EFTS_ECOLI
ID EFTS_ECOLI Reviewed; 283 AA.
AC P0A6P1; P02997;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Elongation factor Ts {ECO:0000255|HAMAP-Rule:MF_00050};
DE Short=EF-Ts {ECO:0000255|HAMAP-Rule:MF_00050};
DE AltName: Full=Bacteriophage Q beta RNA-directed RNA polymerase subunit IV {ECO:0000303|PubMed:816798};
GN Name=tsf {ECO:0000255|HAMAP-Rule:MF_00050};
GN OrderedLocusNames=b0170, JW0165;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6272196; DOI=10.1093/nar/9.16.4163;
RA An G., Bendiak D.S., Mamelak L.A., Friesen J.D.;
RT "Organization and nucleotide sequence of a new ribosomal operon in
RT Escherichia coli containing the genes for ribosomal protein S2 and
RT elongation factor Ts.";
RL Nucleic Acids Res. 9:4163-4172(1981).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8202364; DOI=10.1093/nar/22.9.1637;
RA Fujita N., Mori H., Yura T., Ishihama A.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-
RT 4.1 min (110,917-193,643 bp) region.";
RL Nucleic Acids Res. 22:1637-1639(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA Takemoto K., Mori H., Murayama N., Kataoka K., Yano M., Itoh T.,
RA Yamamoto Y., Inokuchi H., Miki T., Hatada E., Fukuda R., Ichihara S.,
RA Mizuno T., Makino K., Nakata A., Yura T., Sampei G., Mizobuchi K.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 4.0
RT - 6.0 min (189,987 - 281,416bp) region.";
RL Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [7]
RP PROTEIN SEQUENCE OF 2-14.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA Pasquali C., Sanchez J.-C., Ravier F., Golaz O., Hughes G.J., Frutiger S.,
RA Paquet N., Wilkins M., Appel R.D., Bairoch A., Hochstrasser D.F.;
RL Submitted (SEP-1994) to UniProtKB.
RN [8]
RP PROTEIN SEQUENCE OF 2-22.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [9]
RP PROTEIN SEQUENCE OF 2-5.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9600841; DOI=10.1006/jmbi.1998.1726;
RA Wilkins M.R., Gasteiger E., Tonella L., Ou K., Tyler M., Sanchez J.-C.,
RA Gooley A.A., Walsh B.J., Bairoch A., Appel R.D., Williams K.L.,
RA Hochstrasser D.F.;
RT "Protein identification with N and C-terminal sequence tags in proteome
RT projects.";
RL J. Mol. Biol. 278:599-608(1998).
RN [10]
RP PROTEIN SEQUENCE OF 52-56, AND MASS SPECTROMETRY.
RX PubMed=7615087; DOI=10.1016/0014-5793(95)00597-3;
RA Boegestrand S., Wiborg O., Thirup S., Nyborg J.;
RT "Analysis and crystallization of a 25 kDa C-terminal fragment of cloned
RT elongation factor Ts from Escherichia coli.";
RL FEBS Lett. 368:49-54(1995).
RN [11]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 179-283.
RX PubMed=1447125; DOI=10.1128/jb.174.23.7517-7526.1992;
RA Yamanaka K., Ogura T., Niki H., Hiraga S.;
RT "Identification and characterization of the smbA gene, a suppressor of the
RT mukB null mutant of Escherichia coli.";
RL J. Bacteriol. 174:7517-7526(1992).
RN [12]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 199-275.
RX PubMed=2661533; DOI=10.1128/jb.171.7.3689-3695.1989;
RA Ichikawa S., Ryoji M., Siegfried Z., Kaji A.;
RT "Localization of the ribosome-releasing factor gene in the Escherichia coli
RT chromosome.";
RL J. Bacteriol. 171:3689-3695(1989).
RN [13]
RP FUNCTION IN VIRAL RNA REPLICATION (MICROBIAL INFECTION), AND SUBUNIT
RP (MICROBIAL INFECTION).
RX PubMed=816798; DOI=10.1016/s0021-9258(17)33551-2;
RA Carmichael G.G., Landers T.A., Weber K.;
RT "Immunochemical analysis of the functions of the subunits of phage Qbeta
RT ribonucleic acid replicase.";
RL J. Biol. Chem. 251:2744-2748(1976).
