EFTS_LIMRD
ID EFTS_LIMRD Reviewed; 291 AA.
AC A5VJC6;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 81.
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=Lreu_0685;
OS Limosilactobacillus reuteri (strain DSM 20016) (Lactobacillus reuteri).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Limosilactobacillus.
OX NCBI_TaxID=557436;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20016;
RX PubMed=21379339; DOI=10.1371/journal.pgen.1001314;
RA Frese S.A., Benson A.K., Tannock G.W., Loach D.M., Kim J., Zhang M.,
RA Oh P.L., Heng N.C., Patil P.B., Juge N., Mackenzie D.A., Pearson B.M.,
RA Lapidus A., Dalin E., Tice H., Goltsman E., Land M., Hauser L., Ivanova N.,
RA Kyrpides N.C., Walter J.;
RT "The evolution of host specialization in the vertebrate gut symbiont
RT Lactobacillus reuteri.";
RL PLoS Genet. 7:E1001314-E1001314(2011).
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; CP000705; ABQ82950.1; -; Genomic_DNA.
DR RefSeq; WP_003666861.1; NZ_AZDD01000002.1.
DR AlphaFoldDB; A5VJC6; -.
DR SMR; A5VJC6; -.
DR STRING; 557436.Lreu_0685; -.
DR PRIDE; A5VJC6; -.
DR EnsemblBacteria; ABQ82950; ABQ82950; Lreu_0685.
DR GeneID; 66470826; -.
DR KEGG; lre:Lreu_0685; -.
DR PATRIC; fig|557436.17.peg.758; -.
DR eggNOG; COG0264; Bacteria.
DR HOGENOM; CLU_047155_0_2_9; -.
DR OMA; DAGMMDC; -.
DR Proteomes; UP000001991; 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..291
FT /note="Elongation factor Ts"
FT /id="PRO_1000057355"
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 291 AA; 31962 MW; 56D39E7547E60577 CRC64;
MAEIKAAQVM QLRKKSGAGI MDAKKALVAS DGDMDKAMDY LREKGIAKAA KKSDRVAAEG
LADIAVNGNT AAIVELNSET DFVAASEPFK DLLKKVTKLI SENKPANVEE ALEIKTENGT
LNDDIISTTQ KTGEKVSLRR FTVVEKDDGD SFGAYLHQGG QIAALVVLEG ADDATAKDVA
MHVAAINPEF MTRDDVSQER LDHERAIFKE ETLNEGKPEK IVDKIVEGRL NKFLSQICLA
DQDFVKDSDQ TVEQYVSSKN GKLKSFIRYE VGEGIEKKQD DFAQEVKDQM N