ID A0A088CM22_9XANT Unreviewed; 197 AA. AC A0A088CM22; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 27-NOV-2024, entry version 22. DE RecName: Full=Elongation factor G {ECO:0000256|ARBA:ARBA00017872}; DE Flags: Fragment; GN Name=fusA {ECO:0000313|EMBL:AIF74998.1}; OS Xanthomonas sp. NI1. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Lysobacterales; OC Lysobacteraceae; Xanthomonas. OX NCBI_TaxID=1507997 {ECO:0000313|EMBL:AIF74998.1}; RN [1] {ECO:0000313|EMBL:AIF74998.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NI1 {ECO:0000313|EMBL:AIF74998.1}; RA Jibrin M.O., Timilsina S., Potnis N., Minsavage G.V., Shenge K.C., RA Akpa A.D., Alegbejo M.D., Beed F., Vallad G.E., Jones J.B.; RT "First Report of Xanthomonas euvesicatoria Causing Bacterial Spot Disease RT in Pepper in Northwestern Nigeria."; RL Plant Dis. 98:1426-1426(2014). 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. CC {ECO:0000256|ARBA:ARBA00024731}. 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; KJ938581; AIF74998.1; -; Genomic_DNA. DR AlphaFoldDB; A0A088CM22; -. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW. DR GO; GO:0032790; P:ribosome disassembly; IEA:TreeGrafter. DR CDD; cd01434; EFG_mtEFG1_IV; 1. DR CDD; cd03713; EFG_mtEFG_C; 1. DR FunFam; 3.30.230.10:FF:000003; 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 InterPro; IPR035647; EFG_III/V. DR InterPro; IPR047872; EFG_IV. DR InterPro; IPR035649; EFG_V. DR InterPro; IPR000640; EFG_V-like. DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF. DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr. DR InterPro; IPR005517; Transl_elong_EFG/EF2_IV. 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; PF03764; EFG_IV; 1. DR SMART; SM00838; EFG_C; 1. DR SMART; SM00889; EFG_IV; 1. DR SUPFAM; SSF54980; EF-G C-terminal domain-like; 2. DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1. PE 4: Predicted; KW Elongation factor {ECO:0000256|ARBA:ARBA00022768, KW ECO:0000313|EMBL:AIF74998.1}; GTP-binding {ECO:0000256|ARBA:ARBA00023134}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}; KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022768, KW ECO:0000313|EMBL:AIF74998.1}. FT DOMAIN 25..152 FT /note="Translation elongation factor EFG/EF2" FT /evidence="ECO:0000259|SMART:SM00889" FT DOMAIN 154..197 FT /note="Elongation factor EFG" FT /evidence="ECO:0000259|SMART:SM00838" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:AIF74998.1" FT NON_TER 197 FT /evidence="ECO:0000313|EMBL:AIF74998.1" SQ SEQUENCE 197 AA; 21769 MW; A1D2DB4FA75FAF87 CRC64; ELHLDIIVDR MRREFNVEAN VGKPQVAYRE TIRKSDVKSD YKHAKQSGGK GQYGHVVIEL SPMTEEERKS ENVKDDFLFI NDITGGIIPK EFIPSVEKGL RETITSGPIA GFPVVGVKVK LVFGSYHDVD SSEMAFKLAA SMAFKQGFAK ASPVLLEPIM KVEIVSPEDY LGDVMGDVSR RRGVLQGQDD SPSGKII //