ID   EFG_PASMU               Reviewed;         700 AA.
AC   P57938;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   27-APR-2001, sequence version 1.
DT   03-AUG-2022, entry version 137.
DE   RecName: Full=Elongation factor G;
DE            Short=EF-G;
GN   Name=fusA; OrderedLocusNames=PM1356;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
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; AE004439; AAK03440.1; -; Genomic_DNA.
DR   RefSeq; WP_005717860.1; NC_002663.1.
DR   AlphaFoldDB; P57938; -.
DR   SMR; P57938; -.
DR   STRING; 747.DR93_607; -.
DR   PRIDE; P57938; -.
DR   EnsemblBacteria; AAK03440; AAK03440; PM1356.
DR   GeneID; 62225313; -.
DR   KEGG; pmu:PM1356; -.
DR   HOGENOM; CLU_002794_4_1_6; -.
DR   OMA; AATTCHW; -.
DR   Proteomes; UP000000809; 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; Reference proteome.
FT   CHAIN           1..700
FT                   /note="Elongation factor G"
FT                   /id="PRO_0000091174"
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:0000250"
FT   BINDING         88..92
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         142..145
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   700 AA;  77186 MW;  6CC161F7F9FA9C72 CRC64;
     MARTTPIERY RNIGISAHID AGKTTTSERI LFYTGVSHKL GEVHDGAATM DWMEQEQERG
     ITITSAATTA FWSGMSKQYP QHRINVIDTP GHVDFTIEVE RSMRVLDGAV MVYCAVGGVQ
     PQSETVWRQA NKYQVPRVAF VNKMDRTGAN FLRVVEQIKT RLGGNSVPLQ LPIGSEDNFK
     GVVDLVKMKA INWNEADQGM TFTYEEIPAD MVDACEEWRQ NLVESAAEAS EELMEKYLGG
     EELTEEEIKA GLRQRVLAGE IIPVCCGSAF KNKGVQAMLD AVIDYLPAPT DIPAIKGINP
     DETEGERHAS DDEPFSALAF KIATDPFVGN LTFFRVYSGV INSGDTVLNS VKDKRERFGR
     IVQMHANKRE EIKEVRAGDI AAAIGLKDVG TGDTLCAQDA PIILERMEFP EPVISVAVEP
     KTKADQEKMG LALGRLAQED PSFRVHTDEE SGETIISGMG ELHLDIIVDR MRREFKVEAN
     IGKPQVSYRE TIRTRVNDVE GKHAKQSGGR GQYGHVVIDL YPLDPEGPGY EFVNEIKGGV
     IPGEYIPAVD KGVQEQLKSG PLAGYPVVDL GVRLHFGSYH DVDSSELAFK LAASLAFKAA
     FNKANPVLLE PIMKVEVETP PDYVGDVIGD LSRRRAMVNG QEANEFVVKI NAEVPLSEMF
     GYATDLRSQT QGRASYSMEP LKYAEAPKNV ADAIIEARKK