EFTS_LACDA
ID EFTS_LACDA Reviewed; 342 AA.
AC Q1G9N7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2006, sequence version 1.
DT 03-AUG-2022, entry version 91.
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=Ldb1344;
OS Lactobacillus delbrueckii subsp. bulgaricus (strain ATCC 11842 / DSM 20081
OS / BCRC 10696 / JCM 1002 / NBRC 13953 / NCIMB 11778 / NCTC 12712 / WDCM
OS 00102 / Lb 14).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=390333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11842 / DSM 20081 / BCRC 10696 / JCM 1002 / NBRC 13953 / NCIMB
RC 11778 / NCTC 12712 / WDCM 00102 / Lb 14;
RX PubMed=16754859; DOI=10.1073/pnas.0603024103;
RA van de Guchte M., Penaud S., Grimaldi C., Barbe V., Bryson K., Nicolas P.,
RA Robert C., Oztas S., Mangenot S., Couloux A., Loux V., Dervyn R., Bossy R.,
RA Bolotin A., Batto J.-M., Walunas T., Gibrat J.-F., Bessieres P.,
RA Weissenbach J., Ehrlich S.D., Maguin E.;
RT "The complete genome sequence of Lactobacillus bulgaricus reveals extensive
RT and ongoing reductive evolution.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:9274-9279(2006).
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; CR954253; CAI98145.1; -; Genomic_DNA.
DR RefSeq; WP_004560782.1; NZ_JQAV01000006.1.
DR AlphaFoldDB; Q1G9N7; -.
DR SMR; Q1G9N7; -.
DR STRING; 390333.Ldb1344; -.
DR EnsemblBacteria; CAI98145; CAI98145; Ldb1344.
DR GeneID; 66400209; -.
DR KEGG; ldb:Ldb1344; -.
DR PATRIC; fig|390333.13.peg.1711; -.
DR eggNOG; COG0264; Bacteria.
DR HOGENOM; CLU_047155_0_1_9; -.
DR OMA; DAGMMDC; -.
DR BioCyc; LDEL390333:LDB_RS05755-MON; -.
DR Proteomes; UP000001259; 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; 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_1000006112"
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 342 AA; 37427 MW; 725C0F953DAF33B7 CRC64;
MANITAKQVK ELRETTGAGV MDAKKALVEA EGDMQRAIEI IHEKGEAKAA KKANRIAAEG
LTGVYVDGNV AAIVEVNAET DFVAQNEQFK TLVNETAETI AKGKPANNEE ALALTMPSGE
SLEEAYVNAT ATIGEKISFR RFAVLEKTDD QHFGAYQHNG GHIGVLTVVE GGDEALAKHI
AMHIAAMSPK VLSYKELDPA FVREELAQLN HKIDQDNESR AMVNKPALPH LKYGSKAQLT
DEVIAQAEED IKAELKAEGK PEKIWDKIIP GKMARFMLDN TKVDQENTLL AQLYVMDDSK
TVEQYLESVN ASVVSFVRFE VGEGIEKKQE DFAAEVAAQM KN