EF3A_YEAST
ID EF3A_YEAST Reviewed; 1044 AA.
AC P16521; D6VYP7; O93815; Q06558;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 4.
DT 03-AUG-2022, entry version 226.
DE RecName: Full=Elongation factor 3A;
DE Short=EF-3;
DE Short=EF-3A;
DE EC=3.6.4.- {ECO:0000269|PubMed:29300771, ECO:0000269|PubMed:6456269, ECO:0000269|PubMed:7657623, ECO:0000269|PubMed:7957240};
DE AltName: Full=Eukaryotic elongation factor 3;
DE Short=eEF3;
DE AltName: Full=Translation elongation factor 3A;
DE AltName: Full=Yeast elongation factor 3;
GN Name=YEF3; Synonyms=EFC1, TEF3, YEF3A; OrderedLocusNames=YLR249W;
GN ORFNames=L9672.5;
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=2404974; DOI=10.1016/s0021-9258(19)39916-8;
RA Qin S., Xie A., Bonato M.C.M., McLaughlin C.S.;
RT "Sequence analysis of the translational elongation factor 3 from
RT Saccharomyces cerevisiae.";
RL J. Biol. Chem. 265:1903-1912(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1976386; DOI=10.1016/0167-4781(90)90172-x;
RA Sandbaken M.G., Lupisella J.A., DiDomenico B., Chakraburtty K.;
RT "Isolation and characterization of the structural gene encoding elongation
RT factor 3.";
RL Biochim. Biophys. Acta 1050:230-234(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2203789; DOI=10.1016/s0021-9258(18)55474-0;
RA Sandbaken M.G., Lupisella J.A., DiDomenico B., Chakraburtty K.;
RT "Protein synthesis in yeast. Structural and functional analysis of the gene
RT encoding elongation factor 3.";
RL J. Biol. Chem. 265:15838-15844(1990).
RN [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 446-955.
RC STRAIN=ATCC 208279 / BJ926;
RX PubMed=10361693; DOI=10.1271/bbb.63.769;
RA Uritani M., Shoumura Y., Yamada S.;
RT "Detection and analysis of translation elongation factor 3 genes from
RT various yeasts.";
RL Biosci. Biotechnol. Biochem. 63:769-772(1999).
RN [7]
RP PROTEIN SEQUENCE OF 959-967.
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 [8]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=6456269; DOI=10.1016/s0021-9258(19)68730-2;
RA Dasmahapatra B., Chakraburtty K.;
RT "Protein synthesis in yeast. I. Purification and properties of elongation
RT factor 3 from Saccharomyces cerevisiae.";
RL J. Biol. Chem. 256:9999-10004(1981).
RN [9]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=7657623; DOI=10.1074/jbc.270.35.20473;
RA Triana-Alonso F.J., Chakraburtty K., Nierhaus K.H.;
RT "The elongation factor 3 unique in higher fungi and essential for protein
RT biosynthesis is an E site factor.";
RL J. Biol. Chem. 270:20473-20478(1995).
RN [10]
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY REGULATION.
RX PubMed=7957240; DOI=10.1111/j.1432-1033.1994.tb20034.x;
RA Kovalchuke O., Chakraburtty K.;
RT "Comparative analysis of ribosome-associated adenosinetriphosphatase
RT (ATPase) from pig liver and the ATPase of elongation factor 3 from
RT Saccharomyces cerevisiae.";
RL Eur. J. Biochem. 226:133-140(1994).
RN [11]
RP ACETYLATION AT SER-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 [12]
RP INTERACTION WITH EEF1A.
RX PubMed=9990316; DOI=10.1046/j.1432-1327.1998.2580986.x;
RA Kovalchuke O., Kambampati R., Pladies E., Chakraburtty K.;
RT "Competition and cooperation amongst yeast elongation factors.";
RL Eur. J. Biochem. 258:986-993(1998).
RN [13]
RP CHARACTERIZATION.
RX PubMed=9544245;
RX DOI=10.1002/(sici)1097-0061(199802)14:3<239::aid-yea219>3.0.co;2-b;
RA Sarthy A.V., McGonigal T., Capobianco J.O., Schmidt M., Green S.R.,
RA Moehle C.M., Goldman R.C.;
RT "Identification and kinetic analysis of a functional homolog of elongation
RT factor 3, YEF3 in Saccharomyces cerevisiae.";
RL Yeast 14:239-253(1998).
