ID   EFTS_CAMJD              Reviewed;         357 AA.
AC   A7H2J3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 78.
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};
GN   OrderedLocusNames=JJD26997_0548;
OS   Campylobacter jejuni subsp. doylei (strain ATCC BAA-1458 / RM4099 /
OS   269.97).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=360109;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1458 / RM4099 / 269.97;
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   "Complete genome sequence of Campylobacter jejuni subsp doylei 269.97
RT   isolated from human blood.";
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; CP000768; ABS44242.1; -; Genomic_DNA.
DR   AlphaFoldDB; A7H2J3; -.
DR   SMR; A7H2J3; -.
DR   EnsemblBacteria; ABS44242; ABS44242; JJD26997_0548.
DR   KEGG; cjd:JJD26997_0548; -.
DR   HOGENOM; CLU_047155_0_1_7; -.
DR   OMA; DAGMMDC; -.
DR   Proteomes; UP000002302; 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; 2.
DR   SUPFAM; SSF46934; SSF46934; 1.
DR   SUPFAM; SSF54713; SSF54713; 3.
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..357
FT                   /note="Elongation factor Ts"
FT                   /id="PRO_1000006071"
FT   REGION          82..85
FT                   /note="Involved in Mg(2+) ion dislocation from EF-Tu"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00050"
SQ   SEQUENCE   357 AA;  39616 MW;  5203F799421F3119 CRC64;
     MAEITAAMVK ELRESTGAGM MDCKNALSET NGDFDKAVQL LREKGLGKAA KKADRLAAEG
     LVSVKVSDDF TSATVSEINS ETDFVAKNDQ FIALTKDTTA HIQNNSLQSV EELHSSTING
     VKFEEYLKSQ IATIGENLVV RRFATLKAGA NGVVNGYIHT NGRVGVVIAA ACDSAEVASK
     SRDLLRQICM HIAAMRPSYL SYEDLDMTFV ENEYKALVAE LEKENEERRR LKDPNKPEHK
     IPQFASRKQL SDAILKEAEE KIKEELKTQG KPEKIWDNII PGKMNSFIAD NSQLDSKFTL
     MGQFYVMDDK KTVEQVIAEK EKEFGGKIKI VEFICFEVGE GLEKKTEDFA AEVAAQL