ID   EFG_CARRP               Reviewed;         681 AA.
AC   Q05FI2;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 95.
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=CRP_158;
OS   Carsonella ruddii (strain PV).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Zymobacter group; Candidatus Carsonella.
OX   NCBI_TaxID=387662;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PV;
RX   PubMed=17038615; DOI=10.1126/science.1134196;
RA   Nakabachi A., Yamashita A., Toh H., Ishikawa H., Dunbar H.E., Moran N.A.,
RA   Hattori M.;
RT   "The 160-kilobase genome of the bacterial endosymbiont Carsonella.";
RL   Science 314:267-267(2006).
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; AP009180; BAF35189.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q05FI2; -.
DR   SMR; Q05FI2; -.
DR   STRING; 387662.CRP_158; -.
DR   EnsemblBacteria; BAF35189; BAF35189; CRP_158.
DR   KEGG; crp:CRP_158; -.
DR   HOGENOM; CLU_002794_4_1_6; -.
DR   OMA; AATTCHW; -.
DR   Proteomes; UP000000777; 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..681
FT                   /note="Elongation factor G"
FT                   /id="PRO_0000335836"
FT   DOMAIN          5..279
FT                   /note="tr-type G"
FT   BINDING         14..21
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
FT   BINDING         82..86
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
FT   BINDING         136..139
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
SQ   SEQUENCE   681 AA;  77205 MW;  10E3D5E8277F8533 CRC64;
     MNDIKNIRNI GIIAHVDAGK TTTTERILFF SGFSHKIGEV HTGNTITDWM KQEQERGITI
     TSASVTFFWK TNFYNSSINL IDTPGHVDFT IEVERSLRVL DGAVILICAS SGIQPQTETV
     WNQSEKFNIP KILFVNKLDR IGAKYLSIIE NIKKKFFCNI LIINLNIGIE NSFSGIIDLI
     NMKELIWNNS QLEIRNITNK NFDISNKYRN ILLETLSEYD DIFLEKYINS NFSIKDIIES
     IRKLVILNKI IPIACGSSLK NKGIEFLLDS IVNFLPSPID IGIKNVSNIN YSVNIKSKFL
     ALLFKVFNDP YLGLLSFIRI YSGKIEPGQI IFNNSKNIKE KIFRIIRMFA NSKKDLNIAS
     AGDIVVLIGL KNSFTGDTLS FDNEKVLLEK INIPLPVISV SVEPIVKNDY EKLLNLINKF
     CKEDPSLLFK INENTGELIL SGMGELHLEI IIDRINNEFN IKTKTSKPQV SYKESIKKTI
     IQEGKYIKQT GGRGQYGHVV LKIEPILIEK DDFIFKIEVV GGVIPKEYFL SIEKGILEQI
     KCGVVLGYPV TKIKITLING SFHPVDSSEY AFKNAASIAL KEALKKANSF LLEPIMKVEI
     ISPKEYLGIV ISDISKKRGN IISVVDNNNN LKIINSLIPL RELFGYSTDL RSNTKGRANY
     NMEFHNYSET PNYILEKIKK K