ID   EFTS_LACAC              Reviewed;         341 AA.
AC   Q5FJM4;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 89.
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=LBA1269;
OS   Lactobacillus acidophilus (strain ATCC 700396 / NCK56 / N2 / NCFM).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=272621;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700396 / NCK56 / N2 / NCFM;
RX   PubMed=15671160; DOI=10.1073/pnas.0409188102;
RA   Altermann E., Russell W.M., Azcarate-Peril M.A., Barrangou R., Buck B.L.,
RA   McAuliffe O., Souther N., Dobson A., Duong T., Callanan M., Lick S.,
RA   Hamrick A., Cano R., Klaenhammer T.R.;
RT   "Complete genome sequence of the probiotic lactic acid bacterium
RT   Lactobacillus acidophilus NCFM.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:3906-3912(2005).
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; CP000033; AAV43100.1; -; Genomic_DNA.
DR   RefSeq; WP_003547835.1; NC_006814.3.
DR   RefSeq; YP_194131.1; NC_006814.3.
DR   AlphaFoldDB; Q5FJM4; -.
DR   SMR; Q5FJM4; -.
DR   STRING; 272621.LBA1269; -.
DR   PRIDE; Q5FJM4; -.
DR   EnsemblBacteria; AAV43100; AAV43100; LBA1269.
DR   GeneID; 56942858; -.
DR   KEGG; lac:LBA1269; -.
DR   PATRIC; fig|272621.13.peg.1202; -.
DR   eggNOG; COG0264; Bacteria.
DR   HOGENOM; CLU_047155_0_1_9; -.
DR   OMA; DAGMMDC; -.
DR   BioCyc; LACI272621:G1G49-1250-MON; -.
DR   Proteomes; UP000006381; 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; 2.
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..341
FT                   /note="Elongation factor Ts"
FT                   /id="PRO_0000241489"
FT   REGION          80..83
FT                   /note="Involved in Mg(2+) ion dislocation from EF-Tu"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00050"
SQ   SEQUENCE   341 AA;  37872 MW;  B4D136EB99E82537 CRC64;
     MAQITAKMVK ELRERTGAGV MDAKKALVEV DGDMDKAVEF LREKGMAKAA KKADRVAAEG
     LTGVYVADNV AAVTEINSET DFVSQNDKFV KLVKDVTKTI AEGKPANIEE ADELKMDDGS
     TLDQAFVNAT ATIGEKIVLR RFALEEKTDD QEFGAYQHNG GQIGVITVLE GADAATAKHL
     AMHIAAMNPK VISPDELDDE FITEQLALMN HKIDQDNESR ELVHKKPLPH LVYGSEKQLT
     DDVLAKAKED IKAELKEEGK PEKIWDRIIP GKMQRFIDDN TQVDKQFAVL SQDYIMDDSK
     TVGEFLKEKG AKLVAFQRFE VGEGIEKKQE DFAAEVREQM K