ID   EFG_BUCA5               Reviewed;         702 AA.
AC   B8D9V0;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 79.
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=BUAP5A_520;
OS   Buchnera aphidicola subsp. Acyrthosiphon pisum (strain 5A).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=563178;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=5A;
RX   PubMed=19150844; DOI=10.1126/science.1167140;
RA   Moran N.A., McLaughlin H.J., Sorek R.;
RT   "The dynamics and time scale of ongoing genomic erosion in symbiotic
RT   bacteria.";
RL   Science 323:379-382(2009).
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; CP001161; ACL30871.1; -; Genomic_DNA.
DR   RefSeq; WP_009874478.1; NC_011833.1.
DR   AlphaFoldDB; B8D9V0; -.
DR   SMR; B8D9V0; -.
DR   PRIDE; B8D9V0; -.
DR   KEGG; bap:BUAP5A_520; -.
DR   HOGENOM; CLU_002794_4_1_6; -.
DR   OMA; AATTCHW; -.
DR   OrthoDB; 88967at2; -.
DR   Proteomes; UP000006904; 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..702
FT                   /note="Elongation factor G"
FT                   /id="PRO_1000201443"
FT   DOMAIN          8..290
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   702 AA;  78183 MW;  F583FEF269AB1CF9 CRC64;
     MSRTTPISRY RNIGISAHID AGKTTTTERI LFYTGINHKI GEVHDGAATM DWMEQEQERG
     ITITSAATTT FWSGMAKQFK PHRINIIDTP GHVDFTIEVE RSMRVLDGAV MVYCAVGGVQ
     PQSETVWRQA NKYNVPRIAF VNKMDRMGAN FLKVVKQIKI RLGANPVPLQ LAIGAEDTFV
     GVVDLIKMKA VHWKDSDQGV TFVYNDIPPE MIELSKKWNQ NLIESAVESN EDLLEKYLNG
     DRLSESEIKS ALRKRALNNE IVLITCGSAF KNKGVQALLD AIIEFLPAPN DIQDIKGILN
     DVEQTPAIRN SDDKAPFSAL AFKIASDPFV GNLTFFRVYS GVVKSGDTVF NSAKSQRERF
     GRIVQMHANK REEIKEVYAG DIAAAIGLKD VTTGDTLCDL NDPIILERME FPEPVISISV
     EPKTKVDQEK MGLALGRLAK EDPSFRVRTD QESNQTIISG MGELHLEIII DRMKREFSVD
     ANVGKPQVAY RETILNKVED IEGKHIKQSG GRGQYGHVVI ELFPLQPGGE GYLFVNDIKG
     GVIPSEYISA IDKGIQEQLK CGPLAGYPVV DIGVRLYFGS YHDVDSSELA FKLAASAAFK
     KGFKQAKPIL LEPIMKVEVE TPDDYMGDVI GDLNRRRGII EGMKDLSISK IINACVPLSE
     MFGYATDLRS QTQGRASYSM EFLKYIEAPF NISKDIIERR EK