ID D7DLM5_METV0 Unreviewed; 396 AA. AC D7DLM5; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 24-JAN-2024, entry version 75. 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 OrderedLocusNames=M301_0322 {ECO:0000313|EMBL:ADI28709.1}, M301_0334 GN {ECO:0000313|EMBL:ADI28721.1}; OS Methylotenera versatilis (strain 301). OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales; OC Methylophilaceae; Methylotenera. OX NCBI_TaxID=666681 {ECO:0000313|EMBL:ADI28709.1, ECO:0000313|Proteomes:UP000000383}; RN [1] {ECO:0000313|Proteomes:UP000000383} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=301 {ECO:0000313|Proteomes:UP000000383}; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Clum A., Land M., Hauser L., Kyrpides N., Ivanova N., RA Chistoservova L., Kalyuzhnaya M., Woyke T.; RT "Complete sequence of Methylotenera sp. 301."; RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ADI28709.1, ECO:0000313|Proteomes:UP000000383} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=301 {ECO:0000313|EMBL:ADI28709.1, RC ECO:0000313|Proteomes:UP000000383}; RX PubMed=21622745; DOI=10.1128/JB.00404-11; RA Lapidus A., Clum A., Labutti K., Kaluzhnaya M.G., Lim S., Beck D.A., RA Glavina Del Rio T., Nolan M., Mavromatis K., Huntemann M., Lucas S., RA Lidstrom M.E., Ivanova N., Chistoserdova L.; RT "Genomes of three methylotrophs from a single niche uncover genetic and RT metabolic divergence of Methylophilaceae."; RL J. Bacteriol. 193:3757-3764(2011). 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; CP002056; ADI28709.1; -; Genomic_DNA. DR EMBL; CP002056; ADI28721.1; -; Genomic_DNA. DR RefSeq; WP_013147026.1; NC_014207.1. DR AlphaFoldDB; D7DLM5; -. DR STRING; 666681.M301_0322; -. DR KEGG; meh:M301_0322; -. DR KEGG; meh:M301_0334; -. DR eggNOG; COG0050; Bacteria. DR HOGENOM; CLU_007265_0_0_4; -. DR OrthoDB; 9803139at2; -. DR Proteomes; UP000000383; 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:0097216; F:guanosine tetraphosphate binding; IEA:UniProt. 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|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}; 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}; Reference proteome {ECO:0000313|Proteomes:UP000000383}. FT DOMAIN 10..206 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 396 AA; 42899 MW; C93FC509B17F0DD8 CRC64; MAKGKFERTK PHVNVGTIGH VDHGKTTLTA AITTILSKKF GGEAKAYDQI DAAPEEKARG ITINTAHVEY ETANRHYAHV DCPGHADYVK NMITGAAQMD GAILVCSAAD GPMPQTREHI LLARQVGVPY IVVYLNKADL VDDAELLELV EMEVRDLLSK YDFPGDDTPI ITGSARAALE GDQTEIGEPS IFRLADALDN YIPMPERAID GTFLMPVEDV FSISGRGTVV TGRIERGIIK VGEEIEIVGL KPTVKTTCTG VEMFRKLLDQ GMAGDNVGVL LRGTKREDIE RGQVLAKSGS IKPHTKFTAE IYVLGKDEGG RHTPFFQGYR PQFYFRTTDV TGAVELPAGT EMVMPGDNVS ITVTLISPIA MEEGLRFAIR EGGRTVGAGV VAKIIE //