EF1B_YEAST
ID EF1B_YEAST Reviewed; 206 AA.
AC P32471; D6VPL3;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=Elongation factor 1-beta;
DE Short=EF-1-beta;
DE AltName: Full=Eukaryotic elongation factor 1Balpha;
DE Short=eEF1Balpha;
DE AltName: Full=Translation elongation factor 1B alpha;
GN Name=EFB1; Synonyms=TEF5; OrderedLocusNames=YAL003W;
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=8420802; DOI=10.1016/0014-5793(93)81208-h;
RA Hiraga K., Suzuki K., Tsuchiya E., Miyakawa T.;
RT "Cloning and characterization of the elongation factor EF-1 beta homologue
RT of Saccharomyces cerevisiae. EF-1 beta is essential for growth.";
RL FEBS Lett. 316:165-169(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204511 / S288c / AB972;
RX PubMed=7941740; DOI=10.1002/yea.320100413;
RA Clark M.W., Keng T., Storms R.K., Zhong W.-W., Fortin N., Zeng B.,
RA Delaney S., Ouellette B.F.F., Barton A.B., Kaback D.B., Bussey H.;
RT "Sequencing of chromosome I of Saccharomyces cerevisiae: analysis of the 42
RT kbp SPO7-CENI-CDC15 region.";
RL Yeast 10:535-541(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7731988; DOI=10.1073/pnas.92.9.3809;
RA Bussey H., Kaback D.B., Zhong W.-W., Vo D.H., Clark M.W., Fortin N.,
RA Hall J., Ouellette B.F.F., Keng T., Barton A.B., Su Y., Davies C.J.,
RA Storms R.K.;
RT "The nucleotide sequence of chromosome I from Saccharomyces cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:3809-3813(1995).
RN [4]
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 [5]
RP PROTEIN SEQUENCE OF 14-22 AND 51-56.
RC STRAIN=ATCC 38531 / Y41;
RX PubMed=8935650; DOI=10.1111/j.1574-6968.1996.tb08073.x;
RA Norbeck J., Blomberg A.;
RT "Protein expression during exponential growth in 0.7 M NaCl medium of
RT Saccharomyces cerevisiae.";
RL FEMS Microbiol. Lett. 137:1-8(1996).
RN [6]
RP PROTEIN SEQUENCE OF 168-178.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7895733; DOI=10.1002/elps.11501501210;
RA Garrels J.I., Futcher B., Kobayashi R., Latter G.I., Schwender B.,
RA Volpe T., Warner J.R., McLaughlin C.S.;
RT "Protein identifications for a Saccharomyces cerevisiae protein database.";
RL Electrophoresis 15:1466-1486(1994).
RN [7]
RP ACETYLATION AT ALA-2.
RX PubMed=9298649; DOI=10.1002/elps.1150180810;
RA Garrels J.I., McLaughlin C.S., Warner J.R., Futcher B., Latter G.I.,
RA Kobayashi R., Schwender B., Volpe T., Anderson D.S., Mesquita-Fuentes R.,
RA Payne W.E.;
RT "Proteome studies of Saccharomyces cerevisiae: identification and
RT characterization of abundant proteins.";
RL Electrophoresis 18:1347-1360(1997).
RN [8]
RP FUNCTION, AND MUTAGENESIS OF SER-121.
RX PubMed=10409717; DOI=10.1128/mcb.19.8.5257;
RA Carr-Schmid A., Valente L., Loik V.I., Williams T., Starita L.M.,
RA Kinzy T.G.;
RT "Mutations in elongation factor 1beta, a guanine nucleotide exchange
RT factor, enhance translational fidelity.";
RL Mol. Cell. Biol. 19:5257-5266(1999).
RN [9]
RP PHOSPHORYLATION.
RX PubMed=10523624; DOI=10.1128/mcb.19.11.7357;
RA Futcher B., Latter G.I., Monardo P., McLaughlin C.S., Garrels J.I.;
RT "A sampling of the yeast proteome.";
RL Mol. Cell. Biol. 19:7357-7368(1999).
RN [10]
RP S-THIOLATION.
RX PubMed=12755685; DOI=10.1042/bj20030414;
RA Shenton D., Grant C.M.;
RT "Protein S-thiolation targets glycolysis and protein synthesis in response
RT to oxidative stress in the yeast Saccharomyces cerevisiae.";
RL Biochem. J. 374:513-519(2003).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31 AND SER-86, AND
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).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [15]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-13, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (1.67 ANGSTROMS) OF 113-206 IN COMPLEX WITH EEF1A,
RP AND MUTAGENESIS OF PHE-163.
