ID   EFTS_TREPA              Reviewed;         290 AA.
AC   O83614;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   25-MAY-2022, entry version 127.
DE   RecName: Full=Elongation factor Ts;
DE            Short=EF-Ts;
GN   Name=tsf; OrderedLocusNames=TP_0605;
OS   Treponema pallidum (strain Nichols).
OC   Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX   NCBI_TaxID=243276;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nichols;
RX   PubMed=9665876; DOI=10.1126/science.281.5375.375;
RA   Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G.,
RA   Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A.,
RA   Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D.,
RA   Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M., Utterback T.R.,
RA   McDonald L.A., Artiach P., Bowman C., Cotton M.D., Fujii C., Garland S.A.,
RA   Hatch B., Horst K., Roberts K.M., Sandusky M., Weidman J.F., Smith H.O.,
RA   Venter J.C.;
RT   "Complete genome sequence of Treponema pallidum, the syphilis spirochete.";
RL   Science 281:375-388(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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE000520; AAC65578.1; -; Genomic_DNA.
DR   PIR; G71304; G71304.
DR   RefSeq; WP_010882051.1; NC_021490.2.
DR   AlphaFoldDB; O83614; -.
DR   SMR; O83614; -.
DR   IntAct; O83614; 1.
DR   STRING; 243276.TPANIC_0605; -.
DR   EnsemblBacteria; AAC65578; AAC65578; TP_0605.
DR   GeneID; 57879128; -.
DR   KEGG; tpa:TP_0605; -.
DR   eggNOG; COG0264; Bacteria.
DR   HOGENOM; CLU_047155_0_0_12; -.
DR   OMA; DAGMMDC; -.
DR   OrthoDB; 1405357at2; -.
DR   Proteomes; UP000000811; 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; 1.
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..290
FT                   /note="Elongation factor Ts"
FT                   /id="PRO_0000161225"
FT   REGION          87..90
FT                   /note="Involved in Mg(2+) ion dislocation from EF-Tu"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   290 AA;  31783 MW;  14B9386AF3E42884 CRC64;
     MEIAARDVKS LRDKTGAGMM ECKRALQECA GDALCAEKYL KERGLAAIEN RRGRATAEGV
     IVIKARHAEG AACGASAVAM VELVCETDFV AKNAEFIALA ERIAQAVLEH AYTEVNQVLR
     DMVVDLATRV RENMSLTRLA LLRAGSAGAG QYLSHYVHPD KKTGVVLSFS SDAPDVFLRS
     DVRAFAYDCC LHAAAYTPRY VRAEDVPAEY VREQREVFQA HVASLQKPAH VKESIVQGKL
     EKHLAEICFL KQPFVKDDKL SVEKKMAEVG ARAGGALRFT QALIYQLGVQ