ID   EFG_AQUAE               Reviewed;         699 AA.
AC   O66428;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 137.
DE   RecName: Full=Elongation factor G;
DE            Short=EF-G;
GN   Name=fusA; OrderedLocusNames=aq_001;
OS   Aquifex aeolicus (strain VF5).
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=224324;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5;
RX   PubMed=9537320; DOI=10.1038/32831;
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL   Nature 392:353-358(1998).
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; AE000657; AAC06402.1; -; Genomic_DNA.
DR   PIR; A70300; A70300.
DR   RefSeq; NP_212986.1; NC_000918.1.
DR   RefSeq; WP_010879924.1; NC_000918.1.
DR   AlphaFoldDB; O66428; -.
DR   SMR; O66428; -.
DR   STRING; 224324.aq_001; -.
DR   EnsemblBacteria; AAC06402; AAC06402; aq_001.
DR   KEGG; aae:aq_001; -.
DR   PATRIC; fig|224324.8.peg.1; -.
DR   eggNOG; COG0480; Bacteria.
DR   HOGENOM; CLU_002794_4_1_0; -.
DR   InParanoid; O66428; -.
DR   OMA; AATTCHW; -.
DR   OrthoDB; 88967at2; -.
DR   Proteomes; UP000000798; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
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   GO; GO:0032790; P:ribosome disassembly; IBA:GO_Central.
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..699
FT                   /note="Elongation factor G"
FT                   /id="PRO_0000091058"
FT   DOMAIN          8..287
FT                   /note="tr-type G"
FT   BINDING         17..24
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         85..89
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         139..142
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   699 AA;  78398 MW;  60805A31F24EF4FB CRC64;
     MAREVPIEKL RNIGIVAHID AGKTTTTERI LYYTGKTYKI GEVHEGAATM DWMPQEKERG
     ITITVATTAC YWTRNGERYQ INIIDTPGHV DFSVEVVRSM KVLDGIVFIF SAVEGVQPQS
     EANWRWADRF QVPRIAFINK MDRLGADFYR VFKEIEEKLT IKPVAIQIPL GAEDQFEGVI
     DLMEMKAIRW LEETLGAKYE VVDIPPEYQE KAQEWREKMI ETIVETDDEL MEKYLEGQEI
     SIDELRKALR KATIERKLVP VLCGSAFKNK GVQPLLDAVI DYLPSPIDLP PVKGTNPKTG
     EEEVRHPSDD EPFCAYAFKV MSDPYAGQLT YIRVFSGTLK AGSYVYNATK DEKQRAGRLL
     LMHANSREEI QQVSAGEICA VVGLDAATGD TLCDEKHPII LEKLEFPDPV ISMAIEPKTK
     KDQEKLSQVL NKFMKEDPTF RATTDPETGQ ILIHGMGELH LEIMVDRMKR EYGIEVNVGK
     PQVAYKETIR KKAIGEGKFI KQTGGRGQYG HAIIEIEPLP RGAGFEFIDD IHGGVIPKEF
     IPSVEKGVKE AMQNGILAGY PVVDVRVRLF DGSYHEVDSS DIAFQVAGSL AFKDAAKKAD
     PVLLEPIMEV EVETPEKYVG DVIGDLNSRR GKIMGMENKG VITVIKAHVP LAEMFGYATT
     LRSLTQGRGT FIMKFSHYDE VPQQIAEKII GERMAGKSS