RN [14]
RP INTERACTION WITH 18S RRNA.
RX PubMed=9553076; DOI=10.1074/jbc.273.17.10249;
RA Gontarek R.R., Li H., Nurse K., Prescott C.D.;
RT "The N-terminus of eukaryotic translation elongation factor 3 interacts
RT with 18 S rRNA and 80 S ribosomes.";
RL J. Biol. Chem. 273:10249-10252(1998).
RN [15]
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 [16]
RP MUTAGENESIS OF PHE-650, AND INTERACTION WITH EEF1A.
RX PubMed=12493761; DOI=10.1074/jbc.m209224200;
RA Anand M., Chakraburtty K., Marton M.J., Hinnebusch A.G., Kinzy T.G.;
RT "Functional interactions between yeast translation eukaryotic elongation
RT factor (eEF) 1A and eEF3.";
RL J. Biol. Chem. 278:6985-6991(2003).
RN [17]
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 [18]
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 [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1039 AND SER-1040, AND
RP IDENTIFICATION BY 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 [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-972; SER-1039 AND SER-1040,
RP AND 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 [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-642; THR-972; SER-974;
RP SER-1039 AND SER-1040, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [22]
RP FUNCTION, ASSOCIATION WITH RIBOSOMES, AND DOMAIN.
RX PubMed=22888004; DOI=10.1074/jbc.m112.368266;
RA Visweswaraiah J., Lee S.J., Hinnebusch A.G., Sattlegger E.;
RT "Overexpression of eukaryotic translation elongation factor 3 impairs Gcn2
RT protein activation.";
RL J. Biol. Chem. 287:37757-37768(2012).
RN [23]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [24]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-350 AND LYS-636, AND
RP IDENTIFICATION BY MASS 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 [25]
RP METHYLATION AT LYS-187; LYS-196 AND LYS-789.
RX PubMed=22522802; DOI=10.1002/pmic.201100570;
RA Couttas T.A., Raftery M.J., Padula M.P., Herbert B.R., Wilkins M.R.;
RT "Methylation of translation-associated proteins in Saccharomyces
RT cerevisiae: Identification of methylated lysines and their
RT methyltransferases.";
RL Proteomics 12:960-972(2012).
RN [26]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=29300771; DOI=10.1371/journal.pone.0190524;
RA Mateyak M.K., Pupek J.K., Garino A.E., Knapp M.C., Colmer S.F., Kinzy T.G.,
RA Dunaway S.;
RT "Demonstration of translation elongation factor 3 activity from a non-
RT fungal species, Phytophthora infestans.";
RL PLoS ONE 13:e0190524-e0190524(2018).
RN [27]
RP INDUCTION.
RX PubMed=33260587; DOI=10.3390/genes11121432;
RA Goscinska K., Shahmoradi Ghahe S., Domogala S., Topf U.;
RT "Eukaryotic Elongation Factor 3 Protects Saccharomyces cerevisiae Yeast
RT from Oxidative Stress.";
RL Genes (Basel) 11:E1432-E1432(2020).
CC -!- FUNCTION: Ribosome-dependent ATPase that functions in cytoplasmic
CC translation elongation (PubMed:7657623, PubMed:6456269,
CC PubMed:29300771). Required for the ATP-dependent release of deacylated
CC tRNA from the ribosomal E-site during protein biosynthesis
CC (PubMed:7657623). Stimulates the eEF1A-dependent binding of aminoacyl-
CC tRNA to the ribosomal A-site, which has reduced affinity for tRNA as
CC long as the E-site is occupied (PubMed:7657623). Plays a role as a
CC negative regulator of the GCN2 kinase activity; impairs GCN1-mediated
CC GCN2 activation on ribosomes by reducing GCN1-ribosome affinity, and
CC hence GCN2-mediated eIF-2-alpha phosphorylation in amino acid-starved
CC or repleted cells (PubMed:22888004). {ECO:0000269|PubMed:22888004,
CC ECO:0000269|PubMed:29300771, ECO:0000269|PubMed:6456269,
CC ECO:0000269|PubMed:7657623}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:29300771, ECO:0000269|PubMed:6456269,
CC ECO:0000269|PubMed:7657623, ECO:0000269|PubMed:7957240};
CC -!- ACTIVITY REGULATION: Inhibited by the translational inhibitors neomycin
CC and alpha-sarcin, which suppress the ATPase activity.
