ID B7KSF2_METC4 Unreviewed; 396 AA. AC B7KSF2; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 27-MAR-2024, entry version 89. 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=Mchl_4855 {ECO:0000313|EMBL:ACK85620.1}; OS Methylorubrum extorquens (strain CM4 / NCIMB 13688) (Methylobacterium OS extorquens). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Methylobacteriaceae; Methylorubrum. OX NCBI_TaxID=440085 {ECO:0000313|EMBL:ACK85620.1, ECO:0000313|Proteomes:UP000002385}; RN [1] {ECO:0000313|Proteomes:UP000002385} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CM4 / NCIMB 13688 {ECO:0000313|Proteomes:UP000002385}; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., RA Han C., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., RA Marx C., Richardson P.; RT "Complete sequence of chromosome of Methylobacterium chloromethanicum RT CM4."; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ACK85620.1, ECO:0000313|Proteomes:UP000002385} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CM4 / NCIMB 13688 {ECO:0000313|Proteomes:UP000002385}; RX PubMed=22887658; DOI=10.1128/JB.01009-12; RA Marx C.J., Bringel F., Chistoserdova L., Moulin L., Farhan Ul Haque M., RA Fleischman D.E., Gruffaz C., Jourand P., Knief C., Lee M.C., Muller E.E., RA Nadalig T., Peyraud R., Roselli S., Russ L., Goodwin L.A., Ivanova N., RA Kyrpides N., Lajus A., Land M.L., Medigue C., Mikhailova N., Nolan M., RA Woyke T., Stolyar S., Vorholt J.A., Vuilleumier S.; RT "Complete genome sequences of six strains of the genus Methylobacterium."; RL J. Bacteriol. 194:4746-4748(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; CP001298; ACK85620.1; -; Genomic_DNA. DR RefSeq; WP_012255488.1; NC_011757.1. DR AlphaFoldDB; B7KSF2; -. DR GeneID; 72992127; -. DR KEGG; mch:Mchl_4855; -. DR HOGENOM; CLU_007265_0_0_5; -. DR Proteomes; UP000002385; 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}. 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; 43120 MW; 1FD2FEEF4A6E357B CRC64; MAKEKFSRTK PHCNIGTIGH VDHGKTSLTA AITKVLAESG GATFTAYDQI DKAPEEKARG ITISTAHVEY ETTNRHYAHV DCPGHADYVK NMITGAAQMD GAILVVSAAD GPMPQTREHI LLARQVGVPA LVVFLNKVDM VDDEELLELV ELEVRELLSK YDFPGDDIPI TKGSALMALE DKEPKIGKEA VLALMATVDE YIPQPERPID MPFLMPIEDV FSISGRGTVV TGRVERGIVK VGESVEIVGI RPTTTTTVTG VEMFRKLLDQ GQAGDNVGVL LRGTKREDVE RGQVVCKPGS VKPHSKFKAE AYILTKEEGG RHTPFFTNYR PQFYFRTTDV TGVCTLPEGT EMVMPGDNVT MDVVLIVPVA MEEKLRFAIR EGGRTVGAGV VAAIND //