ID EFTU_BOVIN Reviewed; 452 AA. AC P49410; Q0VCL4; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 27-MAR-2024, entry version 166. DE RecName: Full=Elongation factor Tu, mitochondrial; DE Short=EF-Tu; DE Flags: Precursor; GN Name=TUFM; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; OC Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE. RC TISSUE=Liver; RX PubMed=8547323; DOI=10.1016/0167-4781(95)00176-x; RA Woriax V.L., Burkhart W.A., Spremulli L.L.; RT "Cloning, sequence analysis and expression of mammalian mitochondrial RT protein synthesis elongation factor Tu."; RL Biochim. Biophys. Acta 1264:347-356(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Hereford; TISSUE=Fetal pons; RG NIH - Mammalian Gene Collection (MGC) project; RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases. RN [3] RP X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS). RX PubMed=10715211; DOI=10.1006/jmbi.2000.3564; RA Andersen G.R., Thirup S., Spremulli L.L., Nyborg J.; RT "High resolution crystal structure of bovine mitochondrial EF-Tu in complex RT with GDP."; RL J. Mol. Biol. 297:421-436(2000). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH TSFM. RX PubMed=15557323; DOI=10.1074/jbc.m411782200; RA Jeppesen M.G., Navratil T., Spremulli L.L., Nyborg J.; RT "Crystal structure of the bovine mitochondrial elongation factor Tu.Ts RT complex."; RL J. Biol. Chem. 280:5071-5081(2005). CC -!- FUNCTION: Promotes the GTP-dependent binding of aminoacyl-tRNA to the CC A-site of ribosomes during protein biosynthesis. Also plays a role in CC the regulation of autophagy and innate immunity. Recruits ATG5-ATG12 CC and NLRX1 at mitochondria and serves as a checkpoint of the RIGI-MAVS CC pathway. In turn, inhibits RLR-mediated type I interferon while CC promoting autophagy. {ECO:0000250|UniProtKB:P49411}. CC -!- SUBUNIT: Interacts with NLRX1. Interacts with ATG16L1. CC {ECO:0000250|UniProtKB:P49411}. CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:P49411}. 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|PROSITE-ProRule:PRU01059}. 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; L38996; AAB00500.1; -; mRNA. DR EMBL; BC120109; AAI20110.1; -; mRNA. DR PIR; S62768; S62768. DR RefSeq; NP_776632.1; NM_174207.2. DR PDB; 1D2E; X-ray; 1.94 A; A/B/C/D=55-451. DR PDB; 1XB2; X-ray; 2.20 A; A=44-452. DR PDBsum; 1D2E; -. DR PDBsum; 1XB2; -. DR AlphaFoldDB; P49410; -. DR SMR; P49410; -. DR IntAct; P49410; 1. DR STRING; 9913.ENSBTAP00000025586; -. DR SwissPalm; P49410; -. DR PaxDb; 9913-ENSBTAP00000025586; -. DR PeptideAtlas; P49410; -. DR Ensembl; ENSBTAT00000025586.2; ENSBTAP00000025586.1; ENSBTAG00000019216.2. DR GeneID; 281556; -. DR KEGG; bta:281556; -. DR CTD; 7284; -. DR VEuPathDB; HostDB:ENSBTAG00000019216; -. DR VGNC; VGNC:36517; TUFM. DR eggNOG; KOG0460; Eukaryota. DR GeneTree; ENSGT00940000156748; -. DR HOGENOM; CLU_007265_0_0_1; -. DR InParanoid; P49410; -. DR OMA; FHNNYRP; -. DR OrthoDB; 167272at2759; -. DR TreeFam; TF300432; -. DR EvolutionaryTrace; P49410; -. DR Proteomes; UP000009136; Chromosome 25. DR Bgee; ENSBTAG00000019216; Expressed in digestive system secreted substance and 107 other cell types or tissues. DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:AgBase. DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome. DR GO; GO:0042645; C:mitochondrial nucleoid; IEA:Ensembl. DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0003924; F:GTPase activity; IEA:InterPro. DR GO; GO:0003746; F:translation elongation factor activity; IDA:UniProtKB. DR GO; GO:0070125; P:mitochondrial translational elongation; IBA:GO_Central. DR GO; GO:0006414; P:translational elongation; IDA:UniProtKB. DR CDD; cd01884; EF_Tu; 1. DR CDD; cd03697; EFTU_II; 1. DR CDD; cd03706; mtEFTU_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 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; 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 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 1: Evidence at protein level; KW 3D-structure; Acetylation; Direct protein sequencing; Elongation factor; KW GTP-binding; Mitochondrion; Nucleotide-binding; Phosphoprotein; KW Protein biosynthesis; Reference proteome; Transit peptide. FT TRANSIT 1..43 FT /note="Mitochondrion" FT CHAIN 44..452 FT /note="Elongation factor