EFTS_POLNS
ID EFTS_POLNS Reviewed; 294 AA.
AC B1XTU4;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 25-MAY-2022, entry version 68.
DE RecName: Full=Elongation factor Ts {ECO:0000255|HAMAP-Rule:MF_00050};
DE Short=EF-Ts {ECO:0000255|HAMAP-Rule:MF_00050};
GN Name=tsf {ECO:0000255|HAMAP-Rule:MF_00050}; OrderedLocusNames=Pnec_0508;
OS Polynucleobacter necessarius subsp. necessarius (strain STIR1).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Polynucleobacter.
OX NCBI_TaxID=452638;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=STIR1;
RX PubMed=24167248; DOI=10.1073/pnas.1316687110;
RA Boscaro V., Felletti M., Vannini C., Ackerman M.S., Chain P.S.,
RA Malfatti S., Vergez L.M., Shin M., Doak T.G., Lynch M., Petroni G.;
RT "Polynucleobacter necessarius, a model for genome reduction in both free-
RT living and symbiotic bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:18590-18595(2013).
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00050}.
CC -!- SIMILARITY: Belongs to the EF-Ts family. {ECO:0000255|HAMAP-
CC Rule:MF_00050}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001010; ACB43771.1; -; Genomic_DNA.
DR RefSeq; WP_012357538.1; NC_010531.1.
DR AlphaFoldDB; B1XTU4; -.
DR SMR; B1XTU4; -.
DR STRING; 452638.Pnec_0508; -.
DR EnsemblBacteria; ACB43771; ACB43771; Pnec_0508.
DR KEGG; pne:Pnec_0508; -.
DR eggNOG; COG0264; Bacteria.
DR HOGENOM; CLU_047155_0_2_4; -.
DR OMA; DAGMMDC; -.
DR OrthoDB; 1405357at2; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
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; PS01127; EF_TS_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Elongation factor; Protein biosynthesis.
FT CHAIN 1..294
FT /note="Elongation factor Ts"
FT /id="PRO_1000116769"
FT REGION 80..83
FT /note="Involved in Mg(2+) ion dislocation from EF-Tu"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00050"
SQ SEQUENCE 294 AA; 31142 MW; BC491DD3D121EFE5 CRC64;
MVAITAAMVG ELRAKTDAPM MECKKALTEA DGDMARAEEI LRVKLGSKAG KAASRVTAEG
IVAASINSTT GALLEVNCET DFVSKNDDFL AFANDCVKLV AEKNPADVAA LLALPLNGQT
VDEVRSALIG KIGENIMPRH FKRFAGSNKL VSYLHGTRIG VVVEFEGDDT AAKDVAMHIA
AMKPVALSMA DVPAEAIAVE RSVAVQKAAE SGKPPEIVEK MVEGSIQKYL KEVSLLNQTF
VKNDKQTVEQ MLKAANTTIK GFTMFVVGEG IEKRQDDFAA EVAAQVAAAS KATA