ID   EFTS_BORBU              Reviewed;         279 AA.
AC   O51148;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   25-MAY-2022, entry version 132.
DE   RecName: Full=Elongation factor Ts;
DE            Short=EF-Ts;
GN   Name=tsf; OrderedLocusNames=BB_0122;
OS   Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31)
OS   (Borrelia burgdorferi).
OC   Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX   NCBI_TaxID=224326;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RX   PubMed=9403685; DOI=10.1038/37551;
RA   Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA   Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L.,
RA   Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L.,
RA   Peterson J.D., Kerlavage A.R., Quackenbush J., Salzberg S.L., Hanson M.,
RA   van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F.,
RA   Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C.,
RA   Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B.,
RA   Smith H.O., Venter J.C.;
RT   "Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi.";
RL   Nature 390:580-586(1997).
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 (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the EF-Ts family. {ECO:0000305}.
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DR   EMBL; AE000783; AAC66512.1; -; Genomic_DNA.
DR   PIR; B70115; B70115.
DR   RefSeq; NP_212256.1; NC_001318.1.
DR   RefSeq; WP_010889689.1; NC_001318.1.
DR   AlphaFoldDB; O51148; -.
DR   SMR; O51148; -.
DR   STRING; 224326.BB_0122; -.
DR   PRIDE; O51148; -.
DR   EnsemblBacteria; AAC66512; AAC66512; BB_0122.
DR   KEGG; bbu:BB_0122; -.
DR   PATRIC; fig|224326.49.peg.520; -.
DR   HOGENOM; CLU_047155_0_0_12; -.
DR   OMA; DAGMMDC; -.
DR   Proteomes; UP000001807; Chromosome.
DR   GO; GO:0005829; C:cytosol; IDA:CAFA.
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..279
FT                   /note="Elongation factor Ts"
FT                   /id="PRO_0000161085"
FT   REGION          80..83
FT                   /note="Involved in Mg(2+) ion dislocation from EF-Tu"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   279 AA;  31304 MW;  15E8DBB6AC5AE92E CRC64;
     MSIISPQDVK KLREETNAGF GDCKKALSVA GGDFELAKKK LREMGIASAE KRLDRDAKEG
     RVFSYSNNIY AGLLLVSCET DFVALNHNFV NFGNSLIKEL VESGIDSLTT SQELELKNLA
     ATIKENIQVK KIFITKIQSN EFVKIYLHGE QSKIGVLVKL KVNDFSKTED KIFKNFAMDL
     ALHVAAFAPV YLRNDDVCPN YIKEQEEIFT KQLESSGKPE SIIKGIVAGK IKKHLAEISL
     LEQSFVKNDK ITVKEMLEEI SKAISSKVEM VEFKYLRIG