EFG_THEAQ
ID EFG_THEAQ Reviewed; 17 AA.
AC Q01697;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 25-MAY-2022, entry version 61.
DE RecName: Full=Elongation factor G;
DE Short=EF-G;
DE Flags: Fragment;
GN Name=fusA; Synonyms=fus;
OS Thermus aquaticus.
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=271;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=EP 00276;
RX PubMed=1499561; DOI=10.1111/j.1432-1033.1992.tb17115.x;
RA Voss R.H., Hartmann R.K., Lippmann C., Alexander C., Jahn O., Erdmann V.;
RT "Sequence of the tufA gene encoding elongation factor EF-Tu from Thermus
RT aquaticus and overproduction of the protein in Escherichia coli.";
RL Eur. J. Biochem. 207:839-846(1992).
CC -!- FUNCTION: Catalyzes the GTP-dependent ribosomal translocation step
CC during translation elongation. During this step, the ribosome changes
CC from the pre-translocational (PRE) to the post-translocational (POST)
CC state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound
CC deacylated tRNA move to the P and E sites, respectively. Catalyzes the
CC coordinated movement of the two tRNA molecules, the mRNA and
CC conformational changes in the ribosome (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the GTP-binding elongation factor family. EF-
CC G/EF-2 subfamily. {ECO:0000305}.
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DR EMBL; X66322; CAA46997.1; -; Genomic_DNA.
DR AlphaFoldDB; Q01697; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
PE 3: Inferred from homology;
KW Cytoplasm; Elongation factor; GTP-binding; Nucleotide-binding;
KW Protein biosynthesis.
FT CHAIN <1..17
FT /note="Elongation factor G"
FT /id="PRO_0000091245"
FT NON_TER 1
SQ SEQUENCE 17 AA; 2094 MW; EA46E1EF05F86E1D CRC64;
HYQEVPRQIQ EKLIKGQ