ID   EFG_PHYMT               Reviewed;         688 AA.
AC   B3QZH4;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Elongation factor G {ECO:0000255|HAMAP-Rule:MF_00054};
DE            Short=EF-G {ECO:0000255|HAMAP-Rule:MF_00054};
GN   Name=fusA {ECO:0000255|HAMAP-Rule:MF_00054}; OrderedLocusNames=ATP_00394;
OS   Phytoplasma mali (strain AT).
OC   Bacteria; Tenericutes; Mollicutes; Acholeplasmatales; Acholeplasmataceae;
OC   Candidatus Phytoplasma; 16SrX (Apple proliferation group).
OX   NCBI_TaxID=482235;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AT;
RX   PubMed=18582369; DOI=10.1186/1471-2164-9-306;
RA   Kube M., Schneider B., Kuhl H., Dandekar T., Heitmann K., Migdoll A.M.,
RA   Reinhardt R., Seemueller E.;
RT   "The linear chromosome of the plant-pathogenic mycoplasma 'Candidatus
RT   Phytoplasma mali'.";
RL   BMC Genomics 9:306-306(2008).
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. {ECO:0000255|HAMAP-
CC       Rule:MF_00054}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00054}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. EF-G/EF-2
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_00054}.
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DR   EMBL; CU469464; CAP18581.1; -; Genomic_DNA.
DR   AlphaFoldDB; B3QZH4; -.
DR   SMR; B3QZH4; -.
DR   STRING; 37692.ATP_00394; -.
DR   EnsemblBacteria; CAP18581; CAP18581; ATP_00394.
DR   KEGG; pml:ATP_00394; -.
DR   eggNOG; COG0480; Bacteria.
DR   HOGENOM; CLU_002794_4_1_14; -.
DR   OMA; AATTCHW; -.
DR   Proteomes; UP000002020; Chromosome.
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; Reference proteome.
FT   CHAIN           1..688
FT                   /note="Elongation factor G"
FT                   /id="PRO_1000201481"
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:0000255|HAMAP-Rule:MF_00054"
FT   BINDING         81..85
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
FT   BINDING         135..138
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
SQ   SEQUENCE   688 AA;  77026 MW;  43C38EC1DBFA4CD3 CRC64;
     MPRKFPLEKT RNIGIMAHID AGKTTTTERI LFHTGKIHKI GETHDGDSQM DWMKQEQERG
     ITITSAATTA FWKEHRINII DTPGHVDFTV EVSRSLRVLD GAVAVIDAKA GVEPQTETVW
     RQATEYKVPR IIFVNKMDKI GASFDYAVKT LYQRLGINAS PIQLPIGSEN EFKGIVDLLE
     MTGVEFLGTS DEKFKTIEIP EYMKELAQNK RIELIEKMAN YDEELMMDYL NGKEITVEKL
     KNVIRQATLK ADFFPVLCGS AFKNKGVKKI LDAIIDYLPS PMDVSSIVGC NFENKEIIRK
     TSDNEPFTAL AFKVMTDPYV GKLTFFRVYA GTIKTGSYVT NATKQVKERL GRLLQMHANS
     REEIKEVYAG DIVAAVGLKN TTTGDTLTSI NDDIILESMN FPEPVIEIAI EPKTKADQDK
     IGIALSKLSE EDPTFKIYTN RETGQTIIAG MGELHLEIIL DRLKTEFKVE ANVNQPQVAY
     RETLTKISTT EGKFIRQSGG RGQYGHVIIR FEPNSDKGNE FINKIVGGVI PKEYIPAVKK
     GLEESLSNGI LAGFPLIDVK ATLIDGSYHD VDSSEIAFKI AASMALKQTK NEGNLVILEP
     IMEVEIITPN DYIGNVIGDL TSRRGKLENQ DSRENTVIIK ALVPLSEMFG YATILRSNTQ
     GRASFIMQFL KYERAPKNIA EEIIKKRN