Tu, mitochondrial" FT /id="PRO_0000007461" FT DOMAIN 55..251 FT /note="tr-type G" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059" FT REGION 64..71 FT /note="G1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059" FT REGION 105..109 FT /note="G2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059" FT REGION 126..129 FT /note="G3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059" FT REGION 181..184 FT /note="G4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059" FT REGION 219..221 FT /note="G5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059" FT BINDING 64..71 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250" FT BINDING 126..130 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250" FT BINDING 181..184 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250" FT MOD_RES 79 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P49411" FT MOD_RES 88 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P49411" FT MOD_RES 88 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8BFR5" FT MOD_RES 234 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:Q8BFR5" FT MOD_RES 256 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P49411" FT MOD_RES 278 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P49411" FT MOD_RES 286 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:Q8BFR5" FT MOD_RES 312 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8BFR5" FT MOD_RES 361 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q8BFR5" FT MOD_RES 418 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P49411" FT VARIANT 27 FT /note="L -> P" FT VARIANT 355 FT /note="Q -> H" FT STRAND 57..65 FT /evidence="ECO:0007829|PDB:1D2E" FT HELIX 66..68 FT /evidence="ECO:0007829|PDB:1XB2" FT HELIX 70..83 FT /evidence="ECO:0007829|PDB:1D2E" FT HELIX 92..96 FT /evidence="ECO:0007829|PDB:1D2E" FT STRAND 100..103 FT /evidence="ECO:0007829|PDB:1D2E" FT STRAND 106..109 FT /evidence="ECO:0007829|PDB:1D2E" FT STRAND 111..116 FT /evidence="ECO:0007829|PDB:1D2E" FT STRAND 121..126 FT /evidence="ECO:0007829|PDB:1D2E" FT HELIX 130..139 FT /evidence="ECO:0007829|PDB:1D2E" FT STRAND 145..152 FT /evidence="ECO:0007829|PDB:1D2E" FT TURN 153..155 FT /evidence="ECO:0007829|PDB:1D2E" FT HELIX 159..170 FT /evidence="ECO:0007829|PDB:1D2E" FT STRAND 176..181 FT /evidence="ECO:0007829|PDB:1D2E" FT HELIX 183..185 FT /evidence="ECO:0007829|PDB:1D2E" FT HELIX 189..205 FT /evidence="ECO:0007829|PDB:1D2E" FT TURN 210..212 FT /evidence="ECO:0007829|PDB:1D2E" FT STRAND 215..217 FT /evidence="ECO:0007829|PDB:1D2E" FT HELIX 220..224 FT /evidence="ECO:0007829|PDB:1D2E" FT TURN 229..232 FT /evidence="ECO:0007829|PDB:1D2E" FT HELIX 233..246 FT /evidence="ECO:0007829|PDB:1D2E" FT STRAND 259..261 FT /evidence="ECO:0007829|PDB:1D2E" FT STRAND 264..268 FT /evidence="ECO:0007829|PDB:1D2E" FT TURN 269..271 FT /evidence="ECO:0007829|PDB:1D2E" FT STRAND 272..278 FT /evidence="ECO:0007829|PDB:1D2E" FT STRAND 281..285 FT /evidence="ECO:0007829|PDB:1D2E" FT STRAND 289..294 FT /evidence="ECO:0007829|PDB:1D2E" FT STRAND 297..308 FT /evidence="ECO:0007829|PDB:1D2E" FT STRAND 311..317 FT /evidence="ECO:0007829|PDB:1D2E" FT STRAND 321..328 FT /evidence="ECO:0007829|PDB:1D2E" FT HELIX 331..333 FT /evidence="ECO:0007829|PDB:1D2E" FT STRAND 339..342 FT /evidence="ECO:0007829|PDB:1D2E" FT STRAND 349..358 FT /evidence="ECO:0007829|PDB:1D2E" FT HELIX 361..363 FT /evidence="ECO:0007829|PDB:1D2E" FT STRAND 377..380 FT /evidence="ECO:0007829|PDB:1D2E" FT STRAND 383..390 FT /evidence="ECO:0007829|PDB:1D2E" FT STRAND 403..414 FT /evidence="ECO:0007829|PDB:1D2E" FT STRAND 421..426 FT /evidence="ECO:0007829|PDB:1D2E" FT STRAND 429..438 FT /evidence="ECO:0007829|PDB:1D2E" FT HELIX 444..447 FT /evidence="ECO:0007829|PDB:1D2E" SQ SEQUENCE 452 AA; 49398 MW; 51031B10DA06A7F9 CRC64; MAAATLLRAT PLFSGLGAGP APLLQGLLRP LKAQALPVLC RGLAVEAKKT YVRDKPHVNV GTIGHVDHGK TTLTAAITKI LAEGGGAKFK KYEEIDNAPE ERARGITINA AHVEYSTAAR HYAHTDCPGH ADYVKNMITG TAPLDGCILV VAANDGPMPQ TREHLLLARQ IGVEHVVVYV NKADAVQDSE MVELVELEIR ELLTEFGYKG EETPIIVGSA LCALEQRDPE LGLKSVQKLL DAVDTYIPVP TRDLEKPFLL PVESVYSIPG RGTVVTGTLE RGILKKGDEC EFLGHSKNIR TVVTGIEMFH KSLDRAEAGD NLGALVRGLK REDLRRGLVM AKPGSIQPHQ KVEAQVYILT KEEGGRHKPF VSHFMPVMFS LTWDMACRII LPPGKELAMP GEDLKLTLIL RQPMILEKGQ RFTLRDGNRT IGTGLVTDTP AMTEEDKNIK WS //