RX PubMed=11106763; DOI=10.1016/s1097-2765(00)00122-2;
RA Andersen G.R., Pedersen L., Valente L., Chatterjee I., Kinzy T.G.,
RA Kjeldgaard M., Nyborg J.;
RT "Structural basis for nucleotide exchange and competition with tRNA in the
RT yeast elongation factor complex eEF1A:eEF1Balpha.";
RL Mol. Cell 6:1261-1266(2000).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 113-206 IN COMPLEX WITH EEF1A,
RP AND MUTAGENESIS OF LYS-205.
RX PubMed=11373622; DOI=10.1038/88598;
RA Andersen G.R., Valente L., Pedersen L., Kinzy T.G., Nyborg J.;
RT "Crystal structures of nucleotide exchange intermediates in the eEF1A-
RT eEF1Balpha complex.";
RL Nat. Struct. Biol. 8:531-534(2001).
CC -!- FUNCTION: Catalytic subunit of the guanine nucleotide exchange factor
CC (GEF) (eEF1B subcomplex) of the eukaryotic elongation factor 1 complex
CC (eEF1). Stimulates the exchange of GDP for GTP on elongation factor 1A
CC (eEF1A), probably by displacing GDP from the nucleotide binding pocket
CC in eEF1A. The 30-fold higher concentration of GTP compared to GDP in
CC cells favors the formation of eEF1A-GTP, which rapidly forms a ternary
CC complex with aminoacyl-tRNA that in turn displaces eEF1B from the
CC complex. {ECO:0000269|PubMed:10409717}.
CC -!- PATHWAY: Protein biosynthesis; polypeptide chain elongation.
CC -!- SUBUNIT: The eukaryotic elongation factor 1 complex (eEF1) is probably
CC a heterohexamer. Two trimeric complexes, each composed of eEF1A (TEF1
CC or TEF2), eEF1Balpha (EFB1) and eEF1Bgamma (CAM1 or TEF4), are probably
CC dimerized via the eF1Bgamma subunits. eEF1Balpha interacts directly
CC with eEF1A. eEF1Balpha and eEF1Bgamma form the eEF1B subcomplex with
CC the GEF activity. {ECO:0000269|PubMed:11106763,
CC ECO:0000269|PubMed:11373622}.
CC -!- INTERACTION:
CC P32471; P02994: TEF2; NbExp=2; IntAct=EBI-6319, EBI-6314;
CC -!- DOMAIN: The C-terminus (pos. 119-205) exhibits guanine nucleotide
CC exchange activity.
CC -!- PTM: S-thiolated in response to oxidative stress, probably inhibiting
CC the protein and causing a reduction in protein synthesis.
CC {ECO:0000269|PubMed:12755685}.
CC -!- SIMILARITY: Belongs to the EF-1-beta/EF-1-delta family. {ECO:0000305}.
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DR EMBL; D14080; BAA03165.1; -; Genomic_DNA.
DR EMBL; L22015; AAC04954.1; -; Genomic_DNA.
DR EMBL; BK006935; DAA06983.1; -; Genomic_DNA.
DR PIR; S43445; S43445.
DR RefSeq; NP_009398.1; NM_001178150.1.
DR PDB; 1F60; X-ray; 1.67 A; B=113-206.
DR PDB; 1G7C; X-ray; 2.05 A; B=113-206.
DR PDB; 1IJE; X-ray; 2.40 A; B=117-206.
DR PDB; 1IJF; X-ray; 3.00 A; B=117-206.
DR PDB; 2B7B; X-ray; 2.60 A; B=113-204.
DR PDB; 2B7C; X-ray; 1.80 A; B=113-204.
DR PDB; 5O8W; X-ray; 1.67 A; B=113-206.
DR PDBsum; 1F60; -.
DR PDBsum; 1G7C; -.
DR PDBsum; 1IJE; -.
DR PDBsum; 1IJF; -.
DR PDBsum; 2B7B; -.
DR PDBsum; 2B7C; -.
DR PDBsum; 5O8W; -.
DR AlphaFoldDB; P32471; -.
DR SMR; P32471; -.
DR BioGRID; 31787; 86.
DR ComplexPortal; CPX-2854; Elongation Factor eEF1 complex, variant CAM1.
DR ComplexPortal; CPX-425; Elongation Factor eEF1 complex, variant TEF4.
DR DIP; DIP-6445N; -.
DR IntAct; P32471; 9.
DR MINT; P32471; -.
DR STRING; 4932.YAL003W; -.
DR iPTMnet; P32471; -.
DR SWISS-2DPAGE; P32471; -.
DR MaxQB; P32471; -.
DR PaxDb; P32471; -.
DR PRIDE; P32471; -.
DR TopDownProteomics; P32471; -.
DR EnsemblFungi; YAL003W_mRNA; YAL003W; YAL003W.
DR GeneID; 851260; -.
DR KEGG; sce:YAL003W; -.
DR SGD; S000000003; EFB1.
DR VEuPathDB; FungiDB:YAL003W; -.
