EFTU_BOVIN
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 03-AUG-2022, entry version 159.
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 RIG-
CC I/DDX58-MAVS pathway. In turn, inhibits RLR-mediated type I interferon
CC while 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}.
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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 PaxDb; P49410; -.
DR PeptideAtlas; P49410; -.
DR PRIDE; P49410; -.
DR Ensembl; ENSBTAT00000025586; ENSBTAP00000025586; ENSBTAG00000019216.
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; EGDKEWG; -.
DR OrthoDB; 491836at2759; -.
DR TreeFam; TF300432; -.
DR EvolutionaryTrace; P49410; -.
DR Proteomes; UP000009136; Chromosome 25.
DR Bgee; ENSBTAG00000019216; Expressed in digestive system secreted substance and 107 other 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 Gene3D; 3.40.50.300; -; 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; 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 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; SSF50447; SSF50447; 1.
DR SUPFAM; SSF50465; SSF50465; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00485; EF-Tu; 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
