EFGM_YEAST
ID EFGM_YEAST Reviewed; 761 AA.
AC P25039; D6VY70; Q6B1Y6; Q99360;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Elongation factor G, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03061};
DE Short=EF-Gmt {ECO:0000255|HAMAP-Rule:MF_03061};
DE AltName: Full=Elongation factor G 1, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03061};
DE Short=mEF-G 1 {ECO:0000255|HAMAP-Rule:MF_03061};
DE AltName: Full=Elongation factor G1 {ECO:0000255|HAMAP-Rule:MF_03061};
DE Flags: Precursor;
GN Name=MEF1 {ECO:0000255|HAMAP-Rule:MF_03061}; OrderedLocusNames=YLR069C;
GN ORFNames=L2195;
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=1935960; DOI=10.1111/j.1432-1033.1991.tb16325.x;
RA Vambutas A., Ackerman S.H., Tzagoloff A.;
RT "Mitochondrial translational-initiation and elongation factors in
RT Saccharomyces cerevisiae.";
RL Eur. J. Biochem. 201:643-652(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP 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: Mitochondrial GTPase that catalyzes the GTP-dependent
CC ribosomal translocation step during translation elongation. During this
CC step, the ribosome changes from the pre-translocational (PRE) to the
CC post-translocational (POST) state as the newly formed A-site-bound
CC peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E
CC sites, respectively. Catalyzes the coordinated movement of the two tRNA
CC molecules, the mRNA and conformational changes in the ribosome.
CC {ECO:0000255|HAMAP-Rule:MF_03061}.
CC -!- PATHWAY: Protein biosynthesis; polypeptide chain elongation.
CC {ECO:0000255|HAMAP-Rule:MF_03061}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03061,
CC ECO:0000269|PubMed:14562095, 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:0000255|HAMAP-Rule:MF_03061}.
CC -!- MISCELLANEOUS: Present with 6348 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. EF-G/EF-2
CC subfamily. {ECO:0000305}.
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DR EMBL; X58378; CAA41267.1; -; Genomic_DNA.
DR EMBL; X94607; CAA64315.1; -; Genomic_DNA.
DR EMBL; Z73241; CAA97626.1; -; Genomic_DNA.
DR EMBL; AY692944; AAT92963.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09386.1; -; Genomic_DNA.
DR PIR; S61642; S61642.
DR RefSeq; NP_013170.1; NM_001181956.1.
DR AlphaFoldDB; P25039; -.
DR SMR; P25039; -.
DR BioGRID; 31343; 72.
DR IntAct; P25039; 3.
DR MINT; P25039; -.
DR STRING; 4932.YLR069C; -.
DR iPTMnet; P25039; -.
DR MaxQB; P25039; -.
DR PaxDb; P25039; -.
DR PRIDE; P25039; -.
DR EnsemblFungi; YLR069C_mRNA; YLR069C; YLR069C.
DR GeneID; 850758; -.
DR KEGG; sce:YLR069C; -.
DR SGD; S000004059; MEF1.
DR VEuPathDB; FungiDB:YLR069C; -.
DR eggNOG; KOG0465; Eukaryota.
DR GeneTree; ENSGT00550000074911; -.
DR HOGENOM; CLU_002794_4_1_1; -.
DR InParanoid; P25039; -.
DR OMA; AATTCHW; -.
DR BioCyc; YEAST:G3O-32222-MON; -.
DR UniPathway; UPA00345; -.
DR PRO; PR:P25039; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P25039; protein.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:0005739; C:mitochondrion; IMP:SGD.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0003746; F:translation elongation factor activity; ISA:SGD.
DR GO; GO:0032543; P:mitochondrial translation; IMP:SGD.
DR GO; GO:0070125; P:mitochondrial translational elongation; ISA:SGD.
DR CDD; cd16262; EFG_III; 1.
DR CDD; cd01434; EFG_mtEFG1_IV; 1.
