EFTS_LIGS1
ID EFTS_LIGS1 Reviewed; 291 AA.
AC Q1WUL4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 1.
DT 25-MAY-2022, entry version 87.
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=LSL_0512;
OS Ligilactobacillus salivarius (strain UCC118) (Lactobacillus salivarius).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Ligilactobacillus.
OX NCBI_TaxID=362948;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCC118;
RX PubMed=16617113; DOI=10.1073/pnas.0511060103;
RA Claesson M.J., Li Y., Leahy S., Canchaya C., van Pijkeren J.P.,
RA Cerdeno-Tarraga A.M., Parkhill J., Flynn S., O'Sullivan G.C., Collins J.K.,
RA Higgins D., Shanahan F., Fitzgerald G.F., van Sinderen D., O'Toole P.W.;
RT "Multireplicon genome architecture of Lactobacillus salivarius.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:6718-6723(2006).
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}.
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DR EMBL; CP000233; ABD99321.1; -; Genomic_DNA.
DR RefSeq; WP_003699817.1; NC_007929.1.
DR RefSeq; YP_535404.1; NC_007929.1.
DR AlphaFoldDB; Q1WUL4; -.
DR SMR; Q1WUL4; -.
DR STRING; 362948.LSL_0512; -.
DR EnsemblBacteria; ABD99321; ABD99321; LSL_0512.
DR GeneID; 57059002; -.
DR KEGG; lsl:LSL_0512; -.
DR PATRIC; fig|362948.14.peg.590; -.
DR HOGENOM; CLU_047155_0_2_9; -.
DR OMA; DAGMMDC; -.
DR Proteomes; UP000006559; Chromosome.
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; PS01126; EF_TS_1; 1.
DR PROSITE; PS01127; EF_TS_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Elongation factor; Protein biosynthesis; Reference proteome.
FT CHAIN 1..291
FT /note="Elongation factor Ts"
FT /id="PRO_1000006117"
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 291 AA; 31688 MW; 116EAC452DE59619 CRC64;
MAKISAAQVK ELRDKTGVGM MDAKKALVAV EGDMEKAIDF LREKGMAKAA KKSDRVAAEG
LANVAVNGNK AVIVEVNAET DFVAQNDQFK ALVKHIADVI AENTPADVEA ALQLKTDKGT
LNDELIEATQ VIGEKISLRR FEVVEKADAD NFGAYLHDGG RIAVLSVVEG ADEATAKDVA
MHVAAINPKY VNRDEVPEAE VAHEKEVLTE EAKNEGKPEK IIEKMVAGRL NKFFAEVALD
DQDFVKDPDL TVAKYVASKN GKVKSFVRYE VGEGIEKKEE NFAEEVMSQI K