ID   EFTU_THIDL              Reviewed;         396 AA.
AC   P42481; O50566;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 100.
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   Thiomonas delicata (Thiomonas cuprina).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Thiomonas.
OX   NCBI_TaxID=364030;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=HOE5;
RX   PubMed=8085791; DOI=10.1007/bf00873088;
RA   Ludwig W., Neumaier J., Klugbauer N., Brockmann E., Roller C.,
RA   Klugbauer S., Reetz K., Schachtner I., Ludvigsen A., Bachleitner M.,
RA   Fischer U., Schleifer K.H.;
RT   "Phylogenetic relationships of Bacteria based on comparative sequence
RT   analysis of elongation factor Tu and ATP-synthase beta-subunit genes.";
RL   Antonie Van Leeuwenhoek 64:285-305(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DSM 5495 / NBRC 102094 / Hoe5;
RA   Moreira D., Amils R.;
RT   "The str operon from the chemolithotrophic bacterium Thiobacillus
RT   cuprinus.";
RL   Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
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; X76871; CAA54198.1; -; Genomic_DNA.
DR   EMBL; U78300; AAB87734.1; -; Genomic_DNA.
DR   AlphaFoldDB; P42481; -.
DR   SMR; P42481; -.
DR   PRIDE; P42481; -.
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..396
FT                   /note="Elongation factor Tu"
FT                   /id="PRO_0000091427"
FT   DOMAIN          10..206
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        109
FT                   /note="A -> G (in Ref. 2; AAB87734)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        383
FT                   /note="G -> A (in Ref. 2; AAB87734)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        387..388
FT                   /note="GA -> AG (in Ref. 2; AAB87734)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   396 AA;  43026 MW;  06D557D04ADB44AB CRC64;
     MAKSKFERTK PHVNVGTIGH VDHGKTTLTA AITTVLSSKF GGEAKAYDQI DAAPEEKARG
     ITINTAHVEY ETANRHYAHV DCPGHADYVK NMITGAAQMD GAILVVSAAD GPMPQTREHI
     LLARQVGVPY IIVFLNKCDM VDDAELLELV EMEVRELLSK YDFPGDDTPI IKGSAKLALE
     GDKGELGEGA ILKLAEALDT YIPTPERAVD GAFLMPVEDV FSISGRGTVV TGRVERGIIK
     VGEEIEIVGL KPTLKTTCTG VEMFRKLLDQ GQAGDNVGIL LRGTKREEVE RGQVLCKPGS
     IKPHTHFTAE VYVLSKDEGG RHTPFFNNYR PQFYFRTTDV TGAIELPKDK EMVMPGDNVS
     ITVKLIAPIA MEEGLRFAIR EGGRTVGAGV VAKIIE