ID   EFTS_AYWBP              Reviewed;         274 AA.
AC   Q2NIS3;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   03-AUG-2022, entry version 89.
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=AYWB_553;
OS   Aster yellows witches'-broom phytoplasma (strain AYWB).
OC   Bacteria; Tenericutes; Mollicutes; Acholeplasmatales; Acholeplasmataceae;
OC   Candidatus Phytoplasma; Candidatus Phytoplasma asteris.
OX   NCBI_TaxID=322098;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AYWB;
RX   PubMed=16672622; DOI=10.1128/jb.188.10.3682-3696.2006;
RA   Bai X., Zhang J., Ewing A., Miller S.A., Jancso Radek A., Shevchenko D.V.,
RA   Tsukerman K., Walunas T., Lapidus A., Campbell J.W., Hogenhout S.A.;
RT   "Living with genome instability: the adaptation of phytoplasmas to diverse
RT   environments of their insect and plant hosts.";
RL   J. Bacteriol. 188:3682-3696(2006).
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; CP000061; ABC65670.1; -; Genomic_DNA.
DR   RefSeq; WP_011412832.1; NC_007716.1.
DR   AlphaFoldDB; Q2NIS3; -.
DR   SMR; Q2NIS3; -.
DR   STRING; 322098.AYWB_553; -.
DR   EnsemblBacteria; ABC65670; ABC65670; AYWB_553.
DR   KEGG; ayw:AYWB_553; -.
DR   eggNOG; COG0264; Bacteria.
DR   HOGENOM; CLU_047155_0_2_14; -.
DR   OMA; DAGMMDC; -.
DR   OrthoDB; 1405357at2; -.
DR   PhylomeDB; Q2NIS3; -.
DR   Proteomes; UP000001934; 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.
FT   CHAIN           1..274
FT                   /note="Elongation factor Ts"
FT                   /id="PRO_0000241461"
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;  31169 MW;  8A75BE1FFB4B45EF CRC64;
     MKITAEMIKD LRQKTHAGMN ECHKALQQTE GNIEKAIVFL REKGIIKAAQ KQGRVTSEGI
     TNIVFAGNNA FLYEINSETD FVSKNEHFQQ LVKMLGEIIL KKQLSNVKDL LAFNYQNKTV
     QELLFEKTSV LGENITLKRV LKVTKKPQES FGIYKHQGGR ISVLVVLKND CPSVSEDIAM
     HIAASKPQFL TPDKVDPTFL AEEKKILHKQ AAKELSDKPA QMIEKIIENR LGKMLKDMCL
     SEQPFVKNAD QKVKDYLKAN NTDVVYYVRW EMGN