ID   EFTS_HELPJ              Reviewed;         355 AA.
AC   Q9ZJ71;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 123.
DE   RecName: Full=Elongation factor Ts;
DE            Short=EF-Ts;
GN   Name=tsf; OrderedLocusNames=jhp_1444;
OS   Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=85963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J99 / ATCC 700824;
RX   PubMed=9923682; DOI=10.1038/16495;
RA   Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C.,
RA   Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J.,
RA   Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D.,
RA   Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.;
RT   "Genomic sequence comparison of two unrelated isolates of the human gastric
RT   pathogen Helicobacter pylori.";
RL   Nature 397:176-180(1999).
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; AE001439; AAD07029.1; -; Genomic_DNA.
DR   PIR; G71804; G71804.
DR   RefSeq; WP_000014467.1; NZ_CP011330.1.
DR   AlphaFoldDB; Q9ZJ71; -.
DR   SMR; Q9ZJ71; -.
DR   STRING; 85963.jhp_1444; -.
DR   EnsemblBacteria; AAD07029; AAD07029; jhp_1444.
DR   KEGG; hpj:jhp_1444; -.
DR   PATRIC; fig|85963.30.peg.1099; -.
DR   eggNOG; COG0264; Bacteria.
DR   OMA; DAGMMDC; -.
DR   Proteomes; UP000000804; 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; 1.
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.
FT   CHAIN           1..355
FT                   /note="Elongation factor Ts"
FT                   /id="PRO_0000161132"
FT   REGION          82..85
FT                   /note="Involved in Mg(2+) ion dislocation from EF-Tu"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   355 AA;  39859 MW;  36DE2A8F16EB3FD5 CRC64;
     MSGISAQLVK KLRDLTDAGM MDCKKALVEV AGDLQKAIDF LREKGLSKAA KKADRIAAEG
     VVALEVAPDF KSAMMVEINS ETDFVAKNEG FKELVKKTLE TIKTHNIHTT EELLKSPLDN
     KPFEEYLHSQ IAVIGENILV RKIAHLKAPS SHIINGYAHS NARVGVLIAI EYNNEKNAPK
     VVELARNIAM HAAAMKPQVL DCKDFSLDFV KKETLALIAE IEKDNEEAKR LGKPLKNIPT
     FGSRIELSDE VLAHQKKAFE DELKEQGKPE KIWDKIVPGK MERFIADNTL IDQRLTLLGQ
     FYVMDDKKTI AQVIADCSKE WDDNLKITEY VRFELGEGIE KKTENFAEEV ALQMK