ID EFG_CHLPM Reviewed; 704 AA. AC A4SCQ6; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAY-2007, sequence version 1. DT 18-JUN-2025, entry version 106. DE RecName: Full=Elongation factor G {ECO:0000255|HAMAP-Rule:MF_00054}; DE Short=EF-G {ECO:0000255|HAMAP-Rule:MF_00054}; GN Name=fusA {ECO:0000255|HAMAP-Rule:MF_00054}; GN OrderedLocusNames=Cvib_0243; OS Chlorobium phaeovibrioides (strain DSM 265 / 1930) (Prosthecochloris OS vibrioformis (strain DSM 265)). OC Bacteria; Pseudomonadati; Chlorobiota; Chlorobiia; Chlorobiales; OC Chlorobiaceae; Chlorobium/Pelodictyon group; Chlorobium. OX NCBI_TaxID=290318; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 265 / 1930; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Schmutz J., RA Larimer F., Land M., Hauser L., Mikhailova N., Li T., Overmann J., RA Schuster S.C., Bryant D.A., Richardson P.; RT "Complete sequence of Prosthecochloris vibrioformis DSM 265."; RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000607; ABP36265.1; -; Genomic_DNA. DR AlphaFoldDB; A4SCQ6; -. DR SMR; A4SCQ6; -. DR STRING; 290318.Cvib_0243; -. DR KEGG; pvi:Cvib_0243; -. DR eggNOG; COG0480; Bacteria. DR HOGENOM; CLU_002794_4_1_10; -. DR OrthoDB; 9801591at2; -. 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 GO; GO:0032790; P:ribosome disassembly; IEA:TreeGrafter. DR CDD; cd01886; EF-G; 1. DR CDD; cd16262; EFG_III; 1. DR CDD; cd01434; EFG_mtEFG1_IV; 1. DR CDD; cd03713; EFG_mtEFG_C; 1. DR CDD; cd04088; EFG_mtEFG_II; 1. DR FunFam; 2.40.30.10:FF:000006; Elongation factor G; 1. DR FunFam; 3.30.230.10:FF:000003; Elongation factor G; 1. DR FunFam; 3.30.70.240:FF:000001; Elongation factor G; 1. DR FunFam; 3.30.70.870:FF:000001; Elongation factor G; 1. DR FunFam; 3.40.50.300:FF:000029; Elongation factor G; 1. DR Gene3D; 3.30.230.10; -; 1. DR Gene3D; 3.30.70.240; -; 1. DR Gene3D; 3.30.70.870; Elongation Factor G (Translational Gtpase), domain 3; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR Gene3D; 2.40.30.10; Translation factors; 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; IPR047872; EFG_IV. 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_Su5_D2-typ_SF. DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr. DR InterPro; IPR005225; Small_GTP-bd. 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 NCBIfam; TIGR00484; EF-G; 1. DR NCBIfam; NF009381; PRK12740.1-5; 1. DR NCBIfam; TIGR00231; small_GTP; 1. DR PANTHER; PTHR43261:SF1; RIBOSOME-RELEASING FACTOR 2, MITOCHONDRIAL; 1. DR PANTHER; PTHR43261; TRANSLATION ELONGATION FACTOR G-RELATED; 1. 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; SSF54980; EF-G C-terminal domain-like; 2. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1. DR SUPFAM; SSF50447; Translation proteins; 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. FT CHAIN 1..704 FT /note="Elongation factor G" FT /id="PRO_1000074967" FT DOMAIN 8..291 FT /note="tr-type G" FT BINDING 17..24 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00054" FT BINDING 90..94 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00054" FT BINDING 144..147 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00054" SQ SEQUENCE 704 AA; 78045 MW; 81923B68A0AA4C71 CRC64; MTRQVALDKV RNIGIMAHID AGKTTTTERI LYYTGRLHRM GEVHDGGATM DWMEQEKERG ITITSAATTC FWSPKYGNYK GENHRINIID TPGHVDFTVE VERSLRVLDG AVALFCAVGG VEPQSETVWR QANKYGVPRI AYINKMDRTG ADFFDTIKAI RERLNSNPVP LQIPIGEGEI YAGFVDLIRM KGIIFDKEDG STYEEVEIPH DLENEARTWR INMLEAVSEV DETLLEKYLN GEDITESEVR KVLRQATLNV DIIPVLCGSS FKNKGVQFML DAVVDYLASP LDDGEVEGHH PRTEEDVVRH PSDDEPFAAL AFKIATDPFV GKLTFFRVYS GMLKAGSYVL NSITGKKERV GRVLQMHSNK REDLDAVYAG DIAAAVGLKE VRTGDTLCDE ASPVVLEKMV FPEPVIQIAI EPKTKVDSDK LGVSLAKLAE EDPTFRVKTD DETGQTLIAG MGELHLEILV DRLRREFKVE ANVGQPQVAY RETIRSKVDF EGKFVRQSGG KGQFGLVNIT VEPLEEGKGY EFVDAVKGGV IPREYIPAVN AGIQEAMKDG VVAGYPMQDI KVTLFDGKYH DVDSSEMAFK IAGSIGFKGG ARKANPVLLE PIMKVEVVTP EEYLGDVMGD LSGRRGHIEG MGQRAGAQFV GAKVPLSAMF GYSTDLRSMT QGRANYSMEF ESYREVPKNI AETLQEKRSS KDAQ //