ID EFTU_MAGMM Reviewed; 396 AA. AC A0L5V8; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 12-DEC-2006, sequence version 1. DT 27-MAR-2024, entry version 102. DE RecName: Full=Elongation factor Tu {ECO:0000255|HAMAP-Rule:MF_00118}; DE Short=EF-Tu {ECO:0000255|HAMAP-Rule:MF_00118}; GN Name=tuf1 {ECO:0000255|HAMAP-Rule:MF_00118}; GN OrderedLocusNames=Mmc1_0832; GN and GN Name=tuf2 {ECO:0000255|HAMAP-Rule:MF_00118}; GN OrderedLocusNames=Mmc1_0845; OS Magnetococcus marinus (strain ATCC BAA-1437 / JCM 17883 / MC-1). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Magnetococcales; OC Magnetococcaceae; Magnetococcus. OX NCBI_TaxID=156889; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1437 / JCM 17883 / MC-1; RX PubMed=19465526; DOI=10.1128/aem.02874-08; RA Schubbe S., Williams T.J., Xie G., Kiss H.E., Brettin T.S., Martinez D., RA Ross C.A., Schuler D., Cox B.L., Nealson K.H., Bazylinski D.A.; RT "Complete genome sequence of the chemolithoautotrophic marine magnetotactic RT coccus strain MC-1."; RL Appl. Environ. Microbiol. 75:4835-4852(2009). 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}. 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; CP000471; ABK43351.1; -; Genomic_DNA. DR EMBL; CP000471; ABK43364.1; -; Genomic_DNA. DR RefSeq; WP_011712511.1; NC_008576.1. DR AlphaFoldDB; A0L5V8; -. DR SMR; A0L5V8; -. DR STRING; 156889.Mmc1_0832; -. DR KEGG; mgm:Mmc1_0832; -. DR KEGG; mgm:Mmc1_0845; -. DR eggNOG; COG0050; Bacteria. DR HOGENOM; CLU_007265_0_0_5; -. DR OrthoDB; 9803139at2; -. DR Proteomes; UP000002586; 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; Elongation factor; GTP-binding; Nucleotide-binding; KW Protein biosynthesis; Reference proteome. FT CHAIN 1..396 FT /note="Elongation factor Tu" FT /id="PRO_0000337426" FT DOMAIN 10..206 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 396 AA; 43194 MW; CDCFF607E9F15C49 CRC64; MAKEKFARTK PHVNIGTIGH VDHGKTTLTA AITKVMAAAG RAEFRAYDQI DGAPEERERG ITISTAHVEY ETEARHYAHV DCPGHADYVK NMITGAAQMD GGILVVSAAD GPMPQTREHI LLARQVGVPA LVVFLNKVDQ VDDEELLELV EMEVRELLSS YDFPGDDIPV IKGSALKALE GEESEMGVDA INRLMDAVDA YIPEPERPLD QAFLMPIEDV FTISGRGTVV TGRIERGIVK VGEQVAIIGI KDTVVTTCTG VEMFRKLLDQ GQAGDNVGVL LRGTKREDVQ RGQVLAAPNS IKPHTKFNAE SYILTKEEGG RHTPFFSNYR PQFYFRTTDV TGVLKLPEGV EMVMPGDNIT MEVELIAPIA MEKGLRFAIR EGGRTVGAGV VAEVID //