EFG_HELPY
ID EFG_HELPY Reviewed; 692 AA.
AC P56002;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Elongation factor G;
DE Short=EF-G;
GN Name=fusA; OrderedLocusNames=HP_1195;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
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; AE000511; AAD08239.1; -; Genomic_DNA.
DR PIR; C64669; C64669.
DR RefSeq; NP_207986.1; NC_000915.1.
DR RefSeq; WP_000101814.1; NC_018939.1.
DR AlphaFoldDB; P56002; -.
DR SMR; P56002; -.
DR DIP; DIP-3214N; -.
DR IntAct; P56002; 2.
DR MINT; P56002; -.
DR STRING; 85962.C694_06180; -.
DR PaxDb; P56002; -.
DR EnsemblBacteria; AAD08239; AAD08239; HP_1195.
DR KEGG; hpy:HP_1195; -.
DR PATRIC; fig|85962.47.peg.1284; -.
DR eggNOG; COG0480; Bacteria.
DR OMA; AATTCHW; -.
DR PhylomeDB; P56002; -.
DR Proteomes; UP000000429; 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 INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..692
FT /note="Elongation factor G"
FT /id="PRO_0000091134"
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; 77021 MW; 810011C34378E899 CRC64;
MARKTPLNRI RNIGIAAHID AGKTTTSERI LFYTGVSHKI GEVHDGAATM DWMEQEKERG
ITITSAATTC FWKDHQINLI DTPGHVDFTI EVERSMRVLD GAVSVFCSVG GVQPQSETVW
RQANKYGVPR IVFVNKMDRI GANFYNVENQ IKLRLKANPV PINIPIGAED TFIGVIDLVQ
MKAIVWNNET MGAKYDVEEI PSDLLEKAKE YREKLVEAVA EQDEALMEKY LGGEELSIEE
IKKGIKAGCL NMSLVPMLCG 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
