EFTU_YEAST
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 03-AUG-2022, entry version 188.
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; 196.
DR DIP; DIP-4130N; -.
DR IntAct; P02992; 14.
DR MINT; P02992; -.
DR STRING; 4932.YOR187W; -.
DR iPTMnet; P02992; -.
DR MaxQB; P02992; -.
DR PaxDb; P02992; -.
DR PRIDE; P02992; -.
DR EnsemblFungi; YOR187W_mRNA; YOR187W; YOR187W.
DR GeneID; 854359; -.
DR KEGG; sce:YOR187W; -.
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; EGDKEWG; -.
DR BioCyc; YEAST:G3O-33697-MON; -.
DR UniPathway; UPA00345; -.
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 GO; GO:0006414; P:translational elongation; IBA:GO_Central.
DR CDD; cd01884; EF_Tu; 1.
DR CDD; cd03697; EFTU_II; 1.
DR Gene3D; 3.40.50.300; -; 1.
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 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 TIGRFAMs; TIGR00231; small_GTP; 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
