ID EFG_BRUSU Reviewed; 694 AA. AC Q8G075; G0KAF7; DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 27-MAR-2024, entry version 121. 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=BR1236, BS1330_I1232; OS Brucella suis biovar 1 (strain 1330). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Brucellaceae; Brucella/Ochrobactrum group; Brucella. OX NCBI_TaxID=204722; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1330; RX PubMed=12271122; DOI=10.1073/pnas.192319099; RA Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F., RA Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., RA Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., RA Nelson W.C., Ayodeji B., Kraul M., Shetty J., Malek J.A., Van Aken S.E., RA Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L., RA Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M.; RT "The Brucella suis genome reveals fundamental similarities between animal RT and plant pathogens and symbionts."; RL Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1330; RX PubMed=22038969; DOI=10.1128/jb.06181-11; RA Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R.; RT "Revised genome sequence of Brucella suis 1330."; RL J. Bacteriol. 193:6410-6410(2011). 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; AE014291; AAN30155.1; -; Genomic_DNA. DR EMBL; CP002997; AEM18573.1; -; Genomic_DNA. DR RefSeq; WP_004685700.1; NZ_KN046804.1. DR AlphaFoldDB; Q8G075; -. DR SMR; Q8G075; -. DR GeneID; 55590911; -. DR KEGG; bms:BR1236; -. DR KEGG; bsi:BS1330_I1232; -. DR PATRIC; fig|204722.21.peg.3393; -. DR HOGENOM; CLU_002794_4_1_5; -. DR PhylomeDB; Q8G075; -. DR Proteomes; UP000007104; Chromosome I. 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:UniProt. DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule. 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 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_dom. 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; 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..694 FT /note="Elongation factor G" FT /id="PRO_0000091089" FT DOMAIN 8..287 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 86..90 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00054" FT BINDING 140..143 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00054" SQ SEQUENCE 694 AA; 76265 MW; 1EC9ABC88B769A59 CRC64; MAREYKIEDY RNFGIMAHID AGKTTMTERI LFYTGKNHKI GETHDGASTM DWMEQEQERG ITITSAATTT FWQGRDGKKR RFNIIDTPGH VDFTIEVERS LRVLDGAIAL LDANAGVEPQ TETVWRQAEK YHVPRMVFVN KMDKIGADFY RSVEMVGSRL GAVALPVQLP IGAENDFVGV VDLIEMKALT WDGTIGAPAT VGEIPADMAD KAEEYREKLI ELAVEIDEAA MEAYLEGTMP TNDELRALIR KGTIEVKFHP ILCGTAFKNR GVQPLLDAVV EFLPAPTDVP AIKGIDVKTE TETTRESSDE APLSMLAFKI MNDPFVGSLT FARIYSGKLT KGVSLENTVK GKRERIGRML QMHSNSREDI DEAFAGDIVA LAGLKETTTG DTLCDPLKPV ILERMEFPDP VIEIAIEPKT KADQEKMGIA LNRLAAEDPS FRVKSDEESG QTIIAGMGEL HLDILVDRMK REFKVEANVG APQVAYRESI TRAAEIDYTH KKQSGGSGQF ARVKIIFEPH DGDDFIFESK IVGGSVPKEY IPGVQKGIES VMGAGPLAGF PMLGVKATLI DGAYHDVDSS VLAFEIASRA AFREGAQKAG AQLLEPIMKV EVVTPEDYVG DVIGDLNSRR GQISGTEARG IATVVNAMVP LANMFGYVNS LRSMSQGRAQ YTMQFDHYEP VPTAVAQEIQ KKFA //