DR eggNOG; KOG1668; Eukaryota.
DR GeneTree; ENSGT00950000183014; -.
DR HOGENOM; CLU_050172_0_2_1; -.
DR InParanoid; P32471; -.
DR OMA; FEVKPWD; -.
DR BioCyc; YEAST:G3O-28818-MON; -.
DR Reactome; R-SCE-156842; Eukaryotic Translation Elongation.
DR UniPathway; UPA00345; -.
DR EvolutionaryTrace; P32471; -.
DR PRO; PR:P32471; -.
DR Proteomes; UP000002311; Chromosome I.
DR RNAct; P32471; protein.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005853; C:eukaryotic translation elongation factor 1 complex; IMP:SGD.
DR GO; GO:0005840; C:ribosome; IDA:ComplexPortal.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:SGD.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR GO; GO:1990145; P:maintenance of translational fidelity; IMP:SGD.
DR GO; GO:0032232; P:negative regulation of actin filament bundle assembly; IDA:SGD.
DR GO; GO:0006449; P:regulation of translational termination; IGI:SGD.
DR GO; GO:0006414; P:translational elongation; IDA:ComplexPortal.
DR CDD; cd00292; EF1B; 1.
DR Gene3D; 3.30.70.60; -; 1.
DR InterPro; IPR036219; eEF-1beta-like_sf.
DR InterPro; IPR018940; EF-1_beta_acid_region_euk.
DR InterPro; IPR014038; EF1B_bsu/dsu_GNE.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR014717; Transl_elong_EF1B/ribosomal_S6.
DR InterPro; IPR001326; Transl_elong_EF1B_B/D_CS.
DR Pfam; PF10587; EF-1_beta_acid; 1.
DR Pfam; PF00736; EF1_GNE; 1.
DR SMART; SM01182; EF-1_beta_acid; 1.
DR SMART; SM00888; EF1_GNE; 1.
DR SUPFAM; SSF47616; SSF47616; 1.
DR SUPFAM; SSF54984; SSF54984; 1.
DR PROSITE; PS00824; EF1BD_1; 1.
DR PROSITE; PS00825; EF1BD_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; Elongation factor;
KW Isopeptide bond; Phosphoprotein; Protein biosynthesis; Reference proteome;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9298649"
FT CHAIN 2..206
FT /note="Elongation factor 1-beta"
FT /id="PRO_0000155042"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:9298649"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 86
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT CROSSLNK 13
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT MUTAGEN 120..122
FT /note="KSI->R: In TEF5-7; reduces translation efficiency
FT and enhances translation fidelity."
FT MUTAGEN 121
FT /note="S->I,L,N: Reduces translation efficiency and
FT enhances translation fidelity."
FT /evidence="ECO:0000269|PubMed:10409717"
FT MUTAGEN 163
FT /note="F->A: Temperature-sensitive."
FT /evidence="ECO:0000269|PubMed:11106763"
FT MUTAGEN 205
FT /note="K->A: Loss of catalytic activity, but still binds to
FT eEF1A."
FT /evidence="ECO:0000269|PubMed:11373622"
FT CONFLICT 49
FT /note="S -> F (in Ref. 1; BAA03165)"
FT /evidence="ECO:0000305"
FT CONFLICT 57
FT /note="S -> F (in Ref. 1; BAA03165)"
FT /evidence="ECO:0000305"
FT CONFLICT 98
FT /note="L -> W (in Ref. 1; BAA03165)"
FT /evidence="ECO:0000305"
FT CONFLICT 168
FT /note="L -> E (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 120..131
FT /evidence="ECO:0007829|PDB:1F60"
FT HELIX 136..144
FT /evidence="ECO:0007829|PDB:1F60"
FT STRAND 151..162
FT /evidence="ECO:0007829|PDB:1F60"
FT STRAND 165..175
FT /evidence="ECO:0007829|PDB:1F60"
FT TURN 176..178
FT /evidence="ECO:0007829|PDB:1F60"
FT HELIX 181..189
FT /evidence="ECO:0007829|PDB:1F60"
FT TURN 192..194
FT /evidence="ECO:0007829|PDB:1F60"
FT STRAND 195..205
FT /evidence="ECO:0007829|PDB:1F60"
SQ SEQUENCE 206 AA; 22627 MW; BEA764852CE125F7 CRC64;
MASTDFSKIE TLKQLNASLA DKSYIEGTAV SQADVTVFKA FQSAYPEFSR WFNHIASKAD
EFDSFPAASA AAAEEEEDDD VDLFGSDDEE ADAEAEKLKA ERIAAYNAKK AAKPAKPAAK
SIVTLDVKPW DDETNLEEMV ANVKAIEMEG LTWGAHQFIP IGFGIKKLQI NCVVEDDKVS
LDDLQQSIEE DEDHVQSTDI AAMQKL
