ID   EFTU_YEAST              Reviewed;         437 AA.
AC   P02992; D6W2P3;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   27-MAR-2024, entry version 195.
DE   RecName: Full=Elongation factor Tu, mitochondrial;
DE   AltName: Full=tufM;
DE   Flags: Precursor;
GN   Name=TUF1; Synonyms=TUFM; OrderedLocusNames=YOR187W;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6353412; DOI=10.1073/pnas.80.20.6192;
RA   Nagata S., Tsunetsugu-Yokota Y., Naito A., Kaziro Y.;
RT   "Molecular cloning and sequence determination of the nuclear gene coding
RT   for mitochondrial elongation factor Tu of Saccharomyces cerevisiae.";
RL   Proc. Natl. Acad. Sci. U.S.A. 80:6192-6196(1983).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169874;
RA   Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA   Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA   Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA   Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA   Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA   Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA   Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA   Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA   Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA   Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA   Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA   Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA   Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA   Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA   Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA   Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA   Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL   Nature 387:98-102(1997).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   FUNCTION.
RX   PubMed=3905388; DOI=10.1002/j.1460-2075.1985.tb03896.x;
RA   Myers A.M., Pape L.K., Tzagoloff A.;
RT   "Mitochondrial protein synthesis is required for maintenance of intact
RT   mitochondrial genomes in Saccharomyces cerevisiae.";
RL   EMBO J. 4:2087-2092(1985).
RN   [5]
RP   CLEAVAGE BY MPP AND MIP, AND IDENTIFICATION OF PROBABLE CLEAVAGE SITE.
RX   PubMed=7593000; DOI=10.1074/jbc.270.45.27366;
RA   Branda S.S., Isaya G.;
RT   "Prediction and identification of new natural substrates of the yeast
RT   mitochondrial intermediate peptidase.";
RL   J. Biol. Chem. 270:27366-27373(1995).
RN   [6]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [7]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [8]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 76625 / YPH499;
RX   PubMed=14576278; DOI=10.1073/pnas.2135385100;
RA   Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E.,
RA   Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P.,
RA   Pfanner N., Meisinger C.;
RT   "The proteome of Saccharomyces cerevisiae mitochondria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
CC   -!- FUNCTION: G-protein that, in its active GTP-bound form, binds to and
CC       delivers aminoacyl-tRNA to the A-site of ribosomes during protein
CC       biosynthesis. In the presence of a correct codon-anticodon match
CC       between the aminoacyl-tRNA and the A-site codon of the ribosome-bound
CC       mRNA, the ribosome acts as a GTPase activator and the GTP is
CC       hydrolyzed. The inactive GDP-bound form leaves the ribosome and must be
CC       recycled before binding another molecule of aminoacyl-tRNA. Required
CC       for mitochondrial protein biosynthesis and maintenance of mitochondrial
CC       DNA. {ECO:0000269|PubMed:3905388}.
CC   -!- PATHWAY: Protein biosynthesis; polypeptide chain elongation.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14562095,
CC       ECO:0000269|PubMed:14576278}.
CC   -!- PTM: The precursor is processed in two steps involving mitochondrial
CC       intermediate peptidase (MIP) and mitochondrial processing peptidase
CC       (MPP). {ECO:0000269|PubMed:7593000}.
CC   -!- MISCELLANEOUS: Present with 58527 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A
CC       subfamily. {ECO:0000305}.
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DR   EMBL; K00428; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; Z75095; CAA99396.1; -; Genomic_DNA.
DR   EMBL; BK006948; DAA10959.1; -; Genomic_DNA.
DR   PIR; A03520; EFBYT.
DR   RefSeq; NP_014830.1; NM_001183606.1.
DR   AlphaFoldDB; P02992; -.
DR   SMR; P02992; -.
DR   BioGRID; 34582; 220.
DR   DIP; DIP-4130N; -.
DR   IntAct; P02992; 14.
DR   MINT; P02992; -.
DR   STRING; 4932.YOR187W; -.
DR   iPTMnet; P02992; -.
DR   MaxQB; P02992; -.
DR   PaxDb; 4932-YOR187W; -.
DR   PeptideAtlas; P02992; -.
DR   EnsemblFungi; YOR187W_mRNA; YOR187W; YOR187W.
DR   GeneID; 854359; -.
DR   KEGG; sce:YOR187W; -.
DR   AGR; SGD:S000005713; -.
DR   SGD; S000005713; TUF1.
DR   VEuPathDB; FungiDB:YOR187W; -.
DR   eggNOG; KOG0460; Eukaryota.
DR   GeneTree; ENSGT00940000156748; -.
DR   HOGENOM; CLU_007265_0_1_1; -.
DR   InParanoid; P02992; -.
DR   OMA; FHNNYRP; -.
DR   OrthoDB; 167272at2759; -.
DR   BioCyc; YEAST:G3O-33697-MONOMER; -.
DR   UniPathway; UPA00345; -.
DR   BioGRID-ORCS; 854359; 4 hits in 10 CRISPR screens.
DR   PRO; PR:P02992; -.
DR   Proteomes; UP000002311; Chromosome XV.
DR   RNAct; P02992; Protein.
DR   GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IDA:SGD.
DR   GO; GO:0003746; F:translation elongation factor activity; IDA:SGD.
DR   GO; GO:0032543; P:mitochondrial translation; IDA:SGD.
DR   GO; GO:0070125; P:mitochondrial translational elongation; IMP:SGD.
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   1: Evidence at protein level;
KW   Elongation factor; GTP-binding; Mitochondrion; Nucleotide-binding;
KW   Protein biosynthesis; Reference proteome; Transit peptide.
FT   TRANSIT         1..38
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000305"
FT   CHAIN           39..437
FT                   /note="Elongation factor Tu, mitochondrial"
FT                   /id="PRO_0000007465"
FT   DOMAIN          46..242
FT                   /note="tr-type G"
FT   REGION          55..62
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          96..100
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          117..120
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          172..175
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          210..212
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   BINDING         55..62
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         117..121
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         172..175
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   437 AA;  47972 MW;  26F4DFE805D1A93B CRC64;
     MSALLPRLLT RTAFKASGKL LRLSSVISRT FSQTTTSYAA AFDRSKPHVN IGTIGHVDHG
     KTTLTAAITK TLAAKGGANF LDYAAIDKAP EERARGITIS TAHVEYETAK RHYSHVDCPG
     HADYIKNMIT GAAQMDGAII VVAATDGQMP QTREHLLLAR QVGVQHIVVF VNKVDTIDDP
     EMLELVEMEM RELLNEYGFD GDNAPIIMGS ALCALEGRQP EIGEQAIMKL LDAVDEYIPT
     PERDLNKPFL MPVEDIFSIS GRGTVVTGRV ERGNLKKGEE LEIVGHNSTP LKTTVTGIEM
     FRKELDSAMA GDNAGVLLRG IRRDQLKRGM VLAKPGTVKA HTKILASLYI LSKEEGGRHS
     GFGENYRPQM FIRTADVTVV MRFPKEVEDH SMQVMPGDNV EMECDLIHPT PLEVGQRFNI
     REGGRTVGTG LITRIIE
//