ID   EFG_APPPP               Reviewed;         688 AA.
AC   Q9ZEU4;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Elongation factor G;
DE            Short=EF-G;
GN   Name=fusA; Synonyms=fus;
OS   Apple proliferation phytoplasma.
OC   Bacteria; Tenericutes; Mollicutes; Acholeplasmatales; Acholeplasmataceae;
OC   Candidatus Phytoplasma; 16SrX (Apple proliferation group).
OX   NCBI_TaxID=37692;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=AT;
RX   PubMed=9889337; DOI=10.1016/s0378-1119(98)00552-6;
RA   Berg M., Seemueller E.;
RT   "Chromosomal organization and nucleotide sequence of the genes coding for
RT   the elongation factors G and Tu of the Apple proliferation phytoplasma.";
RL   Gene 226:103-109(1999).
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 TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. EF-G/EF-2
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AJ011104; CAA09487.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9ZEU4; -.
DR   SMR; Q9ZEU4; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
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   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_00054_B; EF_G_EF_2_B; 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; IPR004161; EFTu-like_2.
DR   InterPro; IPR031157; G_TR_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   InterPro; IPR004540; Transl_elong_EFG/EF2.
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   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF03144; GTP_EFTU_D2; 1.
DR   PRINTS; PR00315; ELONGATNFCT.
DR   SMART; SM00838; EFG_C; 1.
DR   SMART; SM00889; EFG_IV; 1.
DR   SUPFAM; SSF50447; SSF50447; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   SUPFAM; SSF54980; SSF54980; 2.
DR   TIGRFAMs; TIGR00484; EF-G; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS00301; G_TR_1; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Elongation factor; GTP-binding; Nucleotide-binding;
KW   Protein biosynthesis.
FT   CHAIN           1..688
FT                   /note="Elongation factor G"
FT                   /id="PRO_0000091057"
FT   DOMAIN          8..282
FT                   /note="tr-type G"
FT   BINDING         17..24
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         81..85
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         135..138
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   688 AA;  77227 MW;  3671936865D1815D CRC64;
     MPRKFPLEKT RNIGIMAHID AGKTTTTERI LFHTGKIHKI GETHDGDSQM DWMKQEQERG
     ITITSAATTA FWKEHRINII DTPGHVDFTV EVSRSLRVLD GAVAVIDAKA GVEPQTETVW
     RQATEYKVPR IIFVNKMDKI GASFDYAVKT LYQRLGINAS PIQLPIGSEN EFKGIVDLLE
     MTGVEFLGTS DEKFKTIEIP EYMKEFAQNK RIELIEKWHN YDEELMMDYL NGKEITVEKL
     KNVIRQATLK ADFFPVLCGS AFKNKGVKKI LDAIIDYLPS PMDVSSIVGC NFENKEIIRK
     TSDNEPFTAL AFKVMTDPYV GKLTFFRVYA GTIKTGSYVT NATKQVKERL GRLLQMHANS
     REEIKEVYAG DIVAAVGLKN TTPGDTLTSI NDDIILESMN FPEPVIEIAI EPKTKADQDK
     IGIALSKLSE EHPTFKIYTN RETAQTIIAA MGELHLEIIL DRLKTEFKVE ANVNQPQVAY
     RETLTKISTT EGKFIRQSGG RGQYGHVIIR FEPNSDKGNE FINKIVGGVI PKEYIPAVKK
     GLEESLSNGI LAGFPLIDVK ATLIDGSYHD VDSSEIAFKI AASMALKQTK NEGNLVILEP
     IMEVEIITPN DYIGNVIGDL TSRRGKLENQ DSRENTVIIK ALVPLSEMFG YATILRSNTQ
     GRASFIMQFL KYERAPKNIA EEIIKKRN