ID   EFG_RICHE               Reviewed;         699 AA.
AC   Q8KTB4;
DT   22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 85.
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};
OS   Rickettsia helvetica.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=35789;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=12140235; DOI=10.1093/oxfordjournals.molbev.a004184;
RA   Amiri H., Alsmark C.M., Andersson S.G.E.;
RT   "Proliferation and deterioration of Rickettsia palindromic elements.";
RL   Mol. Biol. Evol. 19:1234-1243(2002).
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; AF502175; AAM90923.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8KTB4; -.
DR   SMR; Q8KTB4; -.
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..699
FT                   /note="Elongation factor G"
FT                   /id="PRO_0000091198"
FT   DOMAIN          8..283
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   699 AA;  77682 MW;  3FF103D678219E06 CRC64;
     MSKINKLEHI RNIGICAHID AGKTTTTERI LYYTGKSHKI GEVHEGGATM DWMEQEQERG
     ITITSAATTC RWQDKIINII DTPGHVDFTI EVERSLRVLD GAVAVFDGVA GVEPQSETVW
     RQADKYNVPR MCFVNKMDRM GADFYRCVEM IKDRLGAKPL VIQLPVGIEE NFKGIIDLVK
     MKAVIWKDES LGAKYFEEHI PADMKDKAEE YRAKLLDMVV ELDDHVMEKY LSGEEVTEEE
     IKILIRNGTI SAAFYPVLCG SAFKNKGVQP LLDAVVDFLP SPIDIGIVKG MEVNTGEEKD
     FPISITEPFS ALAFKIMNDP FVGSLTFIRI YSGKITSGAS VINTVKNKRE KIGRMLLMHA
     NNREDIKEAS AGDIVALAGL KDTSTGDTLS DIDTQVVLER MEFPEPVIEL AVEPKSTADQ
     EKMGLALSRL AAEDPSFRVS TDHETGQTVI KGMGELHLEI IIDRMRREFK VEANIGVPQV
     AYRETITKAC EIDYTHKKQS GGAGQFARVK IIFEPLKEVK DLKDEDKNKT FVFESKIVGG
     AVPKEYIPGV EKGLNNIRET GVIAGYPMID FKATLVDGAF HDVDSSVLAF EIAAKAAFRE
     GMPKGNPKLL EPIMKVEVIT PDEYMGDIIG DLNSRRGQIQ SMDPRGNAQV VTANVPLAEM
     FGYVNMLRSL SQGRAQFSMI FSHYDQVPSQ VADIIKAKK