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