ID   EFG_BLOPB               Reviewed;         704 AA.
AC   Q492B1;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 106.
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=BPEN_585;
OS   Blochmannia pennsylvanicus (strain BPEN).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; ant endosymbionts; Candidatus Blochmannia.
OX   NCBI_TaxID=291272;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BPEN;
RX   PubMed=16077009; DOI=10.1101/gr.3771305;
RA   Degnan P.H., Lazarus A.B., Wernegreen J.J.;
RT   "Genome sequence of Blochmannia pennsylvanicus indicates parallel
RT   evolutionary trends among bacterial mutualists of insects.";
RL   Genome Res. 15:1023-1033(2005).
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; CP000016; AAZ41191.1; -; Genomic_DNA.
DR   RefSeq; WP_011283102.1; NC_007292.1.
DR   AlphaFoldDB; Q492B1; -.
DR   SMR; Q492B1; -.
DR   STRING; 291272.BPEN_585; -.
DR   EnsemblBacteria; AAZ41191; AAZ41191; BPEN_585.
DR   KEGG; bpn:BPEN_585; -.
DR   eggNOG; COG0480; Bacteria.
DR   HOGENOM; CLU_002794_4_1_6; -.
DR   OMA; AATTCHW; -.
DR   BioCyc; CBLO291272:BPEN_RS02885-MON; -.
DR   Proteomes; UP000007794; 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.
FT   CHAIN           1..704
FT                   /note="Elongation factor G"
FT                   /id="PRO_0000225194"
FT   DOMAIN          8..291
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         88..92
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
FT   BINDING         142..145
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
SQ   SEQUENCE   704 AA;  78491 MW;  85106A01CB29E9A0 CRC64;
     MARVTPIVRY RNIGISAHID AGKTTTTERI LFYTGVNHKI GEVHTGSATM DWMEQEQERG
     ITITSAATTC FWSGMANQFD SHRINIIDTP GHVDFTIEVE RSMRILDGVV MVYCAVGGVQ
     PQSETVWRQA NKYKVPRIAF INKMDRVGAD YLRVVEQLKT RLFANPVPIQ LAVGSEDKFT
     GIIDLIKMKA IHWNELDQGV TFSYSEIPDN LTDLSGIWRK HLIESAVEVS EELMDKYLSN
     SDQLTEQEIK QALRQRVLSN EIVLVTCGSA FKNKGVQAML DAVVEYLPSP SDVTSITGVL
     KDGSTRVNRH ANDHEPFSAL AFKIATDPFV GNLTFFRVYS GVVSSGDSVL NPIKEKRERF
     GRIVQMHANK REEIKSVHAG DIAAAIGLKD VDTGDTLCAP SSPIILERME FPEPVISVMV
     EAKTKSDQEK MGFALNRLAQ EDPSFRVWID KDSGQTIIAG MGELHLEILV ERMRREFNVE
     ANVGKPQVAY RETIRTSVKQ EGKFIRQSGG RGQFGHVWLR IEPMPAREEG YKFLNEIVGG
     AVPKEYIPAV DKGVREQISN GILAGYPIVD VCVTIFDGSY HEVDSSEIAF KIAGSIAFKE
     GFMKAHPVLL EPIMNVEIET PEDYMGDVIA DLNRRRGIIS GLENSTISGK IICAQVPLSE
     MFGYATGLRS QTQGRASYSM EFLKYNEVPN SIAQIIINSR QIKQ