ID   EFTU_MYCMS              Reviewed;         395 AA.
AC   Q6MU81;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 106.
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=MSC_0160;
OS   Mycoplasma mycoides subsp. mycoides SC (strain PG1).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=272632;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PG1;
RX   PubMed=14762060; DOI=10.1101/gr.1673304;
RA   Westberg J., Persson A., Holmberg A., Goesmann A., Lundeberg J.,
RA   Johansson K.-E., Pettersson B., Uhlen M.;
RT   "The genome sequence of Mycoplasma mycoides subsp. mycoides SC type strain
RT   PG1T, the causative agent of contagious bovine pleuropneumonia (CBPP).";
RL   Genome Res. 14:221-227(2004).
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; BX293980; CAE76805.1; -; Genomic_DNA.
DR   RefSeq; NP_975163.1; NC_005364.2.
DR   AlphaFoldDB; Q6MU81; -.
DR   SMR; Q6MU81; -.
DR   STRING; 272632.MSC_0160; -.
DR   EnsemblBacteria; CAE76805; CAE76805; MSC_0160.
DR   KEGG; mmy:MSC_0160; -.
DR   PATRIC; fig|272632.4.peg.169; -.
DR   eggNOG; COG0050; Bacteria.
DR   HOGENOM; CLU_007265_0_0_14; -.
DR   OMA; EGDKEWG; -.
DR   PRO; PR:Q6MU81; -.
DR   Proteomes; UP000001016; 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; 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; Reference proteome.
FT   CHAIN           1..395
FT                   /note="Elongation factor Tu"
FT                   /id="PRO_1000015700"
FT   DOMAIN          10..204
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"
SQ   SEQUENCE   395 AA;  43304 MW;  908B9E1844E6070E CRC64;
     MAKEQFDRSL PHVNIGTIGH VDHGKTTLTA AITKVLSEQG NAEFKDYANI DNAPEERERG
     ITINTAHVEY KTANRHYAHV DCPGHADYVK NMITGAAQMD GAILVVAATD GPMPQTREHI
     LLSRQVGVPK IVVFLNKCDM VEDDEMIDLV EMEIRDLLTE YDFDGEGAPV IRGSALGALN
     GDSKWTGAIN ELMAAVDEYI PTPQRDADKT FLMPVEDVFT ITGRGTVATG RVERGTVKVN
     EEVEIIGLKE EPTKTVVTGL EMFRKLLDFA VAGDNVGALL RGVDRHSVER GQVLAKPGTI
     KPHTVLKASV YALTQEEGGR HKPFFNKYRP QFYFRTTDVT GEVTLPEGTD MVMPGDNVEM
     EIQLIKPVAV EEGTKFSIRE GGRTIGAGTV ISIEK