ID   EFTS_ONYPE              Reviewed;         274 AA.
AC   P61337;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 2.
DT   03-AUG-2022, entry version 103.
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=PAM_166;
OS   Onion yellows phytoplasma (strain OY-M).
OC   Bacteria; Tenericutes; Mollicutes; Acholeplasmatales; Acholeplasmataceae;
OC   Candidatus Phytoplasma; Candidatus Phytoplasma asteris.
OX   NCBI_TaxID=262768;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OY-M;
RX   PubMed=14661021; DOI=10.1038/ng1277;
RA   Oshima K., Kakizawa S., Nishigawa H., Jung H.-Y., Wei W., Suzuki S.,
RA   Arashida R., Nakata D., Miyata S., Ugaki M., Namba S.;
RT   "Reductive evolution suggested from the complete genome sequence of a
RT   plant-pathogenic phytoplasma.";
RL   Nat. Genet. 36:27-29(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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD04251.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AP006628; BAD04251.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; P61337; -.
DR   SMR; P61337; -.
DR   STRING; 262768.PAM_166; -.
DR   EnsemblBacteria; BAD04251; BAD04251; PAM_166.
DR   KEGG; poy:PAM_166; -.
DR   eggNOG; COG0264; Bacteria.
DR   HOGENOM; CLU_047155_0_2_14; -.
DR   OMA; DAGMMDC; -.
DR   OrthoDB; 1405357at2; -.
DR   BioCyc; OYEL262768:G1G26-205-MON; -.
DR   Proteomes; UP000002523; 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; 1.
DR   TIGRFAMs; TIGR00116; tsf; 1.
DR   PROSITE; PS01127; EF_TS_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Elongation factor; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..274
FT                   /note="Elongation factor Ts"
FT                   /id="PRO_0000161166"
FT   REGION          79..82
FT                   /note="Involved in Mg(2+) ion dislocation from EF-Tu"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00050"
SQ   SEQUENCE   274 AA;  31019 MW;  8A8F962270A4D8AB CRC64;
     MKITAEMIKD LRQKTHAGMK ECHKALQQTE GNIEKAIVFL REKGIIKAAQ KQGRATSEGI
     TNIVFDGNNA FLYEINSETD FVSKNEHFQQ LVKVLGEIIL KNQLSNAKDL LAFNYQNKTV
     QELLLEKTSV LGENITLKRV LKVTKKPQES FGTYKHQGGR ISVLVVLKND CPSVSEDIAM
     HIAASKPQFL TPDKVDPTFL AEEKKILHKQ TAKELSDKPA QMIEKIVENR LGKMLKDMCL
     SEQPFVKNAD QKVKDYLKAN NTDVVSYVRW EMGN