ID LEPA_BUCAP Reviewed; 601 AA. AC Q8K9Q9; DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 27-MAR-2024, entry version 126. DE RecName: Full=Elongation factor 4 {ECO:0000255|HAMAP-Rule:MF_00071}; DE Short=EF-4 {ECO:0000255|HAMAP-Rule:MF_00071}; DE EC=3.6.5.n1 {ECO:0000255|HAMAP-Rule:MF_00071}; DE AltName: Full=Ribosomal back-translocase LepA {ECO:0000255|HAMAP-Rule:MF_00071}; GN Name=lepA {ECO:0000255|HAMAP-Rule:MF_00071}; GN OrderedLocusNames=BUsg_251; OS Buchnera aphidicola subsp. Schizaphis graminum (strain Sg). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Erwiniaceae; Buchnera. OX NCBI_TaxID=198804; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Sg; RX PubMed=12089438; DOI=10.1126/science.1071278; RA Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., RA Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.; RT "50 million years of genomic stasis in endosymbiotic bacteria."; RL Science 296:2376-2379(2002). CC -!- FUNCTION: Required for accurate and efficient protein synthesis under CC certain stress conditions. May act as a fidelity factor of the CC translation reaction, by catalyzing a one-codon backward translocation CC of tRNAs on improperly translocated ribosomes. Back-translocation CC proceeds from a post-translocation (POST) complex to a pre- CC translocation (PRE) complex, thus giving elongation factor G a second CC chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP- CC dependent manner. {ECO:0000255|HAMAP-Rule:MF_00071}. CC -!- CATALYTIC ACTIVITY: CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.n1; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00071}; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00071}; CC Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_00071}; CC Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_00071}. CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase CC superfamily. Classic translation factor GTPase family. LepA subfamily. CC {ECO:0000255|HAMAP-Rule:MF_00071}. 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; AE013218; AAM67810.1; -; Genomic_DNA. DR AlphaFoldDB; Q8K9Q9; -. DR SMR; Q8K9Q9; -. DR STRING; 198804.BUsg_251; -. DR KEGG; bas:BUsg_251; -. DR eggNOG; COG0481; Bacteria. DR HOGENOM; CLU_009995_3_3_6; -. DR Proteomes; UP000000416; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule. DR GO; GO:0097216; F:guanosine tetraphosphate binding; IEA:UniProt. DR GO; GO:0043022; F:ribosome binding; IEA:UniProtKB-UniRule. DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule. DR GO; GO:0045727; P:positive regulation of translation; IEA:UniProtKB-UniRule. DR CDD; cd03699; EF4_II; 1. DR CDD; cd16260; EF4_III; 1. DR CDD; cd01890; LepA; 1. DR CDD; cd03709; lepA_C; 1. DR Gene3D; 3.30.70.240; -; 1. DR Gene3D; 3.30.70.2570; Elongation factor 4, C-terminal domain; 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_00071; LepA; 1. DR InterPro; IPR006297; EF-4. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR000640; EFG_V-like. DR InterPro; IPR004161; EFTu-like_2. DR InterPro; IPR031157; G_TR_CS. DR InterPro; IPR038363; LepA_C_sf. DR InterPro; IPR013842; LepA_CTD. DR InterPro; IPR035654; LepA_IV. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR InterPro; IPR000795; T_Tr_GTP-bd_dom. DR NCBIfam; TIGR01393; lepA; 1. DR NCBIfam; TIGR00231; small_GTP; 1. DR PANTHER; PTHR43512:SF4; TRANSLATION FACTOR GUF1 HOMOLOG, CHLOROPLASTIC; 1. DR PANTHER; PTHR43512; TRANSLATION FACTOR GUF1-RELATED; 1. DR Pfam; PF00679; EFG_C; 1. DR Pfam; PF00009; GTP_EFTU; 1. DR Pfam; PF03144; GTP_EFTU_D2; 1. DR Pfam; PF06421; LepA_C; 1. DR PRINTS; PR00315; ELONGATNFCT. DR SUPFAM; SSF54980; EF-G C-terminal domain-like; 2. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS00301; G_TR_1; 1. DR PROSITE; PS51722; G_TR_2; 1. PE 3: Inferred from homology; KW Cell membrane; GTP-binding; Hydrolase; Membrane; Nucleotide-binding; KW Protein biosynthesis. FT CHAIN 1..601 FT /note="Elongation factor 4" FT /id="PRO_0000176247" FT DOMAIN 6..188 FT /note="tr-type G" FT BINDING 18..23 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00071" FT BINDING 135..138 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00071" SQ SEQUENCE 601 AA; 67748 MW; AAEA8B0EF6091ECA CRC64; MVKKMKNIRN FSIIAHIDHG KSTLSDRLIQ KCGGLSEREM SDQVLDSMDL EKERGITIKA QSVMIDYKDK NGNVFHLNFI DTPGHVNFSY EVSRSLAACE GALLVVDSSQ GVEAQTLANC ATALEMKLSI VPVLNKIDLP NSNPEKVARE IKEIIGISAL DAIRCSAKTG QGIEELIEQI IKKIPAPDGD EKKPLQALII DSWFDNYLGV VSLIRIKNGI ISKKDKIKVM STGKTYFVDH LGIFTPKKIN KNYLKCGEVG WIVCGIKNIS AAPVGDTLTN AKNPAMNMLT GFKKIKPQIY AGLFPVTSDQ YEIFRDALGK LSLNDSSLFY EPINSTALGF GFRCGFLGLL HMEIVQARLE REYSLNLIST APNVIYQIEF NNGEKIYLDT PSNFPVDNKI RKIKEPIVEC NILLPPKFLG PVMKLCIKKR GTEINMIYHE QQVSLKYHIP MNEVVLNFFD ELKSVSSGYA SLEYDFKYFK TVKMVRIDIL INSERVDALT VISYYKNAQN RAREIVNKMK ELIPRHQFDI NIQATINNSI VARSTIKQLR KNVLAKCYGG DISRKKKLLK KQKDGKKRMK KIGNVNMPKT AFLDILNIHK D //