ID   EFG_THIDL               Reviewed;         702 AA.
AC   O50565;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Elongation factor G;
DE            Short=EF-G;
GN   Name=fusA; Synonyms=fus;
OS   Thiomonas delicata (Thiomonas cuprina).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Thiomonas.
OX   NCBI_TaxID=364030;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DSM 5495 / NBRC 102094 / Hoe5;
RA   Moreira D., Amils R.;
RT   "The str operon from the chemolithotrophic bacterium Thiobacillus
RT   cuprinus.";
RL   Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
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; U78300; AAB87733.1; -; Genomic_DNA.
DR   AlphaFoldDB; O50565; -.
DR   SMR; O50565; -.
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; -; 2.
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..702
FT                   /note="Elongation factor G"
FT                   /id="PRO_0000091251"
FT   DOMAIN          8..196
FT                   /note="tr-type G"
FT   BINDING         17..24
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         88..92
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         142..145
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   702 AA;  78147 MW;  A9F58AEC60472AF2 CRC64;
     MARKTPIERY RNIGISAHID AGKTTTTERI LFYTGVNHKI GEVHDGAATM DWMEQEQERG
     ITITSAATTC FWKGMDLSLP EHRINIIDTP GHVDFTIEVE RSMRVLDGAC MVYCAVGGVQ
     PQSETVWRQA NKYKVPRLAF VNKMDRTGAN FFKTTSQMEG RLGQPVPVVF PIGAEENFRG
     VIDLLKMKAI IWDEASQGMK FEYQDPAELL SDAEKWRSAM VEAAAEANEE LMNRYLESGE
     LSEEEIKAWL EKRVLNAEQI LAYALRTAFK NKGVQAMLAV IDFLPSPVDI PPCNGTDDNE
     HDTVRRASDD EKFSALAFKL MTDPYVGQLT FIRVYSGILQ SGDTVYNPIK GKKERIGRFV
     QMHANQRDEI KEVRAGDIAP AIGLREITTG ETLCDPESII TLEKMVFPEP VISQAVEPKT
     KADQEKMGIA LQRVAQEDPS FRVKTDEESG QTIISGMGEL HLEILVDRMK REFGVEANVG
     KPQVAYRETI RKTVDDVDGK QAKHSGGRGH YGHVVIAMYR LDRESKPKGY DCMNDIKGGV
     SPGEYIPPVD NGIHEQLNSG VLAGYPVVDV KVTLHFGSYH EVDSSEQAFK MAASIGFKEG
     CRKANPVILE PMMAVEVETP EDYAGNVMGD LSSRRGMVQG MDEIVTGGKV IRAEVPLSEM
     FGYSTTLRSM SQGRATYSME FKHYAEAPRN VAERSSARVQ GK