ID   EFTS_COREF              Reviewed;         275 AA.
AC   Q8FP71;
DT   25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   04-NOV-2026, entry version 115.
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=CE1914;
OS   Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189
OS   / NBRC 100395).
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=196164;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395;
RX   PubMed=12840036; DOI=10.1101/gr.1285603;
RA   Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S.,
RA   Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.;
RT   "Comparative complete genome sequence analysis of the amino acid
RT   replacements responsible for the thermostability of Corynebacterium
RT   efficiens.";
RL   Genome Res. 13:1572-1579(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; BA000035; BAC18724.1; -; Genomic_DNA.
DR   RefSeq; WP_006767915.1; NC_004369.1.
DR   AlphaFoldDB; Q8FP71; -.
DR   SMR; Q8FP71; -.
DR   STRING; 196164.gene:10742342; -.
DR   KEGG; cef:CE1914; -.
DR   eggNOG; COG0264; Bacteria.
DR   HOGENOM; CLU_047155_0_0_11; -.
DR   OMA; AACPYVN; -.
DR   OrthoDB; 9808348at2; -.
DR   Proteomes; UP000001409; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
DR   CDD; cd14275; UBA_EF-Ts; 1.
DR   FunFam; 1.10.286.20:FF:000001; Elongation factor Ts; 1.
DR   FunFam; 1.10.8.10:FF:000001; Elongation factor Ts; 1.
DR   Gene3D; 1.10.286.20; -; 1.
DR   Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR   Gene3D; 3.30.479.20; Elongation factor Ts, dimerisation domain; 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   NCBIfam; TIGR00116; tsf; 1.
DR   PANTHER; PTHR11741; ELONGATION FACTOR TS; 1.
DR   PANTHER; PTHR11741:SF0; ELONGATION FACTOR TS, MITOCHONDRIAL; 1.
DR   Pfam; PF00889; EF_TS; 1.
DR   SUPFAM; SSF54713; Elongation factor Ts (EF-Ts), dimerisation domain; 1.
DR   SUPFAM; SSF46934; UBA-like; 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..275
FT                   /note="Elongation factor Ts"
FT                   /id="PRO_0000161111"
FT   REGION          76..79
FT                   /note="Involved in Mg(2+) ion dislocation from EF-Tu"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00050"
SQ   SEQUENCE   275 AA;  29412 MW;  DEFFC2BD01A0FE0A CRC64;
     MANYTAADVK KLRELTGSGM LDCKKALEES AGDFDKAVEI LRIKGAKDVG KRAERNATEG
     LVAVSGNTMI EVNSETDFVA KNDEFKNFAA KIAEAAAAAK ANSPEELAAV DVDGQSAQDA
     LQEFSAKIGE KLELRRAVTL EGDNVAVYLH HRSADLPPSV GVLVAYTGEG EEAEAAARQA
     AMQIAALRAS YLTREDVPAE VIEKERSIAE QITREEGKPE QAIPKIVEGR LNGFYKENVL
     LEQASVADSK KTVKALLDEA GATVTAFARF EVGQA
//