ID EFG_PORG3 Reviewed; 707 AA. AC B2RLZ4; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-2008, sequence version 1. DT 04-NOV-2026, entry version 101. 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=PGN_1870; OS Porphyromonas gingivalis (strain ATCC 33277 / DSM 20709 / CIP 103683 / JCM OS 12257 / NCTC 11834 / 2561). OC Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales; OC Porphyromonadaceae; Porphyromonas. OX NCBI_TaxID=431947; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / RC 2561; RX PubMed=18524787; DOI=10.1093/dnares/dsn013; RA Naito M., Hirakawa H., Yamashita A., Ohara N., Shoji M., Yukitake H., RA Nakayama K., Toh H., Yoshimura F., Kuhara S., Hattori M., Hayashi T., RA Nakayama K.; RT "Determination of the genome sequence of Porphyromonas gingivalis strain RT ATCC 33277 and genomic comparison with strain W83 revealed extensive genome RT rearrangements in P. gingivalis."; RL DNA Res. 15:215-225(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; AP009380; BAG34389.1; -; Genomic_DNA. DR RefSeq; WP_012458579.1; NC_010729.1. DR AlphaFoldDB; B2RLZ4; -. DR SMR; B2RLZ4; -. DR GeneID; 29257021; -. DR KEGG; pgn:PGN_1870; -. DR eggNOG; COG0480; Bacteria. DR HOGENOM; CLU_002794_4_1_10; -. DR OMA; AACVGMK; -. DR OrthoDB; 9801591at2; -. DR BioCyc; PGIN431947:G1G2V-2084-MONOMER; -. DR Proteomes; UP000008842; Chromosome. 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; 3.30.70.870: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; fusA; 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; Reference proteome. FT CHAIN 1..707 FT /note="Elongation factor G" FT /id="PRO_1000091747" FT DOMAIN 8..288 FT /note="tr-type G" FT REGION 288..308 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 17..24 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00054" FT BINDING 85..89 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00054" FT BINDING 139..142 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00054" SQ SEQUENCE 707 AA; 78326 MW; 924792C58C512CC8 CRC64; MAIDKELQFT RNIGIMAHID AGKTTTSERI LFYTGLTHKI GEVHDGAATM DWMEQEQERG ITITSAATTA FWNYNNQKYK INLIDTPGHV DFTVEVERSL RILDGAVAAF CAVGGVEPQS ETVWRQAEKY NVPRIGYVNK MDRSGANFFE VVRQLREVLG ANPCPIQIPI GAEETFKGVV DLVSMKALVW NDETMGAKYD VEDIPAELVG EAEEWRDKML ETLADCDDTL MEKYFDDPST ITEDEIIAAL RKGTLAMQIN PMLCGSSFKN KGVQTLLDAV CKFLPSPADT PTVEGTDPSD PNKVIERKTS PNEPLCALAF KIATDPYVGR LCFFRVYSGE LPAGSYVYNA RSEKKERISR LFQMHSNKQN PKEVIGCGDI GAGVGFKDIR TGDTLCDENH PIVLESMDFP DPVIGIAVEP KTQKDLDRLG VGLAKLAEED PTFRVQTNED SGQTVISGMG ELHLDIIIDR LRREFKVECN QGRPQVSYKE AINDPVELRE VYKKQTGGRG KFADIICRVE PADADFEGEL QFVDEVKGGN IPKEFIPSIQ KGFQRAMKNG VLAGYPLDQL KVTVIDGSFH PVDSDQLSFE ICALQAFKNA CEKAHPTLME PIMKLEVVTP EESMGDVIGD LNKRRGQVEG MESSRTGARI VKAKVPLAEM FGYVTALRTI TSGRATSTMT FSHYSEVPST IAKQVLTEAQ GRVDLIK //