ID   EFTS_STAES              Reviewed;         292 AA.
AC   Q8CPG8;
DT   28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 109.
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=SE_0933;
OS   Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12228 / FDA PCI 1200;
RX   PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA   Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA   Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA   Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT   "Genome-based analysis of virulence genes in a non-biofilm-forming
RT   Staphylococcus epidermidis strain (ATCC 12228).";
RL   Mol. Microbiol. 49:1577-1593(2003).
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; AE015929; AAO04530.1; -; Genomic_DNA.
DR   RefSeq; NP_764488.1; NC_004461.1.
DR   RefSeq; WP_002439509.1; NZ_WBME01000001.1.
DR   AlphaFoldDB; Q8CPG8; -.
DR   SMR; Q8CPG8; -.
DR   STRING; 176280.SE_0933; -.
DR   EnsemblBacteria; AAO04530; AAO04530; SE_0933.
DR   GeneID; 50018931; -.
DR   KEGG; sep:SE_0933; -.
DR   PATRIC; fig|176280.10.peg.908; -.
DR   eggNOG; COG0264; Bacteria.
DR   HOGENOM; CLU_047155_0_2_9; -.
DR   OMA; DAGMMDC; -.
DR   Proteomes; UP000001411; 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.
FT   CHAIN           1..292
FT                   /note="Elongation factor Ts"
FT                   /id="PRO_0000161201"
FT   REGION          79..82
FT                   /note="Involved in Mg(2+) ion dislocation from EF-Tu"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00050"
SQ   SEQUENCE   292 AA;  32511 MW;  928CB226B708CAD9 CRC64;
     MAISAKLVKE LREKTGAGMM DCKKALTETD GDIDKAIDYL REKGIAKAAK KADRIAAEGL
     VHVEVKDNEA AIVEINSETD FVARNEGFQE LVKEIANHIL DSKVETVDAL MESKLSSGKT
     VDERMKEAIS TIGEKLSIRR FSIRTKTDND AFGAYLHMGG RIGVLTVVEG TTDEEAAKDV
     AMHIAAINPK YVSSEQVSEE EINHEREVLK QQALNEGKPE KIVEKMVEGR LRKYLQEICA
     VDQNFVKNPD ETVEAFLKAK GGKLTDFVRY EVGEGMEKRE ENFAEEVKGQ MK