DR CDD; cd04097; mtEFG1_C; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00054_B; EF_G_EF_2_B; 1.
DR InterPro; IPR045044; EFG1-like.
DR InterPro; IPR041095; EFG_II.
DR InterPro; IPR009022; EFG_III.
DR InterPro; IPR035647; EFG_III/V.
DR InterPro; IPR035649; EFG_V.
DR InterPro; IPR000640; EFG_V-like.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR031157; G_TR_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR004540; Transl_elong_EFG/EF2.
DR InterPro; IPR005517; Transl_elong_EFG/EF2_IV.
DR PANTHER; PTHR43636; PTHR43636; 1.
DR Pfam; PF00679; EFG_C; 1.
DR Pfam; PF14492; EFG_III; 1.
DR Pfam; PF03764; EFG_IV; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SMART; SM00838; EFG_C; 1.
DR SMART; SM00889; EFG_IV; 1.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF54980; SSF54980; 2.
DR TIGRFAMs; TIGR00484; EF-G; 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..42
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03061"
FT CHAIN 43..761
FT /note="Elongation factor G, mitochondrial"
FT /id="PRO_0000007449"
FT DOMAIN 68..349
FT /note="tr-type G"
FT BINDING 77..84
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03061"
FT BINDING 148..152
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03061"
FT BINDING 202..205
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03061"
FT CONFLICT 2
FT /note="S -> C (in Ref. 4; AAT92963)"
FT /evidence="ECO:0000305"
FT CONFLICT 66
FT /note="R -> I (in Ref. 1; CAA41267)"
FT /evidence="ECO:0000305"
FT CONFLICT 233
FT /note="I -> V (in Ref. 1; CAA41267)"
FT /evidence="ECO:0000305"
FT CONFLICT 478
FT /note="P -> S (in Ref. 1; CAA41267)"
FT /evidence="ECO:0000305"
FT CONFLICT 629
FT /note="L -> P (in Ref. 1; CAA41267)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 761 AA; 84574 MW; 3E2C534509B09103 CRC64;
MSVQKMMWVP RKMVGGRIPF FTCSKVFSGF SRRSFHESPL ARSTYEEEKV LVDEIKQKLT
PDDIGRCNKL RNIGISAHID SGKTTFTERV LYYTKRIKAI HEVRGRDNVG AKMDSMDLER
EKGITIQSAA TYCSWDKEGK NYHFNLIDTP GHIDFTIEVE RALRVLDGAV LVVCAVSGVQ
SQTVTVDRQM RRYNVPRVTF INKMDRMGSD PFRAIEQLNS KLKIPAAAVQ IPIGSESSLS
GVVDLINRVA IYNKGDNGEI IEKGPVPENL KPLMEEKRQL LIETLADVDD EMAEMFLEEK
EPTTQQIKDA IRRSTIARSF TPVLMGSALA NTGIQPVLDA IVDYLPNPSE VLNTALDVSN
NEAKVNLVPA VQQPFVGLAF KLEEGKYGQL TYVRVYQGRL RKGNYITNVK TGKKVKVARL
VRMHSSEMED VDEVGSGEIC ATFGIDCASG DTFTDGSVQY SMSSMYVPDA VVSLSITPNS
KDASNFSKAL NRFQKEDPTF RVKFDPESKE TIISGMGELH LEIYVERMRR EYNVDCVTGK
PQVSYRESIT IPADFDYTHK KQSGGAGQYG RVIGTLSPVD DITKGNIFET AIVGGRIPDK
YLAACGKGFE EVCEKGPLIG HRVLDVKMLI NDGAIHAVDS NELSFKTATM SAFRDAFLRA
QPVIMEPIMN VSVTSPNEFQ GNVIGLLNKL QAVIQDTENG HDEFTLKAEC ALSTMFGFAT
SLRASTQGKG EFSLEFSHYA PTAPHVQKEL ISEFQKKQAK K
