC_000918.1.
DR   RefSeq; WP_010879925.1; NC_000918.1.
DR   AlphaFoldDB; O66429; -.
DR   SMR; O66429; -.
DR   STRING; 224324.aq_005; -.
DR   EnsemblBacteria; AAC06403; AAC06403; aq_005.
DR   EnsemblBacteria; AAC07714; AAC07714; aq_1928.
DR   KEGG; aae:aq_005; -.
DR   KEGG; aae:aq_1928; -.
DR   PATRIC; fig|224324.8.peg.1493; -.
DR   eggNOG; COG0050; Bacteria.
DR   HOGENOM; CLU_007265_0_1_0; -.
DR   InParanoid; O66429; -.
DR   OMA; EGDKEWG; -.
DR   OrthoDB; 621774at2; -.
DR   Proteomes; UP000000798; 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; IBA:GO_Central.
DR   GO; GO:0006414; P:translational elongation; IBA:GO_Central.
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   3: Inferred from homology;
KW   Cytoplasm; Elongation factor; GTP-binding; Nucleotide-binding;
KW   Protein biosynthesis; Reference proteome.
FT   CHAIN           1..405
FT                   /note="Elongation factor Tu"
FT                   /id="PRO_0000091284"
FT   DOMAIN          10..213
FT                   /note="tr-type G"
FT   REGION          19..26
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          64..68
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          85..88
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          140..143
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          178..180
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         85..89
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT   BINDING         140..143
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT   VARIANT         140
FT                   /note="N -> S (in TufB)"
FT   VARIANT         294
FT                   /note="K -> R (in TufB)"
SQ   SEQUENCE   405 AA;  44743 MW;  FBE083116BE15F1D CRC64;
     MAKEKFERTK EHVNVGTIGH VDHGKSTLTS AITCVLAAGL VEGGKAKCFK YEEIDKAPEE
     KERGITINIT HVEYETAKRH YAHVDCPGHA DYIKNMITGA AQMDGAILVV SAADGPMPQT
     REHVLLARQV NVPYIVVFMN KCDMVDDEEL LELVELEVRE LLSKYEYPGD EVPVIRGSAL
     GALQELEQNS PGKWVESIKE LLNAMDEYIP TPQREVDKPF LMPIEDVFSI SGRGTVVTGR
     VERGVLRPGD EVEIVGLREE PLKTVATSIE MFRKVLDEAL PGDNIGVLLR GVGKDDVERG
     QVLAQPGSVK AHKRFRAQVY VLSKEEGGRH TPFFVNYRPQ FYFRTADVTG TVVKLPEGVE
     MVMPGDNVEL EVELIAPVAL EEGLRFAIRE GGRTVGAGVV TKILD