ID   EFG_AQUPY               Reviewed;         699 AA.
AC   P46211;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Elongation factor G;
DE            Short=EF-G;
GN   Name=fusA; Synonyms=fus;
OS   Aquifex pyrophilus.
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=2714;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DSM 6858 / JCM 9492 / Kol5A;
RX   PubMed=8587125; DOI=10.1007/bf00173160;
RA   Bocchetta M., Ceccarelli E., Creti R., Sanangelantoni A.M., Tiboni O.,
RA   Cammarano P.;
RT   "Arrangement and nucleotide sequence of the gene (fus) encoding elongation
RT   factor G (EF-G) from the hyperthermophilic bacterium Aquifex pyrophilus:
RT   phylogenetic depth of hyperthermophilic bacteria inferred from analysis of
RT   the EF-G/fus sequences.";
RL   J. Mol. Evol. 41:803-812(1995).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA52336.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; X74277; CAA52336.1; ALT_FRAME; Genomic_DNA.
DR   PIR; S38928; S38928.
DR   AlphaFoldDB; P46211; -.
DR   SMR; P46211; -.
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_0000091059"
FT   DOMAIN          8..286
FT                   /note="tr-type G"
FT   BINDING         17..24
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         84..88
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         138..141
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   699 AA;  78158 MW;  41E889EEC1E26940 CRC64;
     MAREVPIEKL RNIGIVAHID AGKTTTTERI PTTGKDIQIG EVTEGAATMD WMPQEKERGI
     TITAATTACY WTRNGERYQI NIIDTPGHVD FSVEVVRSMK VLDGIVFIFS AVEGVQPQSE
     ANWRWADRFK VPRIAFINKM DRLGADFYRV FKEIEEKLTI KPVAIQIPLG AEDQFEGVID
     LMEMKAIRWL EVTLGAKYEV IDIPPGYQEK AQEWREKMIE TIVETDDELM EKYLEAQEIT
     LEELRKALRK ATINRQLVPV LCGSAFKNKG VQPLLDAVIV TYPLPIDLPP VKGTNPNTGE
     EEERRPLDEE PFCAYAFKVM ADPYAGQLTY IRVFSGTLKA GSYVYNATRD EKQRAGRLLL
     MHANSREEIQ QVSAGEICAV VGLDAATGDT LCDEKHPIIL EKLEFPDPVI SMAIEPKTKK
     DQEKLSQVLN LSSLKEDPTF RATTDPETGQ ILIHGMGELH LEIMVDRMRR EYGIEVNVGK
     PQVAYKETIR KKAIGEGKFI KQTGGRGQYG HAIIEIEPLP RGKGFEFIDD IHGGVIPKEF
     IPSVEKGVKE AMQNGILAGY PVVDVRVRLF DGSYHEVDSS DIAFQVAGSL AFKDAAKKAD
     PVLLEPIMEV EVETPEDYVG DVIGDLNSRR GTIMGMENKG NITVVKAHVP LAEMFGYATT
     LRSLTQGRGT FIMRFSHYDE VPQHIAEKII GERMAGKSS