CC {ECO:0000269|PubMed:7957240}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.126 mM for ATP {ECO:0000269|PubMed:7957240};
CC KM=0.125 mM for GTP {ECO:0000269|PubMed:7957240};
CC Vmax=15.2 umol/min/mg enzyme with ATP as substrate
CC {ECO:0000269|PubMed:7957240};
CC -!- PATHWAY: Protein biosynthesis; polypeptide chain elongation.
CC {ECO:0000305}.
CC -!- SUBUNIT: Monomer. Interacts with elongation factor 1A (eEF1A).
CC Interacts through its N-terminus with 18S rRNA. Associates with
CC ribosomes (PubMed:22888004). {ECO:0000269|PubMed:12493761,
CC ECO:0000269|PubMed:22888004, ECO:0000269|PubMed:9553076,
CC ECO:0000269|PubMed:9990316}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- INDUCTION: Increases in strong (1 mM) hydrogen peroxide stress, and
CC decreases in milder (0.5 mM) hydrogen peroxide stress.
CC {ECO:0000269|PubMed:33260587}.
CC -!- DOMAIN: The heat repeats and the C-terminal domain are necessary for
CC impairing GCN1 function on ribosomes, and hence preventing GCN2 kinase
CC activity in amino acid-starved or repleted cells (PubMed:22888004).
CC {ECO:0000269|PubMed:22888004}.
CC -!- MISCELLANEOUS: Present with 870578 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCF family.
CC EF3 subfamily. {ECO:0000305}.
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DR EMBL; J05197; AAA35232.1; -; Genomic_DNA.
DR EMBL; J05583; AAA35233.1; -; Genomic_DNA.
DR EMBL; U20865; AAB67391.1; -; Genomic_DNA.
DR EMBL; AB018539; BAA33897.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09563.1; -; Genomic_DNA.
DR PIR; S59395; DVBYE3.
DR RefSeq; NP_013350.1; NM_001182136.1.
DR PDB; 2IW3; X-ray; 2.40 A; A/B=2-981.
DR PDB; 2IWH; X-ray; 3.00 A; A/B=2-981.
DR PDB; 2IX3; X-ray; 2.70 A; A/B=2-981.
DR PDB; 2IX8; EM; 6.00 A; A=2-977.
DR PDB; 7B7D; EM; 3.30 A; EF=1-1044.
DR PDBsum; 2IW3; -.
DR PDBsum; 2IWH; -.
DR PDBsum; 2IX3; -.
DR PDBsum; 2IX8; -.
DR PDBsum; 7B7D; -.
DR AlphaFoldDB; P16521; -.
DR SMR; P16521; -.
DR BioGRID; 31517; 199.
DR DIP; DIP-2249N; -.
DR IntAct; P16521; 83.
DR MINT; P16521; -.
DR STRING; 4932.YLR249W; -.
DR CarbonylDB; P16521; -.
DR iPTMnet; P16521; -.
DR MaxQB; P16521; -.
DR PaxDb; P16521; -.
DR PRIDE; P16521; -.
DR EnsemblFungi; YLR249W_mRNA; YLR249W; YLR249W.
DR GeneID; 850951; -.
DR KEGG; sce:YLR249W; -.
DR SGD; S000004239; YEF3.
DR VEuPathDB; FungiDB:YLR249W; -.
DR eggNOG; KOG0062; Eukaryota.
DR eggNOG; KOG1242; Eukaryota.
DR GeneTree; ENSGT00940000176346; -.
DR HOGENOM; CLU_002848_0_0_1; -.
DR InParanoid; P16521; -.
DR OMA; VLSEAMW; -.
DR BioCyc; YEAST:G3O-32354-MON; -.
DR SABIO-RK; P16521; -.
DR UniPathway; UPA00345; -.
DR EvolutionaryTrace; P16521; -.
DR PRO; PR:P16521; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P16521; protein.
DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:SGD.
DR GO; GO:0022626; C:cytosolic ribosome; IDA:SGD.
DR GO; GO:0042788; C:polysomal ribosome; IDA:UniProtKB.
DR GO; GO:0005840; C:ribosome; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0016887; F:ATP hydrolysis activity; IMP:SGD.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003746; F:translation elongation factor activity; IDA:SGD.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; IDA:UniProtKB.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; IDA:UniProtKB.
DR GO; GO:0006414; P:translational elongation; IMP:SGD.
DR GO; GO:0006415; P:translational termination; IDA:SGD.
DR Gene3D; 1.25.10.10; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR040533; 4HB.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR015688; Elongation_fac_3.
