ID E4PTH5_MYCLG Unreviewed; 395 AA. AC E4PTH5; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 27-MAR-2024, entry version 77. DE RecName: Full=Elongation factor Tu {ECO:0000256|ARBA:ARBA00029554, ECO:0000256|HAMAP-Rule:MF_00118}; DE Short=EF-Tu {ECO:0000256|HAMAP-Rule:MF_00118}; GN Name=tuf {ECO:0000256|HAMAP-Rule:MF_00118, GN ECO:0000313|EMBL:ADR23857.1}; GN OrderedLocusNames=MSB_A0204 {ECO:0000313|EMBL:ADR23857.1}; OS Mycoplasma leachii (strain DSM 21131 / NCTC 10133 / N29 / PG50). OC Bacteria; Mycoplasmatota; Mollicutes; Mycoplasmataceae; Mycoplasma. OX NCBI_TaxID=880447 {ECO:0000313|EMBL:ADR23857.1, ECO:0000313|Proteomes:UP000008712}; RN [1] {ECO:0000313|Proteomes:UP000008712} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 21131 / NCTC 10133 / N29 / PG50 RC {ECO:0000313|Proteomes:UP000008712}; RA Wise K., Calcutt M.J., Foecking M.F., Madupu R., DeBoy R.T., Roske K., RA Martin T.R., Hvinden M.L., Durkin A.S., Glass J., Methe B.A.; RT "Genome sequence of Mycoplasma leachii PG50 MU clone A8."; RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ADR23857.1, ECO:0000313|Proteomes:UP000008712} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 21131 / NCTC 10133 / N29 / PG50 RC {ECO:0000313|Proteomes:UP000008712}; RX PubMed=22843585; DOI=10.1128/JB.00761-12; RA Wise K.S., Calcutt M.J., Foecking M.F., Madupu R., Deboy R.T., Roske K., RA Hvinden M.L., Martin T.R., Durkin A.S., Glass J.I., Methe B.A.; RT "Complete Genome Sequences of Mycoplasma leachii Strain PG50T and the RT Pathogenic Mycoplasma mycoides subsp. mycoides Small Colony Biotype Strain RT Gladysdale."; RL J. Bacteriol. 194:4448-4449(2012). CC -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl- CC tRNA to the A-site of ribosomes during protein biosynthesis. CC {ECO:0000256|HAMAP-Rule:MF_00118}. CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00118}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|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:0000256|ARBA:ARBA00007249, ECO:0000256|HAMAP- CC 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; CP002108; ADR23857.1; -; Genomic_DNA. DR RefSeq; WP_011166362.1; NC_014751.1. DR AlphaFoldDB; E4PTH5; -. DR SMR; E4PTH5; -. DR GeneID; 58110184; -. DR KEGG; mlc:MSB_A0204; -. DR eggNOG; COG0050; Bacteria. DR HOGENOM; CLU_007265_0_0_14; -. DR OrthoDB; 9804504at2; -. DR Proteomes; UP000008712; 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 CDD; cd03707; EFTU_III; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR Gene3D; 2.40.30.10; Translation factors; 2. 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 NCBIfam; TIGR00485; EF-Tu; 1. DR NCBIfam; TIGR00231; small_GTP; 1. DR PANTHER; PTHR43721:SF22; ELONGATION FACTOR TU, MITOCHONDRIAL; 1. DR PANTHER; PTHR43721; ELONGATION FACTOR TU-RELATED; 1. 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; SSF50465; EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR SUPFAM; SSF50447; Translation proteins; 1. DR PROSITE; PS00301; G_TR_1; 1. DR PROSITE; PS51722; G_TR_2; 1. PE 3: Inferred from homology; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00118}; KW Elongation factor {ECO:0000256|ARBA:ARBA00022768, ECO:0000256|HAMAP- KW Rule:MF_00118}; KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP- KW Rule:MF_00118}; Hydrolase {ECO:0000313|EMBL:ADR23857.1}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_00118}; KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP- KW Rule:MF_00118}. FT DOMAIN 10..204 FT /note="Tr-type G" FT /evidence="ECO:0000259|PROSITE:PS51722" FT BINDING 19..26 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00118" FT BINDING 81..85 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00118" FT BINDING 136..139 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|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 //