ID A0A0T5ZYC8_9BACT Unreviewed; 567 AA. AC A0A0T5ZYC8; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 07-JUN-2017, entry version 7. 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; candidate division WWE3. 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 RT with 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 CC under certain stress conditions. May act as a fidelity factor of CC the translation reaction, by catalyzing a one-codon backward CC translocation of tRNAs on improperly translocated ribosomes. Back- CC translocation proceeds from a post-translocation (POST) complex to CC a pre-translocation (PRE) complex, thus giving elongation factor G CC a second chance to translocate the tRNAs correctly. Binds to CC ribosomes in a GTP-dependent manner. {ECO:0000256|HAMAP- CC Rule:MF_00071}. CC -!- CATALYTIC ACTIVITY: GTP + H(2)O = GDP + phosphate. CC {ECO:0000256|HAMAP-Rule:MF_00071}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP- CC Rule:MF_00071}; Peripheral membrane protein {ECO:0000256|HAMAP- CC Rule:MF_00071}; Cytoplasmic side {ECO:0000256|HAMAP- CC Rule:MF_00071}. CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase CC superfamily. Classic translation factor GTPase family. LepA CC subfamily. {ECO:0000256|HAMAP-Rule:MF_00071}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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 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-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0043022; F:ribosome binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-HAMAP. DR GO; GO:0045727; P:positive regulation of translation; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00071; LepA; 1. DR InterPro; IPR006297; EF-4. DR InterPro; IPR009022; EFG_III-V. DR InterPro; IPR000640; EFG_V. DR InterPro; IPR013842; LepA_GTP-bd_C. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR InterPro; IPR000795; TF_GTP-bd_dom. DR Pfam; PF00679; EFG_C; 1. DR Pfam; PF06421; LepA_C; 1. DR PRINTS; PR00315; ELONGATNFCT. DR SMART; SM00838; EFG_C; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 2. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51722; G_TR_2; 1. PE 3: Inferred from homology; KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_00071}; KW Complete proteome {ECO:0000313|Proteomes:UP000051297}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00071}; KW Hydrolase {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}; KW Reference proteome {ECO:0000313|Proteomes:UP000051297}. FT DOMAIN 6 185 Tr-type G (guanine nucleotide-binding). FT {ECO:0000259|PROSITE:PS51722}. FT NP_BIND 18 23 GTP. {ECO:0000256|HAMAP-Rule:MF_00071}. FT NP_BIND 134 137 GTP. {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 //