EFG_BACCE
ID EFG_BACCE Reviewed; 11 AA.
AC P83067;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 17-JUN-2020, entry version 35.
DE RecName: Full=Elongation factor G;
DE Short=EF-G;
DE Flags: Fragment;
GN Name=fusA;
OS Bacillus cereus.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1396;
RN [1]
RP PROTEIN SEQUENCE OF 2-11, AND INDUCTION.
RC STRAIN=DSM 626 / NCIMB 11796 / T;
RX PubMed=11851817; DOI=10.1046/j.1365-2672.2001.01478.x;
RA Browne N., Dowds B.C.A.;
RT "Heat and salt stress in the food pathogen Bacillus cereus.";
RL J. Appl. Microbiol. 91:1085-1094(2001).
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 -!- INDUCTION: By salt stress. {ECO:0000269|PubMed:11851817}.
CC -!- SIMILARITY: Belongs to the GTP-binding elongation factor family. EF-
CC G/EF-2 subfamily. {ECO:0000305}.
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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 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Elongation factor; GTP-binding;
KW Nucleotide-binding; Protein biosynthesis; Stress response.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:11851817"
FT CHAIN 2..>11
FT /note="Elongation factor G"
FT /id="PRO_0000271243"
FT NON_TER 11
SQ SEQUENCE 11 AA; 1333 MW; 72DBFE721325AAEB CRC64;
MAREXSKENT R