ID   EFTS_MACCJ              Reviewed;         293 AA.
AC   B9EBD7;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 70.
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=MCCL_0841;
OS   Macrococcus caseolyticus (strain JCSC5402).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae; Macrococcus.
OX   NCBI_TaxID=458233;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCSC5402;
RX   PubMed=19074389; DOI=10.1128/jb.01058-08;
RA   Baba T., Kuwahara-Arai K., Uchiyama I., Takeuchi F., Ito T., Hiramatsu K.;
RT   "Complete genome sequence of Macrococcus caseolyticus strain JCSCS5402,
RT   reflecting the ancestral genome of the human-pathogenic staphylococci.";
RL   J. Bacteriol. 191:1180-1190(2009).
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; AP009484; BAH17548.1; -; Genomic_DNA.
DR   RefSeq; WP_012656748.1; NC_011999.1.
DR   AlphaFoldDB; B9EBD7; -.
DR   SMR; B9EBD7; -.
DR   STRING; 458233.MCCL_0841; -.
DR   PRIDE; B9EBD7; -.
DR   EnsemblBacteria; BAH17548; BAH17548; MCCL_0841.
DR   GeneID; 61129250; -.
DR   KEGG; mcl:MCCL_0841; -.
DR   eggNOG; COG0264; Bacteria.
DR   HOGENOM; CLU_047155_0_2_9; -.
DR   OMA; DAGMMDC; -.
DR   OrthoDB; 1405357at2; -.
DR   Proteomes; UP000001383; 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; 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..293
FT                   /note="Elongation factor Ts"
FT                   /id="PRO_1000117586"
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   293 AA;  32055 MW;  D0F0CF22879E7A78 CRC64;
     MAITAQLVKQ LRERTGAGMM DCKKALTETN GDIDAAVDYL REKGIAKAAK KADRIAAEGT
     TYVASSGNTA VLLELNSETD FVARNEGFQA LVKEMADHIL ATKPADLDAL MASEIETGKT
     VETKLNEAIS TIGEKLTLRR FVLAEKTDAD AFGEYLHMGG RIGVLAVVEN STDAEAAKDV
     AMHIAALNPK FVSREQVSAE ELEHEKEILK QQALNEGKPE NIVEKMVEGR LRKYLEEICA
     VDQPFVKNPD QTVAEFLKSK GGSLKSFVRY EVGEGIEKRQ DNFADEVMGQ MGK