ID   EFG_PLARO               Reviewed;         128 AA.
AC   P72230;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=Elongation factor G;
DE            Short=EF-G;
DE   Flags: Fragment;
GN   Name=fusA; Synonyms=fus;
OS   Planobispora rosea.
OC   Bacteria; Actinobacteria; Streptosporangiales; Streptosporangiaceae;
OC   Planobispora.
OX   NCBI_TaxID=35762;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 53773 / GE2270;
RX   PubMed=8899707; DOI=10.1111/j.1365-2958.1996.tb02654.x;
RA   Sosio M., Amati G., Cappellano C., Sarubbi E., Monti F., Donadio S.;
RT   "An elongation factor Tu (EF-Tu) resistant to the EF-Tu inhibitor GE2270 in
RT   the producing organism Planobispora rosea.";
RL   Mol. Microbiol. 22:43-51(1996).
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}.
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; X98830; CAA67344.1; -; Genomic_DNA.
DR   PIR; S72628; S72628.
DR   AlphaFoldDB; P72230; -.
DR   SMR; P72230; -.
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.
DR   CDD; cd03713; EFG_mtEFG_C; 1.
DR   Gene3D; 3.30.230.10; -; 1.
DR   InterPro; IPR035647; EFG_III/V.
DR   InterPro; IPR035649; EFG_V.
DR   InterPro; IPR000640; EFG_V-like.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR   InterPro; IPR005517; Transl_elong_EFG/EF2_IV.
DR   Pfam; PF00679; EFG_C; 1.
DR   Pfam; PF03764; EFG_IV; 1.
DR   SMART; SM00838; EFG_C; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   SUPFAM; SSF54980; SSF54980; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Elongation factor; GTP-binding; Nucleotide-binding;
KW   Protein biosynthesis.
FT   CHAIN           <1..128
FT                   /note="Elongation factor G"
FT                   /id="PRO_0000091178"
FT   NON_TER         1
SQ   SEQUENCE   128 AA;  14110 MW;  EE0D0A1A9737404B CRC64;
     LQDGAYHEVD SSEMAFKIAG SMAFKEAARK AYAVILEPLM AVEVTTPEDY MGDVIGDLKG
     PRRQIRAMDE RAGARVVQAL VTLLDIFGYV GDLRSKTQGR ASFSMQFDSY AEVPQHIAKK
     IVAKVRAQ