RN [14]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF COMPLEX WITH EF-TU, AND SUBUNIT.
RX PubMed=8596629; DOI=10.1038/379511a0;
RA Kawashima T., Berthet-Colominas C., Wulff M., Cusack S., Leberman R.;
RT "The structure of the Escherichia coli EF-Tu.EF-Ts complex at 2.5-A
RT resolution.";
RL Nature 379:511-518(1996).
RN [16]
RP MUTAGENESIS OF LYS-24; ASP-81; PHE-82 AND HIS-148.
RX PubMed=9468511; DOI=10.1074/jbc.273.8.4556;
RA Zhang Y., Yu N.-J., Spremulli L.L.;
RT "Mutational analysis of the roles of residues in Escherichia coli
RT elongation factor Ts in the interaction with elongation factor Tu.";
RL J. Biol. Chem. 273:4556-4562(1998).
RN [17]
RP CONSTRUCT TO PRODUCE QBETA VIRAL CATALYTIC CORE.
RC STRAIN=A/lambda;
RX PubMed=16781472; DOI=10.1263/jbb.101.421;
RA Kita H., Cho J., Matsuura T., Nakaishi T., Taniguchi I., Ichikawa T.,
RA Shima Y., Urabe I., Yomo T.;
RT "Functional Qbeta replicase genetically fusing essential subunits EF-Ts and
RT EF-Tu with beta-subunit.";
RL J. Biosci. Bioeng. 101:421-426(2006).
RN [18]
RP FUNCTION IN CDI (MICROBIAL INFECTION), AND MUTAGENESIS OF 186-VAL--GLY-225;
RP ALA-202 AND ARG-219.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=28223500; DOI=10.1073/pnas.1619273114;
RA Jones A.M., Garza-Sanchez F., So J., Hayes C.S., Low D.A.;
RT "Activation of contact-dependent antibacterial tRNase toxins by translation
RT elongation factors.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:E1951-E1957(2017).
RN [19]
RP FUNCTION IN CDI (MICROBIAL INFECTION).
RX PubMed=28973472; DOI=10.1093/nar/gkx700;
RA Michalska K., Gucinski G.C., Garza-Sanchez F., Johnson P.M., Stols L.M.,
RA Eschenfeldt W.H., Babnigg G., Low D.A., Goulding C.W., Joachimiak A.,
RA Hayes C.S.;
RT "Structure of a novel antibacterial toxin that exploits elongation factor
RT Tu to cleave specific transfer RNAs.";
RL Nucleic Acids Res. 45:10306-10320(2017).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN QBETA VIRUS RNA POLYMERASE
RP CATALYTIC CORE, FUNCTION IN VIRAL RNA REPLICATION (MICROBIAL INFECTION),
RP AND SUBUNIT.
RX PubMed=20534494; DOI=10.1073/pnas.1003015107;
RA Kidmose R.T., Vasiliev N.N., Chetverin A.B., Andersen G.R., Knudsen C.R.;
RT "Structure of the Qbeta replicase, an RNA-dependent RNA polymerase
RT consisting of viral and host proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:10884-10889(2010).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) IN QBETA VIRUS RNA POLYMERASE
RP CATALYTIC CORE, FUNCTION IN VIRAL RNA REPLICATION (MICROBIAL INFECTION),
RP SUBUNIT, AND MUTAGENESIS OF 188-ALA--VAL-227.
RX PubMed=20798060; DOI=10.1073/pnas.1006559107;
RA Takeshita D., Tomita K.;
RT "Assembly of Q{beta} viral RNA polymerase with host translational
RT elongation factors EF-Tu and -Ts.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:15733-15738(2010).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (2.41 ANGSTROMS) IN QBETA VIRUS RNA POLYMERASE
RP CATALYTIC CORE, FUNCTION IN VIRAL RNA REPLICATION (MICROBIAL INFECTION),
RP AND SUBUNIT.
RX PubMed=22245970; DOI=10.1038/nsmb.2204;
RA Takeshita D., Tomita K.;
RT "Molecular basis for RNA polymerization by Qbeta replicase.";
RL Nat. Struct. Mol. Biol. 19:229-237(2012).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) IN QBETA VIRUS RNA POLYMERASE
RP CATALYTIC CORE, FUNCTION IN VIRAL RNA REPLICATION (MICROBIAL INFECTION),
RP AND SUBUNIT.
