ID   EFTU1_STRRA             Reviewed;         397 AA.
AC   P29542;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Elongation factor Tu-1 {ECO:0000255|HAMAP-Rule:MF_00118};
DE            Short=EF-Tu-1 {ECO:0000255|HAMAP-Rule:MF_00118};
GN   Name=tuf1 {ECO:0000255|HAMAP-Rule:MF_00118};
OS   Streptomyces ramocissimus.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1925;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8012612; DOI=10.1099/00221287-140-4-983;
RA   Vijgenboom E., Woudt L.P., Heinstra P.W.H., Rietveld K., van Haarlem J.,
RA   van Wezel G.P., Shochat S., Bosch L.;
RT   "Three tuf-like genes in the kirromycin producer Streptomyces
RT   ramocissimus.";
RL   Microbiology 140:983-998(1994).
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; X67057; CAA47442.1; -; Genomic_DNA.
DR   PIR; S23908; S23908.
DR   AlphaFoldDB; P29542; -.
DR   SMR; P29542; -.
DR   PRIDE; P29542; -.
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..397
FT                   /note="Elongation factor Tu-1"
FT                   /id="PRO_0000091413"
FT   DOMAIN          10..206
FT                   /note="tr-type G"
FT   REGION          19..26
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          62..66
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          83..86
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          138..141
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          176..178
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         83..87
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT   BINDING         138..141
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
SQ   SEQUENCE   397 AA;  43918 MW;  5442152843D4E306 CRC64;
     MAKAKFERTK PHVNIGTIGH IDHGKTTLTA AITKVLHDAY PDLNEATPFD NIDKAPEERQ
     RGITISIAHV EYQTEARHYA HVDCPGHADY IKNMITGAAQ MDGAILVVAA TDGPMPQTKE
     HVLLARQVGV PYIVVALNKA DMVDDEEIME LVELEVRELL SEYEFPGDDL PVVRVSALKA
     LEGDAQWTQS VLDLMKAVDE SIPEPERDVD KPFLMPIEDV FTITGRGTVV TGRIERGVLK
     VNETVDIIGI KTEKTTTTVT GIEMFRKLLD EGQAGENVGL LLRGIKREDV ERGQVIIKPG
     SVTPHTEFEA QAYILSKDEG GRHTPFFNNY RPQFYFRTTD VTGVVHLPEG TEMVMPGDNT
     EMRVELIQPV AMEEGLKFAI REGGRTVGAG QVTKIVK