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EFG2_ALIF1
ID   EFG2_ALIF1              Reviewed;         695 AA.
AC   Q5E7H2;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 102.
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=VF_0529;
OS   Aliivibrio fischeri (strain ATCC 700601 / ES114) (Vibrio fischeri).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Aliivibrio.
OX   NCBI_TaxID=312309;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700601 / ES114;
RX   PubMed=15703294; DOI=10.1073/pnas.0409900102;
RA   Ruby E.G., Urbanowski M., Campbell J., Dunn A., Faini M., Gunsalus R.,
RA   Lostroh P., Lupp C., McCann J., Millikan D., Schaefer A., Stabb E.,
RA   Stevens A., Visick K., Whistler C., Greenberg E.P.;
RT   "Complete genome sequence of Vibrio fischeri: a symbiotic bacterium with
RT   pathogenic congeners.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:3004-3009(2005).
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; CP000020; AAW85024.1; -; Genomic_DNA.
DR   RefSeq; WP_011261294.1; NC_006840.2.
DR   RefSeq; YP_203912.1; NC_006840.2.
DR   AlphaFoldDB; Q5E7H2; -.
DR   SMR; Q5E7H2; -.
DR   STRING; 312309.VF_0529; -.
DR   EnsemblBacteria; AAW85024; AAW85024; VF_0529.
DR   KEGG; vfi:VF_0529; -.
DR   PATRIC; fig|312309.11.peg.520; -.
DR   eggNOG; COG0480; Bacteria.
DR   HOGENOM; CLU_002794_4_1_6; -.
DR   OMA; STTDFME; -.
DR   OrthoDB; 88967at2; -.
DR   Proteomes; UP000000537; 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_0000225248"
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;  76048 MW;  9D833384047755D3 CRC64;
     MTDLSKYRNI GIFAHVDAGK TTTTERILKL TGKIHKIGDT HDGSTTTDFM EQEAERGITI
     QSAAVSCFWN DHRLNVIDTP GHVDFTVEVY RSLKVLDGGI GVFCGSGGVE PQSETNWRYA
     NESEVSRLIF VNKLDRMGAD FFSVVDQVKK VLGATPLVMT LPIGREEDFV GVVDVLNRQA
     FVWDDSGLPE NYEIQDIPAD MVDDVEAYRE ELVETAVEQD DDLMEAYMEG QEPSIEELKR
     CIRKGTRDLA FFPTFCGSAY KNKGIQLILD AVVDYLPAPN EVEPQPLTDK DTGEETGEVA
     TVSADEPFRA LAFKIMDDRF GALTFVRIYS GKLNKGDTVL NSATGKTERI GRMVEMQADE
     RNELTSAQAG DIIAIVGMKN VQTGHTLCDV KHECTLEPMI FPVPVISIAV APKDKGGSEK
     MGIAIGKMVA EDPSFQVETD EETGETILKG MGELHLDIKV DILKRTYGVD LVVGQPQVAY
     RETITQAIED SYTHKKQSGG SGQFGKIDYR IKPGEAGTGF TFSSTVVGGN VPKEFWPAVE
     KGFASMMETG PLAGFPVLDV EVELFDGGFH AVDSSAIAFE IAAKGAFRQS MPKAGAQLLE
     PIMKVDVFTP EDHVGDVIGD LNRRRGMIKD QQAGLTGVRI KGDVPLSEMF GYIGTLRTMT
     SGRGQFSMEF SHYAPCPNSV AEEVIAKAKE EKAAK
 
 
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