ID   EFG2_VIBVY              Reviewed;         695 AA.
AC   Q7MI49;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Elongation factor G 2 {ECO:0000255|HAMAP-Rule:MF_00054};
DE            Short=EF-G 2 {ECO:0000255|HAMAP-Rule:MF_00054};
GN   Name=fusA2 {ECO:0000255|HAMAP-Rule:MF_00054}; OrderedLocusNames=VV2668;
OS   Vibrio vulnificus (strain YJ016).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=196600;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJ016;
RX   PubMed=14656965; DOI=10.1101/gr.1295503;
RA   Chen C.-Y., Wu K.-M., Chang Y.-C., Chang C.-H., Tsai H.-C., Liao T.-L.,
RA   Liu Y.-M., Chen H.-J., Shen A.B.-T., Li J.-C., Su T.-L., Shao C.-P.,
RA   Lee C.-T., Hor L.-I., Tsai S.-F.;
RT   "Comparative genome analysis of Vibrio vulnificus, a marine pathogen.";
RL   Genome Res. 13:2577-2587(2003).
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. {ECO:0000255|HAMAP-
CC       Rule:MF_00054}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00054}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. EF-G/EF-2
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_00054}.
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DR   EMBL; BA000037; BAC95432.1; -; Genomic_DNA.
DR   RefSeq; WP_011079653.1; NC_005139.1.
DR   AlphaFoldDB; Q7MI49; -.
DR   SMR; Q7MI49; -.
DR   STRING; 672.VV93_v1c23890; -.
DR   PRIDE; Q7MI49; -.
DR   EnsemblBacteria; BAC95432; BAC95432; BAC95432.
DR   GeneID; 66965838; -.
DR   KEGG; vvy:VV2668; -.
DR   eggNOG; COG0480; Bacteria.
DR   HOGENOM; CLU_002794_4_1_6; -.
DR   OMA; STTDFME; -.
DR   OrthoDB; 88967at2; -.
DR   Proteomes; UP000002675; Chromosome I.
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..695
FT                   /note="Elongation factor G 2"
FT                   /id="PRO_0000091265"
FT   DOMAIN          5..280
FT                   /note="tr-type G"
FT   BINDING         14..21
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
FT   BINDING         78..82
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
FT   BINDING         132..135
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00054"
SQ   SEQUENCE   695 AA;  76514 MW;  E7B5A69BD989063F CRC64;
     MADLSKYRNI GIFAHVDAGK TTTTERILKL TGKIHRLGEV HDGASTMDFM DQEAERGITI
     QSAATTCFWK DHRFNVIDTP GHVDFTVEVY RSLKVLDGGI GVFCGSGGVE PQSETNWRYA
     NESEVSRLIF VNKLDRMGAD FFRVVEQVKK VLGANPLVMT LPIGREDEFV GVVDVLTRQA
     FVWDDSGLPE NYEIKEIPAD MVDQVEEYRE MMIESAVEQD DELMMAYMEG EEPSIEQIKA
     CIRKGTRDLA FFPTYCGSAF KNKGMQLVLD AVVDYLPSPT EVEPQPLTNP ETGEPTGEVA
     TVSVDAPLKA LAFKIMDDRF GALTFIRIYS GRLKKGDTVL NSATGKTERI GRMVEMHAND
     RNELEAAQAG DIIAVVGMKN VQTGHTLCDP KHECTLEPMI FPEPVISIAV KPKDKNGSEK
     MGIAIGKMVA EDPSFQVETD EDSGETILKG MGELHLDIKV DILKRTYGVE LEVGAPQVAY
     RETITKAVED SYTHKKQSGG SGQFGKIDYR IKPGEPNSGF TFKSTVVGGN VPKEFWPAVE
     KGFEGMMQNG VLAGFPTLDV EVELFDGGFH AVDSSAIAFE IAAKGAFRQS MPKAGPQLLE
     PIMKVDVFTP EDHVGDVIGD LNRRRGMIKN QEMGATGVRV KADVPLSEMF GYIGTLRTMT
     SGRGQFSMEF SHYSACPSNV AEQVIAEVKE RNAKK