DR InterPro; IPR021133; HEAT_type_2.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR19211:SF5; PTHR19211:SF5; 1.
DR Pfam; PF17947; 4HB; 1.
DR Pfam; PF00005; ABC_tran; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
DR PROSITE; PS50077; HEAT_REPEAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Cytoplasm;
KW Direct protein sequencing; Elongation factor; Hydrolase; Isopeptide bond;
KW Methylation; Nucleotide-binding; Phosphoprotein; Protein biosynthesis;
KW Reference proteome; Repeat; RNA-binding; rRNA-binding; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9298649,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..1044
FT /note="Elongation factor 3A"
FT /id="PRO_0000093458"
FT REPEAT 5..42
FT /note="HEAT 1"
FT REPEAT 86..123
FT /note="HEAT 2"
FT REPEAT 125..162
FT /note="HEAT 3"
FT REPEAT 166..203
FT /note="HEAT 4"
FT REPEAT 205..241
FT /note="HEAT 5"
FT REPEAT 242..279
FT /note="HEAT 6"
FT REPEAT 285..323
FT /note="HEAT 7"
FT DOMAIN 426..641
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 667..993
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 974..1044
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 986..1006
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1007..1028
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 463..470
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 701..708
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:9298649,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 187
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000269|PubMed:22522802"
FT MOD_RES 196
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000269|PubMed:22522802"
FT MOD_RES 642
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 789
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000269|PubMed:22522802"
FT MOD_RES 972
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 974
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1039
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 1040
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT CROSSLNK 350
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 636
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT MUTAGEN 650
FT /note="F->S: Reduces ATPase activity and interaction with
FT eEF1A. Required for growth at 37 degrees Celsius and causes
FT a 50% reduction of total protein synthesis at permissive
FT temperatures."
FT /evidence="ECO:0000269|PubMed:12493761"
FT CONFLICT 153
FT /note="I -> F (in Ref. 1; AAA35232, 2; no nucleotide entry
FT and 3; AAA35233)"
FT /evidence="ECO:0000305"
FT CONFLICT 332
FT /note="V -> L (in Ref. 1; AAA35232, 2; no nucleotide entry
FT and 3; AAA35233)"
FT /evidence="ECO:0000305"
FT HELIX 3..18
FT /evidence="ECO:0007829|PDB:2IW3"
FT TURN 23..25
FT /evidence="ECO:0007829|PDB:2IW3"
FT HELIX 26..37
FT /evidence="ECO:0007829|PDB:2IW3"
FT STRAND 42..45
FT /evidence="ECO:0007829|PDB:2IW3"
FT HELIX 48..58
FT /evidence="ECO:0007829|PDB:2IW3"
FT HELIX 61..74
FT /evidence="ECO:0007829|PDB:2IW3"
