ID   EFTS_MYCGE              Reviewed;         298 AA.
AC   P47246;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=Elongation factor Ts;
DE            Short=EF-Ts;
GN   Name=tsf; OrderedLocusNames=MG433;
OS   Mycoplasma genitalium (strain ATCC 33530 / DSM 19775 / NCTC 10195 / G37)
OS   (Mycoplasmoides genitalium).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=243273;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX   PubMed=7569993; DOI=10.1126/science.270.5235.397;
RA   Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A.,
RA   Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M.,
RA   Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L.,
RA   Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M.,
RA   Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S.,
RA   Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.;
RT   "The minimal gene complement of Mycoplasma genitalium.";
RL   Science 270:397-403(1995).
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; L43967; AAC72454.1; -; Genomic_DNA.
DR   PIR; H64247; H64247.
DR   RefSeq; WP_009885600.1; NZ_AAGX01000001.1.
DR   AlphaFoldDB; P47246; -.
DR   SMR; P47246; -.
DR   STRING; 243273.MG_433; -.
DR   EnsemblBacteria; AAC72454; AAC72454; MG_433.
DR   KEGG; mge:MG_433; -.
DR   eggNOG; COG0264; Bacteria.
DR   HOGENOM; CLU_047155_0_2_14; -.
DR   OMA; DAGMMDC; -.
DR   OrthoDB; 1405357at2; -.
DR   BioCyc; MGEN243273:G1GJ2-527-MON; -.
DR   Proteomes; UP000000807; 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; 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..298
FT                   /note="Elongation factor Ts"
FT                   /id="PRO_0000161151"
FT   REGION          79..82
FT                   /note="Involved in Mg(2+) ion dislocation from EF-Tu"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   298 AA;  34265 MW;  014E423EBD2A5F7B CRC64;
     MATKIELIKE LRKSTQASVM DCKQALEKNN DDFEKAVKWL RENGIVKSTK KLNKVASEGI
     IVLKSNLHKA IMVEINSQTD FVAKNQELKE FSDLMLEKIF EKVNPKTELV EIEKIQINND
     EKVSEKLALI ASKTDEKIVL RRVVVFETKT NQIFTYLHAN KRIGVIIEIQ GKLNEDDGKH
     LAMHIAANSP QFIDQSDVNQ TWLQNERNII RSQAELEVKE NPKKAIFLEK TIEGRVNKLL
     IDTCLINQKY LIDETKTIGQ FLKEKQAKVL KFIRYEVGEG IIKETVDFVS EVNAQIKQ