ID   EFTS_CHLTR              Reviewed;         282 AA.
AC   O84686;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   25-MAY-2022, entry version 117.
DE   RecName: Full=Elongation factor Ts;
DE            Short=EF-Ts;
GN   Name=tsf; OrderedLocusNames=CT_679;
OS   Chlamydia trachomatis (strain D/UW-3/Cx).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=272561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D/UW-3/Cx;
RX   PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA   Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA   Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT   "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT   trachomatis.";
RL   Science 282:754-759(1998).
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 (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the EF-Ts family. {ECO:0000305}.
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DR   EMBL; AE001273; AAC68274.1; -; Genomic_DNA.
DR   PIR; F71484; F71484.
DR   RefSeq; NP_220198.1; NC_000117.1.
DR   RefSeq; WP_010725299.1; NC_000117.1.
DR   AlphaFoldDB; O84686; -.
DR   SMR; O84686; -.
DR   STRING; 813.O172_03745; -.
DR   EnsemblBacteria; AAC68274; AAC68274; CT_679.
DR   GeneID; 884475; -.
DR   KEGG; ctr:CT_679; -.
DR   PATRIC; fig|272561.5.peg.746; -.
DR   HOGENOM; CLU_047155_0_0_0; -.
DR   InParanoid; O84686; -.
DR   OMA; DAGMMDC; -.
DR   Proteomes; UP000000431; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003746; F:translation elongation factor activity; IBA:GO_Central.
DR   GO; GO:0006414; P:translational elongation; IBA:GO_Central.
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; 1.
DR   Pfam; PF00889; EF_TS; 1.
DR   SUPFAM; SSF46934; SSF46934; 1.
DR   SUPFAM; SSF54713; SSF54713; 1.
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..282
FT                   /note="Elongation factor Ts"
FT                   /id="PRO_0000161105"
FT   REGION          80..83
FT                   /note="Involved in Mg(2+) ion dislocation from EF-Tu"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   282 AA;  30882 MW;  882A5AF38F0D1F02 CRC64;
     MSDFSMETLK NLRQQTGVGL TKCKEALEHA KGNLEDAVVY LRKLGLASAG KKEHRETKEG
     VIAARVDERG AALVEVNVET DFVANNNVFR AFVTSLLSDL LDHELSDVDA LALVMSSQEP
     SLSVEELKAV TMQTVGENIR ISRAFYTPVN SGQSVGIYSH GNGKAVAIAF LSGSENQEAL
     AKDIAMHIVA SQPQFLSKES VPQEVLERER EVFSSQVAGK PQEVVEKITQ GKFRAFFQEA
     CLLEQAFIKD PEVTIQGLID RAAKASGEPL KVEHFVFWKM GA