ID LEPA_MARSD Reviewed; 601 AA. AC C6BST2; DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot. DT 01-SEP-2009, sequence version 1. DT 09-APR-2025, entry version 88. 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=Desal_3490; OS Maridesulfovibrio salexigens (strain ATCC 14822 / DSM 2638 / NCIMB 8403 / OS VKM B-1763) (Desulfovibrio salexigens). OC Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfovibrionia; OC Desulfovibrionales; Desulfovibrionaceae; Maridesulfovibrio. OX NCBI_TaxID=526222; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 14822 / DSM 2638 / NCIMB 8403 / VKM B-1763; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D., RA Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C., RA Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Anderson I., RA Wall J.D., Arkin A.P., Dehal P., Chivian D., Giles B., Hazen T.C.; RT "Complete sequence of Desulfovibrio salexigens DSM 2638."; RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases. 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 + phosphate + H(+); 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 inner membrane {ECO:0000255|HAMAP- CC Rule:MF_00071}; Peripheral membrane protein {ECO:0000255|HAMAP- CC Rule:MF_00071}; 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; CP001649; ACS81538.1; -; Genomic_DNA. DR RefSeq; WP_015853354.1; NC_012881.1. DR AlphaFoldDB; C6BST2; -. DR SMR; C6BST2; -. DR STRING; 526222.Desal_3490; -. DR KEGG; dsa:Desal_3490; -. DR eggNOG; COG0481; Bacteria. DR HOGENOM; CLU_009995_3_3_7; -. DR OrthoDB; 9801472at2; -. DR Proteomes; UP000002601; 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: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 FunFam; 3.40.50.300:FF:000078; Elongation factor 4; 1. DR FunFam; 2.40.30.10:FF:000015; Translation factor GUF1, mitochondrial; 1. DR FunFam; 3.30.70.240:FF:000007; Translation factor GUF1, mitochondrial; 1. DR FunFam; 3.30.70.2570:FF:000001; Translation factor GUF1, mitochondrial; 1. DR FunFam; 3.30.70.870:FF:000004; Translation factor GUF1, mitochondrial; 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. 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 SMART; SM00838; EFG_C; 1. 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 inner membrane; Cell membrane; GTP-binding; Hydrolase; Membrane; KW Nucleotide-binding; Protein biosynthesis; Reference proteome. FT CHAIN 1..601 FT /note="Elongation factor 4" FT /id="PRO_1000202446" FT DOMAIN 5..187 FT /note="tr-type G" FT BINDING 17..22 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00071" FT BINDING 134..137 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00071" SQ SEQUENCE 601 AA; 67050 MW; 07082EC120712C2A CRC64; MAKLDKIRNF SIIAHIDHGK STLADRILEI TGMVSEREKK DQYLDKMELE QERGITIKAQ TVRIPYKAND GEEYILNLID TPGHVDFSYE VSRSLAASEG ALLVVDSTQG VEAQTLANVF LALDHDLEIV PVLNKVDLPS SDCERVAQEI EEVIGLDCSE PLMISAKTGL NVEDVLESIV KDLPAPQGDP DAPLKALIFD SWYDSYQGVV VLFRILDGTI KKGDKIQIHS TGRTFDVTTL GVYTPEPQKA KELAAGEVGF LCASMKELND APVGDTITLA ADPVEDPFPG FQEVKPMVFC GLYPVEPAEY EPLKAALEKL QLNDTAFSFE PETSTALGFG FRCGFLGLLH MEIIQERLER EFQAKLIATA PSVVYQARLN NGEVLEIDNP SKMPDGGDLE SLAEPFCRLE IHVPNDYVGA VLKLCEEKRG IQKDMRYLTS SRVIITYEVP FAEIMYDFFD KLKSHTKGYA SLDYEIIDYR ESNLVKLDIL INTDPVDAFS AIVHKDSAYP FGRSLALKLK RAIPRQMFEI VIQAAIGRKI IAKERVAPFR KNVTAKCYGG DITRKRKLLE KQKEGKKRMK KMGNVEIPQE AFMAVLKAGE D //