ID   EFTS_CLOPE              Reviewed;         303 AA.
AC   Q8XJQ7;
DT   10-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   25-MAY-2022, entry version 111.
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=CPE1699;
OS   Clostridium perfringens (strain 13 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=195102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=13 / Type A;
RX   PubMed=11792842; DOI=10.1073/pnas.022493799;
RA   Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T.,
RA   Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
RT   "Complete genome sequence of Clostridium perfringens, an anaerobic flesh-
RT   eater.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002).
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; BA000016; BAB81405.1; -; Genomic_DNA.
DR   RefSeq; WP_003459744.1; NC_003366.1.
DR   AlphaFoldDB; Q8XJQ7; -.
DR   SMR; Q8XJQ7; -.
DR   STRING; 195102.gene:10490963; -.
DR   EnsemblBacteria; BAB81405; BAB81405; BAB81405.
DR   GeneID; 29570946; -.
DR   KEGG; cpe:CPE1699; -.
DR   HOGENOM; CLU_047155_2_0_9; -.
DR   OMA; DAGMMDC; -.
DR   Proteomes; UP000000818; 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.
DR   PROSITE; PS01127; EF_TS_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Elongation factor; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..303
FT                   /note="Elongation factor Ts"
FT                   /id="PRO_0000161108"
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   303 AA;  33187 MW;  1EE989D0432BD7AA CRC64;
     MITAKAVKEL RERTGAGMMD CKKALTETNG DMEKAVEVLR EKGLAAAAKK AGRVAAEGIV
     KTYVSEDMKK GSIVEINCET DFVALNEEFV GFAGRVAELV ANSNVNTVEE LLAEKLDGDK
     TVQEVLTELI AKIGENMSVR RFERFSVESG LVQSYIHGGG RIGVMAELAC EASSPVLAEV
     AKDVCMQIAA ANPLFLSEAD VDQESLEKEK EIYRAQALNE GKPEHIVDKM VMGRIKKYCK
     EVCLLDQAWV KDGDKSIAKL LEEKSKEVGS PITITKFVRF ERGEGIEKKE ENFAEEVAKM
     GGK