ID   EFTS_CAMC5              Reviewed;         354 AA.
AC   A7GWR8;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   25-MAY-2022, entry version 75.
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=Ccur92_03560;
GN   ORFNames=CCV52592_1261;
OS   Campylobacter curvus (strain 525.92).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=360105;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=525.92;
RA   Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G.,
RA   Mandrell R.E., Lastovica A.J., Nelson K.E.;
RT   "Genome sequence of Campylobacter curvus 525.92 isolated from human
RT   feces.";
RL   Submitted (JUL-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; CP000767; EAU00944.1; -; Genomic_DNA.
DR   RefSeq; WP_009651037.1; NC_009715.2.
DR   AlphaFoldDB; A7GWR8; -.
DR   SMR; A7GWR8; -.
DR   STRING; 360105.CCV52592_1261; -.
DR   EnsemblBacteria; EAU00944; EAU00944; CCV52592_1261.
DR   KEGG; ccv:CCV52592_1261; -.
DR   HOGENOM; CLU_047155_0_1_7; -.
DR   OMA; DAGMMDC; -.
DR   OrthoDB; 1405357at2; -.
DR   Proteomes; UP000006380; 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; Reference proteome.
FT   CHAIN           1..354
FT                   /note="Elongation factor Ts"
FT                   /id="PRO_0000323446"
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;  39408 MW;  1150EF8C96874910 CRC64;
     MEITAQMVKE LRESTGAGMM DCKKALSEAD GDMQKAVDIL REKGLGQAAK KADRLASEGL
     VSVEVCEHCK RATISEINSE TDFVARNPQF QALTKDTTAH IQAKGITSVE ELNESTLNGV
     KFEEYFKTQI ATIGENLVVR RFETISADEK GVVNGYVHSN GRVGVLIGAA CQSEEVAQKA
     AEFIRNLCMH AAAMKPTVIS YKDLEKDFVE KEFIALKAEL EKENEELKRL GKPLHHIPRF
     ASRSQITPEI LAGVENEIKE ELKAEGKPEK IWDKIIPGKI ERFYADNTIL DQRLTLLGQF
     YVMDDKKTIE QVLAEKSKEL GGKIEIVKYV RFELGEGLEK KVDDFAAEVA AQIG