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EFTS_MYCMO
ID   EFTS_MYCMO              Reviewed;         294 AA.
AC   Q6KIB3;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Elongation factor Ts {ECO:0000255|HAMAP-Rule:MF_00050};
DE            Short=EF-Ts {ECO:0000255|HAMAP-Rule:MF_00050};
GN   Name=tsf {ECO:0000255|HAMAP-Rule:MF_00050}; OrderedLocusNames=MMOB1770;
OS   Mycoplasma mobile (strain ATCC 43663 / 163K / NCTC 11711) (Mesomycoplasma
OS   mobile).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mesomycoplasma.
OX   NCBI_TaxID=267748;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43663 / 163K / NCTC 11711;
RX   PubMed=15289470; DOI=10.1101/gr.2674004;
RA   Jaffe J.D., Stange-Thomann N., Smith C., DeCaprio D., Fisher S., Butler J.,
RA   Calvo S., Elkins T., FitzGerald M.G., Hafez N., Kodira C.D., Major J.,
RA   Wang S., Wilkinson J., Nicol R., Nusbaum C., Birren B., Berg H.C.,
RA   Church G.M.;
RT   "The complete genome and proteome of Mycoplasma mobile.";
RL   Genome Res. 14:1447-1461(2004).
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.
CC       {ECO:0000255|HAMAP-Rule:MF_00050}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00050}.
CC   -!- SIMILARITY: Belongs to the EF-Ts family. {ECO:0000255|HAMAP-
CC       Rule:MF_00050}.
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DR   EMBL; AE017308; AAT27663.1; -; Genomic_DNA.
DR   RefSeq; WP_011264697.1; NC_006908.1.
DR   AlphaFoldDB; Q6KIB3; -.
DR   SMR; Q6KIB3; -.
DR   STRING; 267748.MMOB1770; -.
DR   EnsemblBacteria; AAT27663; AAT27663; MMOB1770.
DR   KEGG; mmo:MMOB1770; -.
DR   eggNOG; COG0264; Bacteria.
DR   HOGENOM; CLU_047155_0_2_14; -.
DR   OMA; HTTRQLC; -.
DR   OrthoDB; 1405357at2; -.
DR   Proteomes; UP000009072; 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; IPR015940; UBA.
DR   InterPro; IPR009060; UBA-like_sf.
DR   PANTHER; PTHR11741; PTHR11741; 1.
DR   Pfam; PF00889; EF_TS; 1.
DR   SMART; SM00165; UBA; 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..294
FT                   /note="Elongation factor Ts"
FT                   /id="PRO_0000161154"
FT   REGION          78..81
FT                   /note="Involved in Mg(2+) ion dislocation from EF-Tu"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00050"
SQ   SEQUENCE   294 AA;  33328 MW;  3A5CF04AD3B51C95 CRC64;
     MVDAEKIKKL REMTDSGFLD CKKALEATKN DLNAAVKWLQ ENGKAKAAKK ADRITAEGLV
     AAFSNDKYGV IIEINSETDF VAKNQKFKDL VNKIGQELLK HDFYKYKNII EEVKIGNETL
     AELVASASAT IGEKLTFRRA EQVKKFNSKQ VIGVYNHFDG QKAAVLIIEN GTEDMAKQLS
     MHITAMNPLF LDEKEVPEKE IKKLRSEFEK DEQIQLKPEK IRPKIIEGMI NKKLSETTFT
     LQEFVVEPGQ SIKQYMNSKN SFPISKIRYE VGEGIEKQVV DFASEVANQM KNKA
 
 
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