RX PubMed=22884418; DOI=10.1016/j.str.2012.07.004;
RA Takeshita D., Yamashita S., Tomita K.;
RT "Mechanism for template-independent terminal adenylation activity of Qbeta
RT replicase.";
RL Structure 20:1661-1669(2012).
RN [24]
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) IN QBETA VIRUS RNA POLYMERASE,
RP FUNCTION IN VIRAL RNA REPLICATION (MICROBIAL INFECTION), AND SUBUNIT.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=25122749; DOI=10.1093/nar/gku745;
RA Takeshita D., Yamashita S., Tomita K.;
RT "Molecular insights into replication initiation by Qbeta replicase using
RT ribosomal protein S1.";
RL Nucleic Acids Res. 42:10809-10822(2014).
CC -!- FUNCTION: Associates with the EF-Tu.GDP complex and induces the
CC exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF-
CC Tu.GTP complex up to the GTP hydrolysis stage on the ribosome.
CC {ECO:0000255|HAMAP-Rule:MF_00050}.
CC -!- FUNCTION: (Microbial infection) In case of infection by bacteriophage
CC Qbeta (and related Leviviruses), part of the viral RNA-dependent RNA
CC polymerase complex. With EF-Tu may provide a stabilizing scaffold for
CC the beta (catalytic) subunit, implicated in the elongation step of
CC viral RNA synthesis where it fixes EF-Tu in an open conformation.
CC {ECO:0000269|PubMed:20534494, ECO:0000269|PubMed:20798060,
CC ECO:0000269|PubMed:22245970, ECO:0000269|PubMed:22884418,
CC ECO:0000269|PubMed:25122749, ECO:0000269|PubMed:816798}.
CC -!- FUNCTION: (Microbial infection) Promotes the tRNase activity of CdiA-CT
CC from E.coli strain EC869 (CdiA-CT-EC869); required in vivo but less so
CC in vitro. Probably loads charged tRNA onto EF-Tu, making more ternary
CC GTP-EF-Tu-aa-tRNA complexes. The guanine nucleotide exchange factor
CC capacity of this protein does not seem to be needed as no GTP
CC hydrolysis occurs during tRNA cleavage. Also required in vivo for toxic
CC activity of CdiA-CT from E.coli strains NC101 and CdiA-CT-96.154. CdiA-
CC CT is the toxic component of a toxin-immunity protein module, which
CC functions as a cellular contact-dependent growth inhibition (CDI)
CC system. CDI modules allow bacteria to communicate with and inhibit the
CC growth of closely related neighboring bacteria in a contact-dependent
CC fashion (PubMed:28223500). EF-Ts interacts with at least 2 different
CC toxic CT domains, the 2 toxins are different and degrade tRNA at
CC different positions (PubMed:28973472, PubMed:28223500).
CC {ECO:0000269|PubMed:28223500, ECO:0000269|PubMed:28973472}.
CC -!- FUNCTION: (Microbial infection) Promotes the tRNase activity of CdiA-CT
CC from E.coli strain NC101 (CdiA-CT-NC101); required in vivo and in
CC vitro. Probably loads charged tRNA onto EF-Tu, making more ternary GTP-
CC EF-Tu-aa-tRNA complexes. The guanine nucleotide exchange factor
CC capacity of this protein does not seem to be needed as no GTP
CC hydrolysis occurs during tRNA cleavage. CdiA-CT is the toxic component
CC of a toxin-immunity protein module, which functions as a cellular
CC contact-dependent growth inhibition (CDI) system. CDI modules allow
CC bacteria to communicate with and inhibit the growth of closely related
CC neighboring bacteria in a contact-dependent fashion (PubMed:28973472).
CC EF-Ts interacts with at least 2 different toxic CT domains, the 2
CC toxins are different and degrade tRNA at different positions
CC (PubMed:28973472, PubMed:28223500). {ECO:0000269|PubMed:28223500,
CC ECO:0000269|PubMed:28973472}.
CC -!- SUBUNIT: Heterotetramer composed of two EF-Ts.EF-Tu dimer complexes.
CC {ECO:0000269|PubMed:8596629}.
