ID EFG1_BORBR Reviewed; 700 AA. AC Q7WRC7; DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2003, sequence version 1. DT 10-JUN-2026, entry version 124. DE RecName: Full=Elongation factor G 1 {ECO:0000255|HAMAP-Rule:MF_00054}; DE Short=EF-G 1 {ECO:0000255|HAMAP-Rule:MF_00054}; GN Name=fusA1 {ECO:0000255|HAMAP-Rule:MF_00054}; GN OrderedLocusNames=BB0026; OS Bordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50) OS (Alcaligenes bronchisepticus). OC Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria; OC Burkholderiales; Alcaligenaceae; Bordetella. OX NCBI_TaxID=257310; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-588 / NCTC 13252 / RB50; RX PubMed=12910271; DOI=10.1038/ng1227; RA Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R., RA Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L., RA Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A., RA Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I., RA Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T., RA Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S., RA Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E., RA Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M., RA Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S., RA Barrell B.G., Maskell D.J.; RT "Comparative analysis of the genome sequences of Bordetella pertussis, RT Bordetella parapertussis and Bordetella bronchiseptica."; RL Nat. Genet. 35:32-40(2003). 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; BX640437; CAE30528.1; -; Genomic_DNA. DR RefSeq; WP_003806902.1; NC_002927.3. DR AlphaFoldDB; Q7WRC7; -. DR SMR; Q7WRC7; -. DR GeneID; 56481291; -. DR KEGG; bbr:BB0026; -. DR eggNOG; COG0480; Bacteria. DR HOGENOM; CLU_002794_4_1_4; -. DR Proteomes; UP000001027; 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: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; Reference proteome. FT CHAIN 1..700 FT /note="Elongation factor G 1" FT /id="PRO_0000091078" FT DOMAIN 8..290 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 88..92 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00054" FT BINDING 142..145 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00054" SQ SEQUENCE 700 AA; 77088 MW; 053E7A662EFCC51F CRC64; MARKTPIERY RNIGISAHID AGKTTTTERI LFYTGVNHKL GETHDGSATM DWMEQEQERG ITITSAATTA FWRGMAGNYP EHRINIIDTP GHVDFTIEVE RSMRVLDGAC MVYCAVGGVQ PQSETVWRQA NKYGVPRLAF VNKMDRTGAN FFKVYDQLKT RLRANPVPIV IPIGAEDSFT GVVDLVKMKA IIWDEASQGT KFEYGDIPAE LEGTANEWRE KLVEAAAESS EELMNKYLET GSLDEDDINV ALRQRTIAGE IQPMLCGTAF KNKGVQRMLD AVIDYLPSPA DIPPVDGQDD DGNPIKRSAD DAEKFSALAF KLMSDPFVGQ LTFVRVYSGV LKSGDTVYNP IKGKKERIGR LLQMHANNRE EIKEVLAGDI AAVVGLKDVT TGETLCDIDS HILLERMEFP EPVISQAVEP KSKADQEKMG LALSRLAQED PSFRVRSDEE SGQTIISGMG ELHLEILVDR MRREFGVEAN VGKPQVAYRE TIRKNCDEVE GKFVKQSGGR GQYGHVVLKL EPLPPGGGYE FVDAIKGGVV PREYIPAVDK GIQETLPAGI LAGYPVVDVK ATLFFGSYHD VDSNENAFKM AASMAFKEGM RRASPVLLEP MMAVEVETPE DYAGTVMGDL SSRRGMVQGM DDIVGGGKTI KAEVPLAEMF GYATNLRSLT QGRATYTMEF KHYAEAPKNV ADEVIAARGK //