ID A0A0T5ZYC8_UNCKA Unreviewed; 567 AA. AC A0A0T5ZYC8; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 13-SEP-2023, entry version 22. DE RecName: Full=Elongation factor 4 {ECO:0000256|HAMAP-Rule:MF_00071}; DE Short=EF-4 {ECO:0000256|HAMAP-Rule:MF_00071}; DE EC=3.6.5.n1 {ECO:0000256|HAMAP-Rule:MF_00071}; DE AltName: Full=Ribosomal back-translocase LepA {ECO:0000256|HAMAP-Rule:MF_00071}; GN Name=lepA {ECO:0000256|HAMAP-Rule:MF_00071}; GN ORFNames=XU08_C0001G0185 {ECO:0000313|EMBL:KRT67775.1}; OS candidate division WWE3 bacterium CSP1-7. OC Bacteria; Katanobacteria. OX NCBI_TaxID=1576480 {ECO:0000313|EMBL:KRT67775.1, ECO:0000313|Proteomes:UP000051297}; RN [1] {ECO:0000313|EMBL:KRT67775.1, ECO:0000313|Proteomes:UP000051297} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CSP1-7 {ECO:0000313|EMBL:KRT67775.1}; RA Hug L.A., Thomas B.C., Sharon I., Brown C.T., Sharma R., Hettich R.L., RA Wilkins M.J., Williams K.H., Singh A., Banfield J.F.; RT "Critical biogeochemical functions in the subsurface are associated with RT bacteria from new phyla and little studied lineages."; RL Submitted (MAY-2015) 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:0000256|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:0000256|HAMAP-Rule:MF_00071}; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_00071}; CC Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_00071}; CC Cytoplasmic side {ECO:0000256|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:0000256|ARBA:ARBA00005454, ECO:0000256|HAMAP-Rule:MF_00071}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:KRT67775.1}. 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; LDXK01000001; KRT67775.1; -; Genomic_DNA. DR AlphaFoldDB; A0A0T5ZYC8; -. DR STRING; 1576480.XU08_C0001G0185; -. DR PATRIC; fig|1576480.3.peg.186; -. DR Proteomes; UP000051297; Unassembled WGS sequence. 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; 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; 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; 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; 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; PS51722; G_TR_2; 1. PE 3: Inferred from homology; KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_00071}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00071}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00071}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_00071}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00071}; KW Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00071}. FT DOMAIN 6..185 FT /note="Tr-type G" FT /evidence="ECO:0000259|PROSITE:PS51722" FT BINDING 18..23 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00071" FT BINDING 134..137 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00071" SQ SEQUENCE 567 AA; 63186 MW; 0574955919D65798 CRC64; MSTSTANIRN FAIIAHIDHG KSTLADRLME RTGLLPPAET ETPRIDRMEL ETERGVTIKL KAVRLPFELL SAKYSLNMID TPGHADFSYE VSRSLAACEG VLLLVDATQG VQAQTLSHLE TARELGLAVV GVINKIDSPL ARIPETEKEL RDLGIEGEIL RLSALEGEGI DEVLRAVVER IPPPQGKLIE PFRALVFDST FDPHLGTIAY VRVVDGEIES ANRPTVKFLG TKASAQVKEI GYFSPDRKPT FALRTGEIGS IATGIRDPRE VRVGDTVVLT NQTTALPGYQ PPQSYVFASF FAKNSDFAEF RRALQTLRLE EPAISIEEIS STAFGRGFRI GFLGTFHLEI VRERLTREFG LELVVTKPTV SFRGLEEEPW ILLTVLTPSE YLARVARLVA ERRGKLGETE TLGNRLKFSA ELPLLEFVRG FYDALKSISH GYASLSWEFL DYRSAPLVEL DILVHEDLVE GLTEIVLRDE AERMGREKLK KLKEILPRQL FAYAIQARSA GKILAREDIS AVRKDVLAKL SGGHVERKMK KLQEQKKGKK KLAKFGRVEM PPAAFLV //