ID   EFTS_CAMC1              Reviewed;         354 AA.
AC   A7ZF27;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 2.
DT   25-MAY-2022, entry version 79.
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=Ccon26_15380;
GN   ORFNames=CCC13826_0550;
OS   Campylobacter concisus (strain 13826).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=360104;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=13826;
RA   Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G.,
RA   Mandrell R.E., On S., Nelson K.E.;
RT   "Genome sequence of Campylobacter concisus 13826 isolated from human
RT   feces.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000792; EAT99242.3; -; Genomic_DNA.
DR   RefSeq; WP_002941206.1; NC_009802.2.
DR   AlphaFoldDB; A7ZF27; -.
DR   SMR; A7ZF27; -.
DR   STRING; 360104.CCC13826_0550; -.
DR   PRIDE; A7ZF27; -.
DR   EnsemblBacteria; EAT99242; EAT99242; CCC13826_0550.
DR   KEGG; cco:CCC13826_0550; -.
DR   eggNOG; COG0264; Bacteria.
DR   HOGENOM; CLU_047155_0_1_7; -.
DR   OMA; DAGMMDC; -.
DR   OrthoDB; 1405357at2; -.
DR   Proteomes; UP000001121; 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; 2.
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..354
FT                   /note="Elongation factor Ts"
FT                   /id="PRO_0000323445"
FT   REGION          81..84
FT                   /note="Involved in Mg(2+) ion dislocation from EF-Tu"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00050"
SQ   SEQUENCE   354 AA;  39139 MW;  B4D9A4C12FB31C72 CRC64;
     MEITAQMVKE LRESTGAGMM DCKKALGEAN GDMEKAVDIL REKGLGQAAK KADRLASEGL
     VSVEVCSKCK KATISEINSE TDFVARNPQF QALAKDTTAH IQSSGIKTVE ELNTSTLNGV
     KFEEYFKTQI ATIGENLVVR RFETISADDK GVVNGYVHSN GRVGVLIGAA CESAEVANKA
     AEFIRNLCMH AAAMKPSVIS YKDLDKDFVE KEFIALRAEL EKENEELKRL GKPLHHIPEY
     ASRCQIGEAE LAKATKAIEE ELKAEGKPEK IWDKIIPGKI ERFYADNTVL DQRLTLLGQF
     YVMDDKKTIE QVIEEKSKEL GGKIEIVKYV RFELGEGLEK KVDDFAAEVA AQIG