ID EFG_WOLPP Reviewed; 691 AA. AC B3CLA3; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 22-JUL-2008, sequence version 1. DT 28-JAN-2026, entry version 102. 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}; OrderedLocusNames=WP0562; OS Wolbachia pipientis subsp. Culex pipiens (strain wPip). OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria; OC Rickettsiales; Anaplasmataceae; Wolbachieae; Wolbachia. OX NCBI_TaxID=570417; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=wPip; RX PubMed=18550617; DOI=10.1093/molbev/msn133; RA Klasson L., Walker T., Sebaihia M., Sanders M.J., Quail M.A., Lord A., RA Sanders S., Earl J., O'Neill S.L., Thomson N., Sinkins S.P., Parkhill J.; RT "Genome evolution of Wolbachia strain wPip from the Culex pipiens group."; RL Mol. Biol. Evol. 25:1877-1887(2008). 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; AM999887; CAQ54670.1; -; Genomic_DNA. DR RefSeq; WP_010406835.1; NC_010981.1. DR AlphaFoldDB; B3CLA3; -. DR SMR; B3CLA3; -. DR KEGG; wpi:WP0562; -. DR eggNOG; COG0480; Bacteria. DR HOGENOM; CLU_002794_4_1_5; -. 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:0097216; F:guanosine tetraphosphate binding; IEA:UniProtKB-ARBA. 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..691 FT /note="Elongation factor G" FT /id="PRO_1000091779" FT DOMAIN 6..281 FT /note="tr-type G" FT BINDING 15..22 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00054" FT BINDING 79..83 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00054" FT BINDING 133..136 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00054" SQ SEQUENCE 691 AA; 76474 MW; 297F86348B8A728A CRC64; MEVLISRYRN IGIMAHIDAG KTTTTERILF YTGKQNRIGE VHDGAASMDW MEQEKERGIT ITSAATTCFW NDHRINIIDT PGHVDFTIEV ERSLRVLDGA VAVFDGVAGV EPQSETVWRQ ADKYNVPRIC FVNKMDRIGA NFYRCVDMIK TKLGASPLVI QLPIGSEKDF KGIIDLISMK AIIWQEETLG AKFSYEDIPS DLLDKAQEYR NLLLDAAAEM DDEAINTYFE SNDLPIDLLK KCVRSGTIKG KFVPVLCGSA FKNKGVQSLL DGVVDFLPSP IDVDVIIGTD PKDSEKKIEI KPSEKEKFVA LAFKVMTDKF VGSLTFIRIY SGKLKSKSAV LNAGKNETEG IGRMLLMHAN NREDINEAKV GDIVALVGLK KTITGDTLCS SDFPILLERM EFPDPVIEIA IEPKTTSDQE KLGVALNRLV AEDPSLRMSV NAESGQTILK GMGELHLEII IDRMKREFNV EANVGAPQVA YRETITKSVE IDYTHKKQSG GAGQFAKVKI KFEPLEPGFG FQFESKIVGG AIPKEYIPGV QNGLELIKEG GIISGFPLID FKATLLDGAF HDVDSSPLAF ELAAKGAFKE MANKAGPKML EPIMKVEIIT PEEYMGDVMG DINSRRGSVV DMLDLGNNSK IITASVPLAN MFGYINVLRS ISQGRAQYSM HFSCYEQVPQ YVVDELKLKY N //