ID   EFTS_LACLA              Reviewed;         342 AA.
AC   Q9CDR5;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   27-APR-2001, sequence version 1.
DT   25-MAY-2022, entry version 120.
DE   RecName: Full=Elongation factor Ts;
DE            Short=EF-Ts;
GN   Name=tsf; OrderedLocusNames=LL2152; ORFNames=L0376;
OS   Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=272623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IL1403;
RX   PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA   Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA   Ehrlich S.D., Sorokin A.;
RT   "The complete genome sequence of the lactic acid bacterium Lactococcus
RT   lactis ssp. lactis IL1403.";
RL   Genome Res. 11:731-753(2001).
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; AE005176; AAK06250.1; -; Genomic_DNA.
DR   PIR; H86893; H86893.
DR   RefSeq; NP_268309.1; NC_002662.1.
DR   RefSeq; WP_010906339.1; NC_002662.1.
DR   AlphaFoldDB; Q9CDR5; -.
DR   SMR; Q9CDR5; -.
DR   STRING; 272623.L0376; -.
DR   PaxDb; Q9CDR5; -.
DR   EnsemblBacteria; AAK06250; AAK06250; L0376.
DR   GeneID; 60356350; -.
DR   KEGG; lla:L0376; -.
DR   PATRIC; fig|272623.7.peg.2311; -.
DR   eggNOG; COG0264; Bacteria.
DR   HOGENOM; CLU_047155_0_1_9; -.
DR   OMA; DAGMMDC; -.
DR   Proteomes; UP000002196; Chromosome.
DR   GO; GO:0009986; C:cell surface; IDA:CAFA.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:2001065; F:mannan binding; IDA:CAFA.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.479.20; -; 3.
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..342
FT                   /note="Elongation factor Ts"
FT                   /id="PRO_0000161135"
FT   REGION          79..82
FT                   /note="Involved in Mg(2+) ion dislocation from EF-Tu"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   342 AA;  36670 MW;  3FE6E63FD0692987 CRC64;
     MAVTAAQVKE LREKTGAGIM DAKRALVETD GNMEAAAELL REKGIAKAAK KADRVAAEGL
     TGIAVNGNVA AIVELNSETD FVAKNDQFVA LVKETAELIA SKKPATNEEA LALETASGIT
     LEAELVQATA TIGEKITFRR FAVIEKTDAQ HFGAYQHNGG KIGVVSVVEG ADETLAKQVS
     MHIAAMNPTV LSADELDSEF VKAELAQMNH KIDEDNASRV LVNKPELPHH EFGSKSQLTE
     EVLAAAKASF EEELKAEGKP EKIWDKILPG KMAKFIVDNT KVDQQFALLA QLYIMDDSKT
     VEAFLESKGA KAIAFTRFEV GEGIEKAETD FAAEVEAAKA GL