ID EFG_RICTY Reviewed; 699 AA. AC Q8KTB2; Q68XN5; DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 09-NOV-2004, sequence version 2. DT 27-MAR-2024, entry version 127. 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=RT0121; OS Rickettsia typhi (strain ATCC VR-144 / Wilmington). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales; OC Rickettsiaceae; Rickettsieae; Rickettsia; typhus group. OX NCBI_TaxID=257363; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=12140235; DOI=10.1093/oxfordjournals.molbev.a004184; RA Amiri H., Alsmark C.M., Andersson S.G.E.; RT "Proliferation and deterioration of Rickettsia palindromic elements."; RL Mol. Biol. Evol. 19:1234-1243(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC VR-144 / Wilmington; RX PubMed=15317790; DOI=10.1128/jb.186.17.5842-5855.2004; RA McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E., RA McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E., RA Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A., Hong C., RA Yu X.-J., Walker D.H., Weinstock G.M.; RT "Complete genome sequence of Rickettsia typhi and comparison with sequences RT of other Rickettsiae."; RL J. Bacteriol. 186:5842-5855(2004). 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; AF502176; AAM90925.1; -; Genomic_DNA. DR EMBL; AE017197; AAU03607.1; -; Genomic_DNA. DR RefSeq; WP_011190594.1; NC_006142.1. DR AlphaFoldDB; Q8KTB2; -. DR SMR; Q8KTB2; -. DR KEGG; rty:RT0121; -. DR eggNOG; COG0480; Bacteria. DR HOGENOM; CLU_002794_4_1_5; -. DR OrthoDB; 9802948at2; -. DR Proteomes; UP000000604; 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: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..699 FT /note="Elongation factor G" FT /id="PRO_0000091205" FT DOMAIN 8..283 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" FT CONFLICT 263 FT /note="F -> L (in Ref. 1; AAM90925)" FT /evidence="ECO:0000305" FT CONFLICT 306 FT /note="T -> L (in Ref. 1; AAM90925)" FT /evidence="ECO:0000305" FT CONFLICT 641 FT /note="S -> K (in Ref. 1; AAM90925)" FT /evidence="ECO:0000305" SQ SEQUENCE 699 AA; 77652 MW; DAACBEB448B39C37 CRC64; MSKINKLEHI RNIGICAHID AGKTTTTERI LYYTGKSHKI GEVHEGGATM DWMEQEQERG ITITSAATTC KWQDKVINII DTPGHVDFTI EVERSLRVLD GAVAVFDGVA GVEPQSETVW RQADKYNVPR MCFVNKMDRM GADFYKCVDM IKDRLGAKSL ILQLPIGIEE NFKGIINLIK MKAVIWKDES LGAEYFEEDI PTDMQDKAAE YRARLLDMTV ELDDTIMERY LSGEEITEEE IKILIRKGTI EAKFYPVLCG SAFKNKGVQP LLDAIVDFLP SPIDIGIVKG IEVSTSEEKD FPISITEPFS ALAFKIMNDP FVGSLTFIRI YSGKITSGAS VVNTVKNKRE KIGRMLLMHA NNREDIKEAS AGDIVALAGL KDTSTGDTLS DIDTQVVLER MEFPEPVIEL AVEPKSTADQ EKMGLALSRL AAEDPSFKVS TDHETGQTVI KGMGELHLEI IIDRMRREFK VEANIGAPQV AYRETITTAC EIDYTHKKQS GGAGQFARVK IIFEPLKDVI DLKDEDKNKT FVFESKIVGG AVPKEYIPGV EKGLNNIRET GIVAGYPMID FKATLVDGAF HDVDSSVLAF EIAAKGAFRE GMQKGNPKLL EPIMKVEVIT PDEYMGDIIG DLNSRRGQIQ SMDPRGNAQV VTAYVPLAEM FGYVNTLRSL SQGRAQFSMI FSHYDQVPSQ VADIIKAKK //