EFTS_DELAS
ID EFTS_DELAS Reviewed; 298 AA.
AC A9BMN1;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 76.
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=Daci_4947;
OS Delftia acidovorans (strain DSM 14801 / SPH-1).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Delftia.
OX NCBI_TaxID=398578;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14801 / SPH-1;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Lowry S., Clum A., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Schleheck D., Richardson P.;
RT "Complete sequence of Delftia acidovorans DSM 14801 / SPH-1.";
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000884; ABX37576.1; -; Genomic_DNA.
DR RefSeq; WP_012206746.1; NC_010002.1.
DR AlphaFoldDB; A9BMN1; -.
DR SMR; A9BMN1; -.
DR STRING; 398578.Daci_4947; -.
DR PRIDE; A9BMN1; -.
DR EnsemblBacteria; ABX37576; ABX37576; Daci_4947.
DR KEGG; dac:Daci_4947; -.
DR eggNOG; COG0264; Bacteria.
DR HOGENOM; CLU_047155_0_2_4; -.
DR OMA; DAGMMDC; -.
DR Proteomes; UP000000784; 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; PS01127; EF_TS_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Elongation factor; Protein biosynthesis; Reference proteome.
FT CHAIN 1..298
FT /note="Elongation factor Ts"
FT /id="PRO_1000116724"
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 298 AA; 31105 MW; 98D7BDD0710751CF CRC64;
MAAITASMVA ELRAKTDAPM MECKKALTEA EGDLVKAEEL LRVKLGTKAG KAASRVTAEG
VIAAFINGNQ GAMIEVNSET DFVSKNDSFI AMANAAAKLV AEQNPADVAA LSALAYEQDG
FGPTLEDVRK GLIGKIGENM SFRRFKRFDG TSLASYLHGS RIGVVVEFDG DATAAKDVAM
HVAAMKPVSV TSADVPAELI EKERTVAAAK AAESGKPAEI VAKMVEGSVQ KYLKEVSLAD
QVFVKAADGK QTVAQMLKAA NTNVKGFTLY VVGEGIEKKV DDFAAEVAAQ VAAAKAGA