ID   EFTU_AQUPY              Reviewed;         405 AA.
AC   O50293;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 90.
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};
OS   Aquifex pyrophilus.
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=2714;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DSM 6858 / JCM 9492 / Kol5A;
RX   PubMed=9588802; DOI=10.1002/elps.1150190416;
RA   Ludwig W., Strunk O., Klugbauer S., Klugbauer N., Weizenegger M.,
RA   Neumaier J., Bachleitner M., Schleifer K.H.;
RT   "Bacterial phylogeny based on comparative sequence analysis.";
RL   Electrophoresis 19:554-568(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; Y15787; CAA75781.1; -; Genomic_DNA.
DR   AlphaFoldDB; O50293; -.
DR   SMR; O50293; -.
DR   PRIDE; O50293; -.
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   3: Inferred from homology;
KW   Cytoplasm; Elongation factor; GTP-binding; Nucleotide-binding;
KW   Protein biosynthesis.
FT   CHAIN           1..405
FT                   /note="Elongation factor Tu"
FT                   /id="PRO_0000091285"
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"
SQ   SEQUENCE   405 AA;  44672 MW;  012A9CD9C60AA16C CRC64;
     MAKEKFERTK EHVNVGTIGH VDHGKSTLTS AITCVLAAGL VEGGKAKCFK YEEIDKAPEE
     KERGITINIT HVEYETAKRH YAHVDCPGHA DYIKNMITGA AQMDGAILVV SAADGPMPQT
     REHVLLARQV NVPYIVVFMN KCDMVDDEEL LELVELEVRE LLSKYEYPGD EVPVIRGSAL
     GALQELEQNS PGKWVGSIKE LLNAMDEYIP TPEREVDKPF LMPIEDVFSI SGRGTVVTGR
     VERGVLRPGD EVEIVGLREE PLKTVATSIE MFRKVLDEAL PGDNIGVLLR GVGKDDVERG
     QVLAQPGSVK AHRKFRAQVY VLSKEEGGRH TPFFVNYRPQ FYFRTADVTG TVVKLPEGVE
     MVMPGDNVEL EVELIAPVAL EEGLRFAIRE GGRTVGAGVV TKILD