ID   EFTS_THEVB              Reviewed;         297 AA.
AC   Q8DIA3;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 105.
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=tll1687;
OS   Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1).
OC   Bacteria; Cyanobacteria; Pseudanabaenales; Thermosynechococcaceae;
OC   Thermosynechococcus.
OX   NCBI_TaxID=197221;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX   PubMed=12240834; DOI=10.1093/dnares/9.4.123;
RA   Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
RA   Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C.,
RA   Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M.,
RA   Takeuchi C., Yamada M., Tabata S.;
RT   "Complete genome structure of the thermophilic cyanobacterium
RT   Thermosynechococcus elongatus BP-1.";
RL   DNA Res. 9:123-130(2002).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BA000039; BAC09239.1; -; Genomic_DNA.
DR   RefSeq; NP_682477.1; NC_004113.1.
DR   RefSeq; WP_011057524.1; NC_004113.1.
DR   AlphaFoldDB; Q8DIA3; -.
DR   SMR; Q8DIA3; -.
DR   STRING; 197221.22295412; -.
DR   PRIDE; Q8DIA3; -.
DR   EnsemblBacteria; BAC09239; BAC09239; BAC09239.
DR   KEGG; tel:tll1687; -.
DR   PATRIC; fig|197221.4.peg.1768; -.
DR   eggNOG; COG0264; Bacteria.
DR   OMA; DAGMMDC; -.
DR   OrthoDB; 1405357at2; -.
DR   Proteomes; UP000000440; 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; -; 1.
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; 2.
DR   SUPFAM; SSF46934; SSF46934; 1.
DR   SUPFAM; SSF54713; SSF54713; 1.
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..297
FT                   /note="Elongation factor Ts"
FT                   /id="PRO_0000161216"
FT   REGION          82..85
FT                   /note="Involved in Mg(2+) ion dislocation from EF-Tu"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00050"
FT   REGION          223..297
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   297 AA;  32068 MW;  23C63E5A1AF8EDEC CRC64;
     MAEISAKLVK ELRDKTGAGM MDCKKALQES NGDMEAAITW LRQKGLASAG KKAGRVTSEG
     LVDSYIHTGG RIGVLVEVNC ETDFVARNEK FKTLVQDIAK QIAACPNVEF VSLDDIPAEY
     KEKERQIALG SDALKGKPPE VQEKIVAGKL EKTLKELCLL YQPFIRDQSK TVEELVKEHI
     AELGENIRIR RFQRFVLGEG IEKQETNLAE EVAAQTQAMR AAAQTAAAAE TAPPEVSEPE
     PAAAVTAEEP TPEPVAAAEQ PAEPVSELVE QPGAESKGFG AATKKSGGKS RSNKKKK