EFTS_RUEST
ID EFTS_RUEST Reviewed; 291 AA.
AC Q1GHC2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2006, sequence version 1.
DT 25-MAY-2022, entry version 103.
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=TM1040_1211;
OS Ruegeria sp. (strain TM1040) (Silicibacter sp.).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Ruegeria; unclassified Ruegeria.
OX NCBI_TaxID=292414;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TM1040;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Brettin T., Bruce D., Han C., Tapia R., Goodwin L., Thompson L.S.,
RA Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA Belas R., Moran M.A., Buchan A., Gonzalez J.M., Schell M.A., Sun F.,
RA Richardson P.;
RT "Complete sequence of chromosome of Silicibacter sp. TM1040.";
RL Submitted (MAY-2006) 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; CP000377; ABF63944.1; -; Genomic_DNA.
DR RefSeq; WP_011538550.1; NC_008044.1.
DR AlphaFoldDB; Q1GHC2; -.
DR SMR; Q1GHC2; -.
DR STRING; 292414.TM1040_1211; -.
DR EnsemblBacteria; ABF63944; ABF63944; TM1040_1211.
DR KEGG; sit:TM1040_1211; -.
DR eggNOG; COG0264; Bacteria.
DR HOGENOM; CLU_047155_2_0_5; -.
DR OMA; DAGMMDC; -.
DR OrthoDB; 1405357at2; -.
DR Proteomes; UP000000636; 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_1000006184"
FT REGION 79..82
FT /note="Involved in Mg(2+) ion dislocation from EF-Tu"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00050"
SQ SEQUENCE 291 AA; 30328 MW; 50CF2471D7F2054C CRC64;
MAITAAMVKE LRESTGAGMM DAKKALVEND GDMEAAVDWL RTKGLAKAAK KSGRTAAEGL
VAVVVDGGKG VAVEVNSETD FVAKNGEFQT MVAGIAKAAL SVNTVEELAE ADLGGKTVAT
TLTDKIATIG ENMTLRRMAK LEGETVVSYV HNAATDGMGK IGVLVALSGG DEAIGKQVAM
HIAAVNPAAL SEADLDPAIV EKERQVQIDI ARESGKPEQV IEKMIEGRMK KFVAESTLLN
QQFVVNPDLT VEAAAKEAGA TVTGFIRVEV GEGIEVEKED FAAEVAKAAQ G