EFTS_BORGP
ID EFTS_BORGP Reviewed; 279 AA.
AC Q662P0;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 25-MAY-2022, entry version 98.
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=BG0123;
OS Borrelia garinii subsp. bavariensis (strain ATCC BAA-2496 / DSM 23469 /
OS PBi) (Borrelia bavariensis).
OC Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX NCBI_TaxID=290434;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-2496 / DSM 23469 / PBi;
RX PubMed=15547252; DOI=10.1093/nar/gkh953;
RA Gloeckner G., Lehmann R., Romualdi A., Pradella S., Schulte-Spechtel U.,
RA Schilhabel M., Wilske B., Suehnel J., Platzer M.;
RT "Comparative analysis of the Borrelia garinii genome.";
RL Nucleic Acids Res. 32:6038-6046(2004).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000013; AAU06981.1; -; Genomic_DNA.
DR RefSeq; WP_011193474.1; NZ_CP028872.1.
DR AlphaFoldDB; Q662P0; -.
DR SMR; Q662P0; -.
DR STRING; 290434.BG0123; -.
DR EnsemblBacteria; AAU06981; AAU06981; BG0123.
DR KEGG; bga:BG0123; -.
DR eggNOG; COG0264; Bacteria.
DR HOGENOM; CLU_047155_0_0_12; -.
DR OMA; DAGMMDC; -.
DR OrthoDB; 1405357at2; -.
DR Proteomes; UP000002276; 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.
FT CHAIN 1..279
FT /note="Elongation factor Ts"
FT /id="PRO_0000161086"
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 279 AA; 31268 MW; D1C644A7FEB0BF2D CRC64;
MSIISPQDVK RLREETNAGF GDCKKALSAA SGDFELAKKK LREMGIASAE KRLDRDAKEG
RVFSYSNNIH AGLLLVSCET DFVALNHNFV NLGNSLIKEL VESGRSFPTA SQELELKNLA
ATIKENIQVK KIFITEIQSN EFVKIYLHGE QSKIGVLVKL KVDDFSKTED KMFQNFAMDL
ALHVAAFAPI YLGNDDVCPN YIKEQEEIFA KQLEFSGKSE SILKGIVAGK IKKHLAEISL
LEQSFVKNDK VTVREMLEEI SKAISSKIEI VEFKYLRIG