ID   EFTS_BIFLO              Reviewed;         283 AA.
AC   Q8G485;
DT   20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 95.
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=BL1504;
OS   Bifidobacterium longum (strain NCC 2705).
OC   Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC   Bifidobacterium.
OX   NCBI_TaxID=206672;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCC 2705;
RX   PubMed=12381787; DOI=10.1073/pnas.212527599;
RA   Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B., Pessi G.,
RA   Zwahlen M.-C., Desiere F., Bork P., Delley M., Pridmore R.D., Arigoni F.;
RT   "The genome sequence of Bifidobacterium longum reflects its adaptation to
RT   the human gastrointestinal tract.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(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}.
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DR   EMBL; AE014295; AAN25299.1; -; Genomic_DNA.
DR   RefSeq; NP_696663.1; NC_004307.2.
DR   RefSeq; WP_007052754.1; NC_004307.2.
DR   AlphaFoldDB; Q8G485; -.
DR   SMR; Q8G485; -.
DR   STRING; 206672.BL1504; -.
DR   EnsemblBacteria; AAN25299; AAN25299; BL1504.
DR   GeneID; 66505328; -.
DR   KEGG; blo:BL1504; -.
DR   PATRIC; fig|206672.9.peg.376; -.
DR   HOGENOM; CLU_047155_0_0_11; -.
DR   OMA; DAGMMDC; -.
DR   PhylomeDB; Q8G485; -.
DR   Proteomes; UP000000439; 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..283
FT                   /note="Elongation factor Ts"
FT                   /id="PRO_0000161083"
FT   REGION          84..87
FT                   /note="Involved in Mg(2+) ion dislocation from EF-Tu"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00050"
SQ   SEQUENCE   283 AA;  29979 MW;  7CA7AFB5939E0617 CRC64;
     MAAITAALIK QVREDTGAGM LDVKKALTEA EGDVARAKEI IRAKGIAAAG KREGRKAQEG
     TIASKVVETA NGETGYAVEL NSETDFVAKT PKFVEFTEEV LGYAVDADAN SADELLEAKA
     GDTTVKLAVE EAAALFGEHV KVGQFAKISG EHVEVYAHKK SAEMPPSIVA MIATDKAGAA
     VAHEAALQIS AMGAKWLTRE DVPADVVESE RRVATEKSLA EGKPEKIVPK IVEGRLNAFF
     KEVVLLEQPF VKDPSKTVGD LFKEVGGNAT AFARVEVGKG EEE