ID   EFG_HELPJ               Reviewed;         692 AA.
AC   Q9ZK24;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 139.
DE   RecName: Full=Elongation factor G;
DE            Short=EF-G;
GN   Name=fusA; OrderedLocusNames=jhp_1118;
OS   Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=85963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J99 / ATCC 700824;
RX   PubMed=9923682; DOI=10.1038/16495;
RA   Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C.,
RA   Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J.,
RA   Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D.,
RA   Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.;
RT   "Genomic sequence comparison of two unrelated isolates of the human gastric
RT   pathogen Helicobacter pylori.";
RL   Nature 397:176-180(1999).
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; AE001439; AAD06689.1; -; Genomic_DNA.
DR   PIR; G71847; G71847.
DR   RefSeq; WP_000101866.1; NZ_CP011330.1.
DR   AlphaFoldDB; Q9ZK24; -.
DR   SMR; Q9ZK24; -.
DR   STRING; 85963.jhp_1118; -.
DR   EnsemblBacteria; AAD06689; AAD06689; jhp_1118.
DR   KEGG; hpj:jhp_1118; -.
DR   PATRIC; fig|85963.30.peg.1459; -.
DR   eggNOG; COG0480; Bacteria.
DR   OMA; AATTCHW; -.
DR   Proteomes; UP000000804; 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   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..692
FT                   /note="Elongation factor G"
FT                   /id="PRO_0000091135"
FT   DOMAIN          8..283
FT                   /note="tr-type G"
FT   BINDING         17..24
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         81..85
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         135..138
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   692 AA;  77127 MW;  A4253CDCF9BD7DF8 CRC64;
     MARKTPLNRI RNIGIAAHID AGKTTTSERI LFYTGVSHKI GEVHDGAATM DWMEQEKERG
     ITITSAATTC FWKDHQINLI DTPGHVDFTI EVERSMRVLD GAVSVFCSVG GVQPQSETVW
     RQANKYGVPR IVFVNKMDRI GANFYNVENQ IKQRLKANPV PINIPIGAED TFIGVIDLVQ
     MKAIVWNNET MGAKYDVEEI PSDLLEKAKQ YREKLVEAVA EQDEALMEKY LGGEELDIEE
     IKKGIKTGCL NMSFVPMLCG SSFKNKGVQT LLDAVIDYLP APTEVVDIKG IDPKTEEEVF
     VKSSDDGEFA GLAFKIMTDP FVGQLTFVRV YRGKLESGSY VYNSTKDKKE RVGRLLKMHS
     NKREDIKEVY AGEICAFVGL KDTLTGDTLC DEKNAVVLER MEFPEPVIHI AVEPKTKADQ
     EKMGVALGKL AEEDPSFRVM TQEETGQTLI GGMGELHLEI IVDRLKREFK VEAEIGQPQV
     AFRETIRSSV SKEHKYAKQS GGRGQYGHVF IKLEPKEPGS GYEFVNEISG GVIPKEYIPA
     VDKGIQEAMQ NGVLAGYPVV DFKVTLYDGS YHDVDSSEMA FKIAGSMAFK EASRAANPVL
     LEPMMKVEVE VPEEYMGDVI GDLNRRRGQI NSMDDRLGLK IVNAFVPLVE MFGYSTDLRS
     ATQGRGTYSM EFDHYGEVPS NIAKEIVEKR KG