ID C6X8R6_METGS Unreviewed; 396 AA. AC C6X8R6; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 27-MAR-2024, entry version 86. 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=Msip34_0287 {ECO:0000313|EMBL:ACT49536.1}, GN Msip34_0299 {ECO:0000313|EMBL:ACT49548.1}; OS Methylovorus glucosotrophus (strain SIP3-4). OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales; OC Methylophilaceae; Methylovorus. OX NCBI_TaxID=582744 {ECO:0000313|EMBL:ACT49536.1, ECO:0000313|Proteomes:UP000002743}; RN [1] {ECO:0000313|Proteomes:UP000002743} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SIP3-4 {ECO:0000313|Proteomes:UP000002743}; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D., RA Goodwin L., Pitluck S., Clum A., Larimer F., Land M., Hauser L., RA Kyrpides N., Mikhailova N., Kayluzhnaya M., Chistoserdova L.; RT "Complete sequence of chromosome of Methylovorus sp. SIP3-4."; RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ACT49536.1, ECO:0000313|Proteomes:UP000002743} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SIP3-4 {ECO:0000313|EMBL:ACT49536.1, RC ECO:0000313|Proteomes:UP000002743}; 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; CP001674; ACT49536.1; -; Genomic_DNA. DR EMBL; CP001674; ACT49548.1; -; Genomic_DNA. DR RefSeq; WP_013441116.1; NC_012969.1. DR AlphaFoldDB; C6X8R6; -. DR STRING; 582744.Msip34_0287; -. DR KEGG; mei:Msip34_0287; -. DR KEGG; mei:Msip34_0299; -. DR eggNOG; COG0050; Bacteria. DR HOGENOM; CLU_007265_0_0_4; -. DR OrthoDB; 9803139at2; -. DR Proteomes; UP000002743; 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:UP000002743}. 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; 42781 MW; 6235B4D6F15BE665 CRC64; MAKGKFERTK PHVNVGTIGH VDHGKTTLTA AITTILSKKF GGEAKAYDQI DAAPEEKARG ITINTAHVEY ETATRHYAHV DCPGHADYVK NMITGAAQMD GAILVCSAAD GPMPQTREHI LLARQVGVPY IVVFMNKADM VDDAELLELV EMEIRELLSK YDFPGDDIPV IKGSALKALE GDQSEIGEPA IFRLADALDS YIPTPERAVD GTFLMPVEDV FSISGRGTVV TGRIERGIVK VGDEIEIVGI KPTLKTTCTG VEMFRKLLDQ GQAGDNVGVL LRGTKREEVE RGQVLAKTGS IKPHTKFSAE IYVLGKDEGG RHTPFFNGYR PQFYFRTTDV TGAVELPAGT EMVMPGDNVS ITVALIAPIA MEDGLRFAIR EGGRTVGAGV VAKIIE //