ID   EFG2_VIBPA              Reviewed;         696 AA.
AC   Q87M30;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 107.
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=VP2428;
OS   Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=223926;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RIMD 2210633;
RX   PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA   Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA   Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA   Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT   "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT   distinct from that of V. cholerae.";
RL   Lancet 361:743-749(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; BA000031; BAC60691.1; -; Genomic_DNA.
DR   RefSeq; NP_798807.1; NC_004603.1.
DR   RefSeq; WP_005456593.1; NC_004603.1.
DR   AlphaFoldDB; Q87M30; -.
DR   SMR; Q87M30; -.
DR   STRING; 223926.28807426; -.
DR   EnsemblBacteria; BAC60691; BAC60691; BAC60691.
DR   GeneID; 1189941; -.
DR   KEGG; vpa:VP2428; -.
DR   PATRIC; fig|223926.6.peg.2329; -.
DR   eggNOG; COG0480; Bacteria.
DR   HOGENOM; CLU_002794_4_1_6; -.
DR   OMA; STTDFME; -.
DR   Proteomes; UP000002493; Chromosome 1.
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..696
FT                   /note="Elongation factor G 2"
FT                   /id="PRO_0000091262"
FT   DOMAIN          5..281
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   696 AA;  76367 MW;  B6C9989C0593FFD8 CRC64;
     MTDLSKYRNI GIFAHVDAGK TTSTERILKL TGKIHKIGDT HDGSTTTDFM EQEAERGITI
     QSAATTCFWN DHRLNIIDTP GHVDFTIEVY RSLKVLDGGI GVFCGSGGVE PQSETNWRYA
     DESHVSRLIF VNKLDRMGAD FYKVVDQVQN VLGATPLVMT LPIGIEEDFV GVVDVLSQQA
     YVWDESGQPE NYEVQEIPAD MVDKAAEYRE MLIETALEQD EDLMMAYLEE GEEPSVEDIK
     RCIRKGTRDL AFFPTYCGSA YKNKGMQLIL DAVVDYLPSP TEVDPQPLTD PDTGEATGEV
     ATVSADEPLK ALAFKIMDDR FGALTFIRIY SGKMKKGDTV LNSATGKTER IGRMVEMHAD
     ERNEIDSAQA GDIIAVVGMK NVQTGHTLCD PKHECTLEPM IFPEPVISIA VKPKDKGGSE
     KMGIAIGKMV AEDPSFQVET DEESGETILK GMGELHLDIK VDILKRTYGV ELEVGAPQVA
     YRETITQAIE DSYTHKKQSG GSGQFAKIDY RIKPGEVGSG FTFKSTVVGG NVPKEFWPAV
     EKGFAGMMET GVLAGFPTLD VEVELYDGGF HAVDSSAIAY EIAAKGAFRQ SMPKAGAQLL
     EPIMKVDVFT PEDHVGDVIG DLNRRRGMIK DQQAGTTGVR IKGDVPLSEM FGYIGTLRTM
     TSGRGQFSME FSHYSPCPNN VAEQVIADVK ERNAKK