CC -!- SUBUNIT: (Microbial infection) In case of infection by bacteriophage
CC Qbeta, part of the viral RNA-dependent RNA polymerase complex, the
CC other subunits are the viral replicase catalytic subunit (AC P14647),
CC host ribosomal protein S1 and EF-Tu (PubMed:816798).
CC {ECO:0000269|PubMed:20534494, ECO:0000269|PubMed:20798060,
CC ECO:0000269|PubMed:22245970, ECO:0000269|PubMed:22884418,
CC ECO:0000269|PubMed:25122749, ECO:0000269|PubMed:816798}.
CC -!- INTERACTION:
CC P0A6P1; P0CE47: tufA; NbExp=12; IntAct=EBI-301164, EBI-301077;
CC P0A6P1; P0CE48: tufB; NbExp=3; IntAct=EBI-301164, EBI-9010251;
CC P0A6P1; P14647; Xeno; NbExp=2; IntAct=EBI-301164, EBI-9010000;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00050}.
CC -!- MASS SPECTROMETRY: Mass=30294; Mass_error=6; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:7615087};
CC -!- MISCELLANEOUS: In order to produce high amounts of bacteriophage Qbeta
CC RNA polymerase catalytic core, a fusion protein consisting of tsf-tufB-
CC replicase with a cleavable linker between tufB and the viral replicase
CC subunit is frequently used. {ECO:0000269|PubMed:16781472,
CC ECO:0000269|PubMed:20798060, ECO:0000269|PubMed:22245970,
CC ECO:0000269|PubMed:22884418, ECO:0000269|PubMed:25122749}.
CC -!- SIMILARITY: Belongs to the EF-Ts family. {ECO:0000255|HAMAP-
CC Rule:MF_00050}.
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DR EMBL; V00343; CAA23632.1; -; Genomic_DNA.
DR EMBL; D13334; BAA02597.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73281.1; -; Genomic_DNA.
DR EMBL; AP009048; BAB96746.1; -; Genomic_DNA.
DR EMBL; U70214; AAB08599.1; -; Genomic_DNA.
DR PIR; A03525; EFECS.
DR RefSeq; NP_414712.1; NC_000913.3.
DR RefSeq; WP_000818114.1; NZ_STEB01000032.1.
DR PDB; 1EFU; X-ray; 2.50 A; B/D=2-283.
DR PDB; 3AGP; X-ray; 2.80 A; A=1-283.
DR PDB; 3AGQ; X-ray; 3.22 A; A=1-283.
DR PDB; 3AVT; X-ray; 2.61 A; A=1-283.
DR PDB; 3AVU; X-ray; 2.91 A; A=1-283.
DR PDB; 3AVV; X-ray; 3.12 A; A=1-283.
DR PDB; 3AVW; X-ray; 2.60 A; A=1-283.
DR PDB; 3AVX; X-ray; 2.41 A; A=1-283.
DR PDB; 3AVY; X-ray; 2.62 A; A=1-283.
DR PDB; 3MMP; X-ray; 2.50 A; A/C=1-283.
DR PDB; 3VNU; X-ray; 3.20 A; A=1-283.
DR PDB; 3VNV; X-ray; 2.60 A; A=1-283.
DR PDB; 4FWT; X-ray; 3.20 A; A=1-283.
DR PDB; 4PC3; X-ray; 1.83 A; C/D=2-283.
DR PDB; 4PC7; X-ray; 3.60 A; C=2-283.
DR PDB; 4Q7J; X-ray; 2.90 A; A/E=2-283.
DR PDB; 4R71; X-ray; 3.21 A; A/C=1-283.
DR PDBsum; 1EFU; -.
DR PDBsum; 3AGP; -.
DR PDBsum; 3AGQ; -.
DR PDBsum; 3AVT; -.
DR PDBsum; 3AVU; -.
DR PDBsum; 3AVV; -.
DR PDBsum; 3AVW; -.
DR PDBsum; 3AVX; -.
DR PDBsum; 3AVY; -.
DR PDBsum; 3MMP; -.
DR PDBsum; 3VNU; -.
DR PDBsum; 3VNV; -.
DR PDBsum; 4FWT; -.
DR PDBsum; 4PC3; -.
DR PDBsum; 4PC7; -.
DR PDBsum; 4Q7J; -.
DR PDBsum; 4R71; -.
DR AlphaFoldDB; P0A6P1; -.
DR SMR; P0A6P1; -.
