ID   EFTS_CAMJE              Reviewed;         357 AA.
AC   Q9PNB4; Q0P975;
DT   10-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-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=Cj1181c;
OS   Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS   11168).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=192222;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700819 / NCTC 11168;
RX   PubMed=10688204; DOI=10.1038/35001088;
RA   Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA   Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA   Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA   Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA   Barrell B.G.;
RT   "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT   reveals hypervariable sequences.";
RL   Nature 403:665-668(2000).
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; AL111168; CAL35296.1; -; Genomic_DNA.
DR   PIR; G81323; G81323.
DR   RefSeq; WP_002864836.1; NC_002163.1.
DR   RefSeq; YP_002344572.1; NC_002163.1.
DR   AlphaFoldDB; Q9PNB4; -.
DR   SMR; Q9PNB4; -.
DR   STRING; 192222.Cj1181c; -.
DR   PaxDb; Q9PNB4; -.
DR   PRIDE; Q9PNB4; -.
DR   EnsemblBacteria; CAL35296; CAL35296; Cj1181c.
DR   GeneID; 905471; -.
DR   KEGG; cje:Cj1181c; -.
DR   PATRIC; fig|192222.6.peg.1162; -.
DR   eggNOG; COG0264; Bacteria.
DR   HOGENOM; CLU_047155_0_1_7; -.
DR   OMA; DAGMMDC; -.
DR   Proteomes; UP000000799; 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; -; 3.
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; 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..357
FT                   /note="Elongation factor Ts"
FT                   /id="PRO_0000161097"
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;  39555 MW;  F9A87A95188B0B31 CRC64;
     MTEITAAMVK ELRESTGAGM MDCKNALSET NGDFDKAVQL LREKGLGKAA KKADRLAAEG
     LVSVKVSDDF TSATVSEINS ETDFVAKNDQ FIALTKDTTA HIQSNSLQSV EELHSSTING
     VKFEEYLKSQ IATIGENLVV RRFATLKAGA NGVVNGYIHT NGRVGVVIAA ACDSAEVASK
     SRDLLRQICM HIAAMRPSYL SYEDLDMTFV ENEYKALVAE LEKENEERRR LKDPNKPEHK
     IPQFASRKQL SDAILKEAEE KIKEELKAQG KPEKIWDNII PGKMNSFIAD NSQLDSKLTL
     MGQFYVMDDK KTVEQVIAEK EKEFGGKIKI VEFICFEVGE GLEKKTEDFA AEVAAQL