ID   EFG_STRRA               Reviewed;         341 AA.
AC   P29541;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=Elongation factor G;
DE            Short=EF-G;
DE   Flags: Fragment;
GN   Name=fus;
OS   Streptomyces ramocissimus.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1925;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8012612; DOI=10.1099/00221287-140-4-983;
RA   Vijgenboom E., Woudt L.P., Heinstra P.W.H., Rietveld K., van Haarlem J.,
RA   van Wezel G.P., Shochat S., Bosch L.;
RT   "Three tuf-like genes in the kirromycin producer Streptomyces
RT   ramocissimus.";
RL   Microbiology 140:983-998(1994).
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; X67057; CAA47441.1; -; Genomic_DNA.
DR   PIR; S23907; S23907.
DR   AlphaFoldDB; P29541; -.
DR   SMR; P29541; -.
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; cd16262; EFG_III; 1.
DR   CDD; cd01434; EFG_mtEFG1_IV; 1.
DR   CDD; cd03713; EFG_mtEFG_C; 1.
DR   Gene3D; 3.30.230.10; -; 1.
DR   InterPro; IPR041095; EFG_II.
DR   InterPro; IPR009022; EFG_III.
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; IPR009000; Transl_B-barrel_sf.
DR   InterPro; IPR005517; Transl_elong_EFG/EF2_IV.
DR   Pfam; PF00679; EFG_C; 1.
DR   Pfam; PF14492; EFG_III; 1.
DR   Pfam; PF03764; EFG_IV; 1.
DR   SMART; SM00838; EFG_C; 1.
DR   SMART; SM00889; EFG_IV; 1.
DR   SUPFAM; SSF50447; SSF50447; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   SUPFAM; SSF54980; SSF54980; 2.
PE   3: Inferred from homology;
KW   Cytoplasm; Elongation factor; GTP-binding; Nucleotide-binding;
KW   Protein biosynthesis.
FT   CHAIN           <1..341
FT                   /note="Elongation factor G"
FT                   /id="PRO_0000091236"
FT   NON_TER         1
SQ   SEQUENCE   341 AA;  37322 MW;  DEED0C72A0A62F91 CRC64;
     IYRMHANKRE EIESVGAGDI VAVMGLKQTT TGETLSDEKS PVILESMDFP APVIQVAIEP
     KSKGDQEKLG VAIQRLAEED PSFQVHSDEE TGQTIIGGMG ELHLEVLVDR MRREFKVEAN
     VGKPQVAYRE TIRQAVEKVE YTHKKQTGGT GQFARVIIAI EPIESGDTSY EFVNKVTGGR
     VPKEYIPSVD AGAQEAMQFG ILAGYEMTGV RVTLLDGAYH EVDSSELAFK IAGSQAFKEA
     ARKAKPVLLE PMMAVEVTTP EDYMGEVIGD INSRRGQIQA MEERAGARVV KGLVPLSEMF
     GYVGDLRSKT SGRASYSMQF DSYAEVPRNV AEEIIAKAKG E