ID   EFTS_CLOK5              Reviewed;         306 AA.
AC   A5N829;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   25-MAY-2022, entry version 82.
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=CKL_1418;
OS   Clostridium kluyveri (strain ATCC 8527 / DSM 555 / NCIMB 10680).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=431943;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8527 / DSM 555 / NCIMB 10680;
RX   PubMed=18218779; DOI=10.1073/pnas.0711093105;
RA   Seedorf H., Fricke W.F., Veith B., Brueggemann H., Liesegang H.,
RA   Strittmatter A., Miethke M., Buckel W., Hinderberger J., Li F.,
RA   Hagemeier C., Thauer R.K., Gottschalk G.;
RT   "The genome of Clostridium kluyveri, a strict anaerobe with unique
RT   metabolic features.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:2128-2133(2008).
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; CP000673; EDK33460.1; -; Genomic_DNA.
DR   RefSeq; WP_012101807.1; NC_009706.1.
DR   AlphaFoldDB; A5N829; -.
DR   SMR; A5N829; -.
DR   STRING; 431943.CKL_1418; -.
DR   EnsemblBacteria; EDK33460; EDK33460; CKL_1418.
DR   KEGG; ckl:CKL_1418; -.
DR   eggNOG; COG0264; Bacteria.
DR   HOGENOM; CLU_047155_0_0_9; -.
DR   OMA; DAGMMDC; -.
DR   OrthoDB; 1405357at2; -.
DR   Proteomes; UP000002411; 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; 3.
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.
PE   3: Inferred from homology;
KW   Cytoplasm; Elongation factor; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..306
FT                   /note="Elongation factor Ts"
FT                   /id="PRO_1000074858"
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   306 AA;  33953 MW;  56E72914151E5F18 CRC64;
     MITAQMVKEL RERTGAGMMD CKKALNEAGG DSEKAIEILR EKGLAAAAKK SGRIASEGLV
     KTYISEDGKV ASIVEVNCET DFVAVNADFV NFVDNLAKQI SLSESTTVEE LSEEKYISDD
     SKTVSETLVN LISKLGENMA IRRFERLAVS KGLIESYIHG GGRIGVLVKL ECEKESEILK
     EVAKDVAMQV AATNPLFLSK DTVDSATLDK EKEIFKVQAL NEGKPEKIAE KIVIGRVQKY
     YKENCLIEQL WVKDSDLTID KYLKSKSKEV GAPIKISNFI RFEKGEGIEK KEEDFAEEVR
     KQIEGK