ID   EFTS_MICAN              Reviewed;         251 AA.
AC   B0JTL3;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 1.
DT   03-AUG-2022, entry version 77.
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=MAE_44940;
OS   Microcystis aeruginosa (strain NIES-843 / IAM M-2473).
OC   Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC   Microcystaceae; Microcystis.
OX   NCBI_TaxID=449447;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-843 / IAM M-247;
RX   PubMed=18192279; DOI=10.1093/dnares/dsm026;
RA   Kaneko T., Nakajima N., Okamoto S., Suzuki I., Tanabe Y., Tamaoki M.,
RA   Nakamura Y., Kasai F., Watanabe A., Kawashima K., Kishida Y., Ono A.,
RA   Shimizu Y., Takahashi C., Minami C., Fujishiro T., Kohara M., Katoh M.,
RA   Nakazaki N., Nakayama S., Yamada M., Tabata S., Watanabe M.M.;
RT   "Complete genomic structure of the bloom-forming toxic cyanobacterium
RT   Microcystis aeruginosa NIES-843.";
RL   DNA Res. 14:247-256(2007).
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; AP009552; BAG04316.1; -; Genomic_DNA.
DR   RefSeq; WP_002753383.1; NC_010296.1.
DR   AlphaFoldDB; B0JTL3; -.
DR   SMR; B0JTL3; -.
DR   STRING; 449447.MAE_44940; -.
DR   PaxDb; B0JTL3; -.
DR   PRIDE; B0JTL3; -.
DR   EnsemblBacteria; BAG04316; BAG04316; MAE_44940.
DR   KEGG; mar:MAE_44940; -.
DR   eggNOG; COG0264; Bacteria.
DR   HOGENOM; CLU_047155_1_1_3; -.
DR   OMA; DAGMMDC; -.
DR   OrthoDB; 1405357at2; -.
DR   BioCyc; MAER449447:MAE_RS19475-MON; -.
DR   Proteomes; UP000001510; 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; 1.
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..251
FT                   /note="Elongation factor Ts"
FT                   /id="PRO_1000074868"
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          215..251
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   251 AA;  27636 MW;  11C267DEB5BC31D6 CRC64;
     MAEITAQQVK ELREKTGAGM MDCKRALTEN AGDITKAIEW LRQKGITSAE KKASRVAAEG
     MIGSYIHTGS RIGVLVEVNC ETDFVARREE FKKLVNDVAM QIAACPNVEY VKVADIPAEI
     AAKEKEIEMG RDDLANKPDN IKEKIVAGRI EKRLKELSLL DQPFIRDQNI SIDELLKQAI
     AALGENIQVR RFQRFVLGEG IEKEETDFAA EVAAQMGQKA PEPVAAAPQV EEKAPEPAAK
     DNPPAKGKKK K