EFTS_CAUSK
ID EFTS_CAUSK Reviewed; 312 AA.
AC B0SZ20;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 70.
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=Caul_2804;
OS Caulobacter sp. (strain K31).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter; unclassified Caulobacter.
OX NCBI_TaxID=366602;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K31;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Bruce D., Goodwin L., Thompson L.S., Brettin T.,
RA Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Kim E., Stephens C., Richardson P.;
RT "Complete sequence of chromosome of Caulobacter sp. K31.";
RL Submitted (JAN-2008) 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; CP000927; ABZ71931.1; -; Genomic_DNA.
DR RefSeq; WP_012286833.1; NC_010338.1.
DR AlphaFoldDB; B0SZ20; -.
DR SMR; B0SZ20; -.
DR STRING; 366602.Caul_2804; -.
DR EnsemblBacteria; ABZ71931; ABZ71931; Caul_2804.
DR KEGG; cak:Caul_2804; -.
DR eggNOG; COG0264; Bacteria.
DR HOGENOM; CLU_047155_2_0_5; -.
DR OMA; DAGMMDC; -.
DR OrthoDB; 1405357at2; -.
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.
FT CHAIN 1..312
FT /note="Elongation factor Ts"
FT /id="PRO_1000074856"
FT REGION 84..87
FT /note="Involved in Mg(2+) ion dislocation from EF-Tu"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00050"
SQ SEQUENCE 312 AA; 32870 MW; 9A3DA1CD61204D87 CRC64;
MAEVTAALVK ELREKSGVGM MDCKKALVEN NGDIDASIDW LRAKGLSKAA KKADRVAAEG
LVGIVVRAEG AGMIAAAVEV NAETDFLSRN ELFQTAVRKI ARAGLDNEGV EAISAAKTPD
GEVVSDLLTH LIATIGENMV LRRSARFAVA HGAVASYIHN ATAPDLGRIG VLVAIEGAGD
QTKILELGRK IAMHVAATAP LSLSPDDLDQ AAIEKERQIF TEQALESGKP PAVVEKMVEG
RIRKFLEEVV LLKQAFVMNP DQTVEQLVAE AGKELGSPLT VKGFVRLALG EGVEKGPEGD
FAAEVAAMTG QA