ID EFG_SYNSC Reviewed; 691 AA. AC Q3AMT5; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 22-NOV-2005, sequence version 1. DT 18-JUN-2025, entry version 116. 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=Syncc9605_0321; OS Synechococcus sp. (strain CC9605). OC Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Synechococcales; OC Synechococcaceae; Synechococcus. OX NCBI_TaxID=110662; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CC9605; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Schmutz J., Martinez M., Larimer F., RA Land M., Kyrpides N., Ivanova N., Richardson P.; RT "Complete sequence of Synechococcus sp. CC9605."; RL Submitted (JUL-2005) 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; CP000110; ABB34097.1; -; Genomic_DNA. DR RefSeq; WP_011363347.1; NC_007516.1. DR AlphaFoldDB; Q3AMT5; -. DR SMR; Q3AMT5; -. DR STRING; 110662.Syncc9605_0321; -. DR KEGG; syd:Syncc9605_0321; -. DR eggNOG; COG0480; Bacteria. DR HOGENOM; CLU_002794_4_1_3; -. DR OrthoDB; 580826at2; -. 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; NF009379; PRK12740.1-3; 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..691 FT /note="Elongation factor G" FT /id="PRO_0000263521" FT DOMAIN 8..282 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 81..85 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00054" FT BINDING 135..138 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00054" SQ SEQUENCE 691 AA; 75031 MW; F53654335C8EA2A2 CRC64; MARDFPLERV RNIGIAAHID AGKTTTTERI LFYSGVVHKI GEVHDGAAVT DWMAQERERG ITITAAAIST SWQDHRINII DTPGHVDFTI EVERSMRVLD GVIAVFCAVG GVQPQSETVW RQADRYSVPR MVFVNKMDRT GADFLKVHGQ IKDRLKANAV PIQLPIGAEG ELSGIIDLVA NKAYIYKNDL GTDIEEADVP ADMADEVAEW RNTLMETVAE TDEALIEKFL ESGELSVDDL KKGIREGVLK HGLVPMLCGS AFKNKGVQLV LDAVIDYLPA PVDVPPIQGV LPDGSEAVRP SDDSAPFSAL AFKVMADPYG KLTFVRMYSG ILEKGSYVLN STKGEKERIS RLVVLKADDR EEVDALRAGD LGAVLGLKNT TTGDTLCTQD DPIVLETLFI PEPVISVAVE PKTKGDMEKL SKALVALAEE DPTFRVNTDS ETGQTVIAGM GELHLEILVD RMLREFKVEA NIGAPQVSYR ETIRGSAGGE GKFSRQTGGK GQYGHVVIEM EPGEPGSGFE FVNKIVGGVV PKEYIKPAEQ GMKETCESGV IAGYPLIDVK CTLVHGSYHD VDSSEMAFKI AGSMAFKDGV KKCNPVLLEP MMKVEVEAPE DFLGSIIGDL SSRRGQVEGQ SVEDGTSKIS AKVPLAEMFG YATELRSMTQ GRGIFSMEFD NYAEVPRNVA EAIISKNQGN S //