EFTS_GRABC
ID EFTS_GRABC Reviewed; 304 AA.
AC Q0BSM6;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 25-MAY-2022, entry version 89.
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};
GN OrderedLocusNames=GbCGDNIH1_1278;
OS Granulibacter bethesdensis (strain ATCC BAA-1260 / CGDNIH1).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Granulibacter.
OX NCBI_TaxID=391165;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1260 / CGDNIH1;
RX PubMed=17827295; DOI=10.1128/jb.00793-07;
RA Greenberg D.E., Porcella S.F., Zelazny A.M., Virtaneva K., Sturdevant D.E.,
RA Kupko J.J. III, Barbian K.D., Babar A., Dorward D.W., Holland S.M.;
RT "Genome sequence analysis of the emerging human pathogenic acetic acid
RT bacterium Granulibacter bethesdensis.";
RL J. Bacteriol. 189:8727-8736(2007).
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; CP000394; ABI62176.1; -; Genomic_DNA.
DR RefSeq; WP_011631985.1; NC_008343.2.
DR AlphaFoldDB; Q0BSM6; -.
DR SMR; Q0BSM6; -.
DR STRING; 391165.GbCGDNIH1_1278; -.
DR EnsemblBacteria; ABI62176; ABI62176; GbCGDNIH1_1278.
DR GeneID; 56915711; -.
DR KEGG; gbe:GbCGDNIH1_1278; -.
DR eggNOG; COG0264; Bacteria.
DR HOGENOM; CLU_047155_2_0_5; -.
DR OMA; DAGMMDC; -.
DR Proteomes; UP000001963; 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..304
FT /note="Elongation factor Ts"
FT /id="PRO_1000006100"
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 304 AA; 32056 MW; 2F08F0A52E323005 CRC64;
MAEITAALVK ELRETTGAGM MDCKKALSET NGDLEAAIDW LRKKGLSAAA KKSGRVAAEG
LVGVASAPQT AAMVEVNAET DFVARNELFQ AFVTETARVA LTVGEDVEAI KAAPYPGTER
TVAEQLTHLV ATIGENMNIR RARVLSVPQG VVASYIHSPV KPGLGKIGVL VAVESASEIS
ALETLGRQVG MQVAAANPHS LDTDNVDPAA LEREKAVLTE QARASGKPEA IIEKMVEGRI
RKYYEEVVLL EQVWVHDGES RVKAIVKNAG AKLTGFARFQ LGEGVEKGPE SDFAAEVAAA
AGLA