ID   EFTS_MYCLE              Reviewed;         276 AA.
AC   O33039;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 120.
DE   RecName: Full=Elongation factor Ts;
DE            Short=EF-Ts;
GN   Name=tsf; OrderedLocusNames=ML1597; ORFNames=MLCB250.64;
OS   Mycobacterium leprae (strain TN).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=272631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TN;
RX   PubMed=11234002; DOI=10.1038/35059006;
RA   Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA   Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA   Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA   Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA   Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA   Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA   Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA   Barrell B.G.;
RT   "Massive gene decay in the leprosy bacillus.";
RL   Nature 409:1007-1011(2001).
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; Z97369; CAB10658.1; -; Genomic_DNA.
DR   EMBL; AL583922; CAC30548.1; -; Genomic_DNA.
DR   PIR; G87108; G87108.
DR   RefSeq; NP_302100.1; NC_002677.1.
DR   RefSeq; WP_010908421.1; NC_002677.1.
DR   AlphaFoldDB; O33039; -.
DR   SMR; O33039; -.
DR   STRING; 272631.ML1597; -.
DR   EnsemblBacteria; CAC30548; CAC30548; CAC30548.
DR   KEGG; mle:ML1597; -.
DR   PATRIC; fig|272631.5.peg.3010; -.
DR   Leproma; ML1597; -.
DR   eggNOG; COG0264; Bacteria.
DR   HOGENOM; CLU_047155_0_0_11; -.
DR   OMA; DAGMMDC; -.
DR   Proteomes; UP000000806; 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..276
FT                   /note="Elongation factor Ts"
FT                   /id="PRO_0000161153"
FT   REGION          76..79
FT                   /note="Involved in Mg(2+) ion dislocation from EF-Tu"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   276 AA;  29156 MW;  6FF0B37E5E5E1BD5 CRC64;
     MANFTVADVK RLRALTGAGM LDCKSVLVET DGNFDKAVES LRIKGAKDVG KRAERATAEG
     LVAAKDGALI ELNCETDFVA KNAEFQKLAN QIVGVVAAAK IVDVDALKGA SVGDKTVEQA
     IAELAAKIGE KLKLRRAAIF NGTVATYLHK RAADLPPAVG VLVEYGAGTD AANSTAAAHA
     AALQIAALKA RFLSRDDVPE DVLASERRIA EETAKAAGKP EQSLPKIVEG RLNGFFKDSV
     LLEQPSVFDN KKTVKVLLDE AGVTVTRFVR FEVGQA