ID   EFTU3_STRRA             Reviewed;         389 AA.
AC   P29544;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Elongation factor Tu-3 {ECO:0000255|HAMAP-Rule:MF_00118};
DE            Short=EF-Tu-3 {ECO:0000255|HAMAP-Rule:MF_00118};
GN   Name=tuf3 {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; X67059; CAA47444.1; -; Genomic_DNA.
DR   PIR; S25547; S25547.
DR   AlphaFoldDB; P29544; -.
DR   SMR; P29544; -.
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   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; 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..389
FT                   /note="Elongation factor Tu-3"
FT                   /id="PRO_0000091415"
FT   DOMAIN          10..203
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          173..175
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"
SQ   SEQUENCE   389 AA;  41171 MW;  BDCA1F1C1184A61F CRC64;
     MSKTAYVRTK PHLNIGTMGH VDHGKTTLTA AITKVLAERG SGTFVPFDRI DRAPEEAARG
     ITINIAHVEY ETDTRHYAHV DMPGHADYVK NMVTGAAQLD GAILVVSALD GIMPQTAEHV
     LLARQVGVDH IVVALNKADA GDEELTDLVE LEVRDLLSEH GYGGDGAPVV RVSGLKALEG
     DPKWTASIEA LLDAVDTYVP MPERYVDAPF LLPVENVLTI TGRGTVVTGA VERGTVRVGN
     RVEVLGAGLE TVVTGLETFG KPMDEAQAGD NVALLLRGVP RDAVRRGHVV AAPGSVVPRS
     RFSAQVYVLS AREGGRTTPV TSGYRPQFYI RTADVVGDVD LGEVGVARPG ETVSMIVELG
     REVPLEPGLG FAIREGGRTV GAGTVTALV