ID   EFTU_THEMA              Reviewed;         400 AA.
AC   P13537;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   03-AUG-2022, entry version 160.
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}; OrderedLocusNames=TM_1502;
OS   Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS   / MSB8).
OC   Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX   NCBI_TaxID=243274;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX   PubMed=2714630; DOI=10.1016/0378-1097(89)90157-2;
RA   Bachleitner M., Ludwig W., Stetter K.O., Schleifer K.H.;
RT   "Nucleotide sequence of the gene coding for the elongation factor Tu from
RT   the extremely thermophilic eubacterium Thermotoga maritima.";
RL   FEMS Microbiol. Lett. 48:115-120(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX   PubMed=10360571; DOI=10.1038/20601;
RA   Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA   Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA   Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA   Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA   Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA   Smith H.O., Venter J.C., Fraser C.M.;
RT   "Evidence for lateral gene transfer between Archaea and Bacteria from
RT   genome sequence of Thermotoga maritima.";
RL   Nature 399:323-329(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-13.
RC   STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX   PubMed=1920450; DOI=10.1007/bf02193628;
RA   Tiboni O., Cantoni R., Creti R., Cammarano P., Sanangelantoni A.M.;
RT   "Phylogenetic depth of Thermotoga maritima inferred from analysis of the
RT   fus gene: amino acid sequence of elongation factor G and organization of
RT   the Thermotoga str operon.";
RL   J. Mol. Evol. 33:142-151(1991).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M27479; AAA27415.1; -; Genomic_DNA.
DR   EMBL; AE000512; AAD36569.1; -; Genomic_DNA.
DR   EMBL; S57688; AAB19929.1; -; Genomic_DNA.
DR   PIR; G72243; G72243.
DR   RefSeq; NP_229302.1; NC_000853.1.
DR   RefSeq; WP_004081839.1; NZ_CP011107.1.
DR   AlphaFoldDB; P13537; -.
DR   SMR; P13537; -.
DR   STRING; 243274.THEMA_06790; -.
DR   EnsemblBacteria; AAD36569; AAD36569; TM_1502.
DR   KEGG; tma:TM1502; -.
DR   eggNOG; COG0050; Bacteria.
DR   InParanoid; P13537; -.
DR   OMA; EGDKEWG; -.
DR   OrthoDB; 621774at2; -.
DR   Proteomes; UP000008183; 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..400
FT                   /note="Elongation factor Tu"
FT                   /id="PRO_0000091421"
FT   DOMAIN          10..208
FT                   /note="tr-type G"
FT   REGION          19..26
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          60..64
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          81..84
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          136..139
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          174..176
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         81..85
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT   BINDING         136..139
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT   CONFLICT        40
FT                   /note="G -> V (in Ref. 1; AAA27415)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   400 AA;  44467 MW;  73F479FE4F69E9A5 CRC64;
     MAKEKFVRTK PHVNVGTIGH IDHGKSTLTA AITKYLSLKG LAQYIPYDQI DKAPEEKARG
     ITINITHVEY ETEKRHYAHI DCPGHADYIK NMITGAAQMD GAILVVAATD GPMPQTREHV
     LLARQVEVPY MIVFINKTDM VDDPELIDLV EMEVRDLLSQ YGYPGDEVPV IRGSALKAVE
     APNDPNHEAY KPIQELLDAM DNYIPDPQRD VDKPFLMPIE DVFSITGRGT VVTGRIERGR
     IRPGDEVEII GLSYEIKKTV VTSVEMFRKE LDEGIAGDNV GCLLRGIDKD EVERGQVLAA
     PGSIKPHKRF KAQIYVLKKE EGGRHTPFTK GYKPQFYIRT ADVTGEIVGL PEGVEMVMPG
     DHVEMEIELI YPVAIEKGQR FAVREGGRTV GAGVVTEVIE