FT TURN 77..79
FT /evidence="ECO:0007829|PDB:2IW3"
FT TURN 82..84
FT /evidence="ECO:0007829|PDB:2IW3"
FT HELIX 85..89
FT /evidence="ECO:0007829|PDB:2IW3"
FT HELIX 92..98
FT /evidence="ECO:0007829|PDB:2IW3"
FT HELIX 104..120
FT /evidence="ECO:0007829|PDB:2IW3"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:2IW3"
FT HELIX 126..139
FT /evidence="ECO:0007829|PDB:2IW3"
FT HELIX 143..159
FT /evidence="ECO:0007829|PDB:2IW3"
FT HELIX 161..178
FT /evidence="ECO:0007829|PDB:2IW3"
FT HELIX 184..197
FT /evidence="ECO:0007829|PDB:2IW3"
FT HELIX 198..200
FT /evidence="ECO:0007829|PDB:2IW3"
FT TURN 204..206
FT /evidence="ECO:0007829|PDB:2IW3"
FT HELIX 207..209
FT /evidence="ECO:0007829|PDB:2IW3"
FT HELIX 210..218
FT /evidence="ECO:0007829|PDB:2IW3"
FT HELIX 222..230
FT /evidence="ECO:0007829|PDB:2IW3"
FT HELIX 241..255
FT /evidence="ECO:0007829|PDB:2IW3"
FT STRAND 257..259
FT /evidence="ECO:0007829|PDB:2IW3"
FT HELIX 260..274
FT /evidence="ECO:0007829|PDB:2IW3"
FT HELIX 280..283
FT /evidence="ECO:0007829|PDB:2IW3"
FT HELIX 284..289
FT /evidence="ECO:0007829|PDB:2IW3"
FT HELIX 291..297
FT /evidence="ECO:0007829|PDB:2IW3"
FT TURN 298..300
FT /evidence="ECO:0007829|PDB:2IW3"
FT HELIX 304..321
FT /evidence="ECO:0007829|PDB:2IW3"
FT TURN 325..327
FT /evidence="ECO:0007829|PDB:2IW3"
FT HELIX 338..348
FT /evidence="ECO:0007829|PDB:2IW3"
FT TURN 349..351
FT /evidence="ECO:0007829|PDB:2IW3"
FT HELIX 356..358
FT /evidence="ECO:0007829|PDB:2IW3"
FT HELIX 359..374
FT /evidence="ECO:0007829|PDB:2IW3"
FT HELIX 380..386
FT /evidence="ECO:0007829|PDB:2IW3"
FT HELIX 388..391
FT /evidence="ECO:0007829|PDB:2IW3"
FT TURN 392..394
FT /evidence="ECO:0007829|PDB:2IW3"
FT HELIX 397..413
FT /evidence="ECO:0007829|PDB:2IW3"
FT STRAND 426..428
FT /evidence="ECO:0007829|PDB:2IW3"
FT STRAND 430..440
FT /evidence="ECO:0007829|PDB:2IW3"
FT STRAND 443..454
FT /evidence="ECO:0007829|PDB:2IW3"
FT STRAND 458..462
FT /evidence="ECO:0007829|PDB:2IW3"
FT HELIX 469..478
FT /evidence="ECO:0007829|PDB:2IW3"
FT TURN 487..489
FT /evidence="ECO:0007829|PDB:2IW3"
FT STRAND 492..494
FT /evidence="ECO:0007829|PDB:2IW3"
FT HELIX 508..513
FT /evidence="ECO:0007829|PDB:2IW3"
FT TURN 514..516
FT /evidence="ECO:0007829|PDB:2IX3"
FT HELIX 520..529
FT /evidence="ECO:0007829|PDB:2IW3"
FT HELIX 534..538
FT /evidence="ECO:0007829|PDB:2IW3"
FT HELIX 541..543
FT /evidence="ECO:0007829|PDB:2IW3"
FT HELIX 546..559
FT /evidence="ECO:0007829|PDB:2IW3"
FT STRAND 563..569
FT /evidence="ECO:0007829|PDB:2IW3"
FT TURN 570..573
FT /evidence="ECO:0007829|PDB:2IW3"
FT HELIX 576..588
FT /evidence="ECO:0007829|PDB:2IW3"
FT STRAND 591..596
FT /evidence="ECO:0007829|PDB:2IW3"
FT HELIX 600..606
FT /evidence="ECO:0007829|PDB:2IW3"
FT STRAND 608..614
FT /evidence="ECO:0007829|PDB:2IW3"
FT STRAND 617..623
FT /evidence="ECO:0007829|PDB:2IW3"
FT HELIX 625..631
FT /evidence="ECO:0007829|PDB:2IW3"
FT HELIX 633..637
FT /evidence="ECO:0007829|PDB:2IW3"
FT STRAND 638..640
FT /evidence="ECO:0007829|PDB:2IW3"
FT TURN 641..643