DR BioGRID; 4260795; 54.
DR ComplexPortal; CPX-2853; Elongation Factor TU-TS, tufB variant.
DR ComplexPortal; CPX-6035; Elongation Factor TU-TS, tufA variant.
DR DIP; DIP-31835N; -.
DR IntAct; P0A6P1; 12.
DR STRING; 511145.b0170; -.
DR CarbonylDB; P0A6P1; -.
DR SWISS-2DPAGE; P0A6P1; -.
DR jPOST; P0A6P1; -.
DR PaxDb; P0A6P1; -.
DR PRIDE; P0A6P1; -.
DR EnsemblBacteria; AAC73281; AAC73281; b0170.
DR EnsemblBacteria; BAB96746; BAB96746; BAB96746.
DR GeneID; 66671542; -.
DR GeneID; 944866; -.
DR KEGG; ecj:JW0165; -.
DR KEGG; eco:b0170; -.
DR PATRIC; fig|1411691.4.peg.2110; -.
DR EchoBASE; EB1026; -.
DR eggNOG; COG0264; Bacteria.
DR HOGENOM; CLU_047155_0_2_6; -.
DR InParanoid; P0A6P1; -.
DR OMA; DAGMMDC; -.
DR PhylomeDB; P0A6P1; -.
DR BioCyc; EcoCyc:EG11033-MON; -.
DR EvolutionaryTrace; P0A6P1; -.
DR PRO; PR:P0A6P1; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; HDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0032045; C:guanyl-nucleotide exchange factor complex; IPI:ComplexPortal.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:EcoCyc.
DR GO; GO:0003746; F:translation elongation factor activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IDA:EcoliWiki.
DR GO; GO:0006414; P:translational elongation; IBA:GO_Central.
DR Gene3D; 3.30.479.20; -; 2.
DR HAMAP; MF_00050; EF_Ts; 1.
DR InterPro; IPR036402; EF-Ts_dimer_sf.
DR InterPro; IPR001816; Transl_elong_EFTs/EF1B.
DR InterPro; IPR014039; Transl_elong_EFTs/EF1B_dimer.
DR InterPro; IPR018101; Transl_elong_Ts_CS.
DR InterPro; IPR009060; UBA-like_sf.
DR PANTHER; PTHR11741; PTHR11741; 1.
DR Pfam; PF00889; EF_TS; 1.
DR SUPFAM; SSF46934; SSF46934; 1.
DR SUPFAM; SSF54713; SSF54713; 2.
DR TIGRFAMs; TIGR00116; tsf; 1.
DR PROSITE; PS01126; EF_TS_1; 1.
DR PROSITE; PS01127; EF_TS_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Elongation factor;
KW Protein biosynthesis; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9298646,
FT ECO:0000269|PubMed:9600841, ECO:0000269|Ref.7"
FT CHAIN 2..283
FT /note="Elongation factor Ts"
FT /id="PRO_0000161117"
FT REGION 80..83
FT /note="Involved in Mg(2+) ion dislocation from EF-Tu"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00050"
FT MUTAGEN 24
FT /note="K->A: No change in binding to EF-Tu and in promoting
FT GDP exchange."
FT /evidence="ECO:0000269|PubMed:9468511"
FT MUTAGEN 81
FT /note="D->A: 2 to 3-fold less active in promoting GDP
FT exchange and slightly lower binding constant for
FT interaction with EF-Tu."
FT /evidence="ECO:0000269|PubMed:9468511"
FT MUTAGEN 82
FT /note="F->A: 2 to 3-fold less active in promoting GDP
FT exchange and 6-fold less active in binding to EF-Tu."
FT /evidence="ECO:0000269|PubMed:9468511"
FT MUTAGEN 148
FT /note="H->A: At least 100-fold decrease in affinity between
FT EF-Ts and EF-Tu and only small amount of GDP exchange
FT activity."
FT /evidence="ECO:0000269|PubMed:9468511"
FT MUTAGEN 186..225
FT /note="VSAEVVEKEYQVQLDIAMQSGKPKEIAEKMVEGRMKKFTG->EPGGEA:
FT Resistant to toxins CdiA-CT-EC869, CdiA-CT-NC101 and CdiA-
FT CT-96.154, but not other CdiA toxins in growth competition
FT experiments, in vitro prevents CdiA-CT-EC869 from digesting
FT tRNA(GUG-Gln). Resistant to bacteriophage R17."