FT /evidence="ECO:0007829|PDB:2IW3"
FT STRAND 664..674
FT /evidence="ECO:0007829|PDB:2IW3"
FT STRAND 679..681
FT /evidence="ECO:0007829|PDB:2IX3"
FT STRAND 683..692
FT /evidence="ECO:0007829|PDB:2IW3"
FT STRAND 696..699
FT /evidence="ECO:0007829|PDB:2IW3"
FT HELIX 705..714
FT /evidence="ECO:0007829|PDB:2IW3"
FT STRAND 721..727
FT /evidence="ECO:0007829|PDB:2IW3"
FT STRAND 733..736
FT /evidence="ECO:0007829|PDB:2IW3"
FT HELIX 738..743
FT /evidence="ECO:0007829|PDB:2IW3"
FT HELIX 744..746
FT /evidence="ECO:0007829|PDB:2IW3"
FT HELIX 752..759
FT /evidence="ECO:0007829|PDB:2IW3"
FT TURN 760..762
FT /evidence="ECO:0007829|PDB:2IW3"
FT TURN 766..772
FT /evidence="ECO:0007829|PDB:2IW3"
FT HELIX 783..785
FT /evidence="ECO:0007829|PDB:2IW3"
FT STRAND 788..790
FT /evidence="ECO:0007829|PDB:2IW3"
FT STRAND 793..806
FT /evidence="ECO:0007829|PDB:2IW3"
FT STRAND 809..821
FT /evidence="ECO:0007829|PDB:2IW3"
FT STRAND 828..831
FT /evidence="ECO:0007829|PDB:2IW3"
FT HELIX 834..836
FT /evidence="ECO:0007829|PDB:2IW3"
FT STRAND 838..841
FT /evidence="ECO:0007829|PDB:2IW3"
FT HELIX 842..844
FT /evidence="ECO:0007829|PDB:2IW3"
FT HELIX 846..863
FT /evidence="ECO:0007829|PDB:2IW3"
FT HELIX 872..881
FT /evidence="ECO:0007829|PDB:2IW3"
FT HELIX 886..891
FT /evidence="ECO:0007829|PDB:2IW3"
FT HELIX 894..896
FT /evidence="ECO:0007829|PDB:2IW3"
FT HELIX 899..911
FT /evidence="ECO:0007829|PDB:2IW3"
FT STRAND 916..921
FT /evidence="ECO:0007829|PDB:2IW3"
FT HELIX 923..925
FT /evidence="ECO:0007829|PDB:2IW3"
FT HELIX 929..940
FT /evidence="ECO:0007829|PDB:2IW3"
FT STRAND 943..949
FT /evidence="ECO:0007829|PDB:2IW3"
FT HELIX 953..956
FT /evidence="ECO:0007829|PDB:2IW3"
FT TURN 957..959
FT /evidence="ECO:0007829|PDB:2IW3"
FT STRAND 962..964
FT /evidence="ECO:0007829|PDB:2IW3"
SQ SEQUENCE 1044 AA; 115945 MW; 41E40B8BDD7A4C33 CRC64;
MSDSQQSIKV LEELFQKLSV ATADNRHEIA SEVASFLNGN IIEHDVPEHF FGELAKGIKD
KKTAANAMQA VAHIANQSNL SPSVEPYIVQ LVPAICTNAG NKDKEIQSVA SETLISIVNA
VNPVAIKALL PHLTNAIVET NKWQEKIAIL AAISAMVDAA KDQVALRMPE LIPVLSETMW
DTKKEVKAAA TAAMTKATET VDNKDIERFI PSLIQCIADP TEVPETVHLL GATTFVAEVT
PATLSIMVPL LSRGLNERET GIKRKSAVII DNMCKLVEDP QVIAPFLGKL LPGLKSNFAT
IADPEAREVT LRALKTLRRV GNVGEDDAIP EVSHAGDVST TLQVVNELLK DETVAPRFKI
VVEYIAAIGA DLIDERIIDQ QAWFTHITPY MTIFLHEKKA KDILDEFRKR AVDNIPVGPN
FDDEEDEGED LCNCEFSLAY GAKILLNKTQ LRLKRARRYG ICGPNGCGKS TLMRAIANGQ
VDGFPTQEEC RTVYVEHDID GTHSDTSVLD FVFESGVGTK EAIKDKLIEF GFTDEMIAMP
ISALSGGWKM KLALARAVLR NADILLLDEP TNHLDTVNVA WLVNYLNTCG ITSITISHDS
VFLDNVCEYI INYEGLKLRK YKGNFTEFVK KCPAAKAYEE LSNTDLEFKF PEPGYLEGVK
TKQKAIVKVT NMEFQYPGTS KPQITDINFQ CSLSSRIAVI GPNGAGKSTL INVLTGELLP
TSGEVYTHEN CRIAYIKQHA FAHIESHLDK TPSEYIQWRF QTGEDRETMD RANRQINEND
AEAMNKIFKI EGTPRRIAGI HSRRKFKNTY EYECSFLLGE NIGMKSERWV PMMSVDNAWI
PRGELVESHS KMVAEVDMKE ALASGQFRPL TRKEIEEHCS MLGLDPEIVS HSRIRGLSGG
QKVKLVLAAG TWQRPHLIVL DEPTNYLDRD SLGALSKALK EFEGGVIIIT HSAEFTKNLT
EEVWAVKDGR MTPSGHNWVS GQGAGPRIEK KEDEEDKFDA MGNKIAGGKK KKKLSSAELR
KKKKERMKKK KELGDAYVSS DEEF