FT /evidence="ECO:0000269|PubMed:28223500"
FT MUTAGEN 188..227
FT /note="Missing: Still associates with EF-Tu, no longer
FT forms the Qbeta viral RNA polymerase complex."
FT /evidence="ECO:0000269|PubMed:20798060"
FT MUTAGEN 202
FT /note="A->E: Resistant to toxin CdiA-CT-EC869, partially
FT resistant to toxins CdiA-CT-NC101 and CdiA-CT-96.154, but
FT not resistant to other CdiA toxins in growth competition
FT experiments, in vitro prevents CdiA-CT-EC869 from digesting
FT tRNA(GUG-Gln). Partially resistant to bacteriophage R17."
FT /evidence="ECO:0000269|PubMed:28223500"
FT MUTAGEN 219
FT /note="R->P: Resistant to toxin CdiA-CT-EC869, partially
FT resistant to toxins CdiA-CT-NC101 and CdiA-CT-96.154, but
FT not resistant to other CdiA toxins in growth competition
FT experiments. Resistant to bacteriophage R17."
FT /evidence="ECO:0000269|PubMed:28223500"
FT HELIX 6..16
FT /evidence="ECO:0007829|PDB:4PC3"
FT HELIX 20..29
FT /evidence="ECO:0007829|PDB:4PC3"
FT TURN 30..32
FT /evidence="ECO:0007829|PDB:4PC3"
FT HELIX 34..52
FT /evidence="ECO:0007829|PDB:4PC3"
FT STRAND 59..67
FT /evidence="ECO:0007829|PDB:4PC3"
FT STRAND 70..79
FT /evidence="ECO:0007829|PDB:4PC3"
FT HELIX 81..85
FT /evidence="ECO:0007829|PDB:4PC3"
FT HELIX 87..103
FT /evidence="ECO:0007829|PDB:4PC3"
FT HELIX 108..126
FT /evidence="ECO:0007829|PDB:4PC3"
FT STRAND 131..139
FT /evidence="ECO:0007829|PDB:4PC3"
FT STRAND 141..148
FT /evidence="ECO:0007829|PDB:4PC3"
FT TURN 149..151
FT /evidence="ECO:0007829|PDB:4PC3"
FT STRAND 152..160
FT /evidence="ECO:0007829|PDB:4PC3"
FT HELIX 163..176
FT /evidence="ECO:0007829|PDB:4PC3"
FT STRAND 179..182
FT /evidence="ECO:0007829|PDB:4PC3"
FT HELIX 183..185
FT /evidence="ECO:0007829|PDB:4PC3"
FT HELIX 188..204
FT /evidence="ECO:0007829|PDB:4PC3"
FT HELIX 209..226
FT /evidence="ECO:0007829|PDB:4PC3"
FT TURN 229..231
FT /evidence="ECO:0007829|PDB:4PC3"
FT STRAND 232..234
FT /evidence="ECO:0007829|PDB:1EFU"
FT STRAND 237..241
FT /evidence="ECO:0007829|PDB:1EFU"
FT HELIX 242..248
FT /evidence="ECO:0007829|PDB:4PC3"
FT STRAND 252..260
FT /evidence="ECO:0007829|PDB:4PC3"
FT TURN 261..264
FT /evidence="ECO:0007829|PDB:4PC3"
FT HELIX 272..279
FT /evidence="ECO:0007829|PDB:4PC3"
SQ SEQUENCE 283 AA; 30423 MW; 0B9D21E928A5051C CRC64;
MAEITASLVK ELRERTGAGM MDCKKALTEA NGDIELAIEN MRKSGAIKAA KKAGNVAADG
VIKTKIDGNY GIILEVNCQT DFVAKDAGFQ AFADKVLDAA VAGKITDVEV LKAQFEEERV
ALVAKIGENI NIRRVAALEG DVLGSYQHGA RIGVLVAAKG ADEELVKHIA MHVAASKPEF
IKPEDVSAEV VEKEYQVQLD IAMQSGKPKE IAEKMVEGRM KKFTGEVSLT GQPFVMEPSK
TVGQLLKEHN AEVTGFIRFE VGEGIEKVET DFAAEVAAMS KQS
