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Database: UniProt
Entry: A0A090VYE4_ESCVU
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ID   A0A090VYE4_ESCVU        Unreviewed;       599 AA.
AC   A0A090VYE4;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   28-MAR-2018, 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   ECO:0000313|EMBL:GAL60282.1};
GN   ORFNames=EV102420_34_00190 {ECO:0000313|EMBL:GAL60282.1};
OS   Pseudescherichia vulneris NBRC 102420.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Pseudescherichia.
OX   NCBI_TaxID=1115515 {ECO:0000313|EMBL:GAL60282.1, ECO:0000313|Proteomes:UP000029462};
RN   [1] {ECO:0000313|EMBL:GAL60282.1, ECO:0000313|Proteomes:UP000029462}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 102420 {ECO:0000313|EMBL:GAL60282.1,
RC   ECO:0000313|Proteomes:UP000029462};
RA   Yoshida Y., Hosoyama A., Tsuchikane K., Ohji S., Ichikawa N.,
RA   Kimura A., Yamazoe A., Ezaki T., Fujita N.;
RT   "Whole genome shotgun sequence of Escherichia vulneris NBRC 102420.";
RL   Submitted (SEP-2014) 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:GAL60282.1}.
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DR   EMBL; BBMZ01000034; GAL60282.1; -; Genomic_DNA.
DR   RefSeq; WP_042395506.1; NZ_BBMZ01000034.1.
DR   EnsemblBacteria; GAL60282; GAL60282; EV102420_34_00190.
DR   Proteomes; UP000029462; 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; 3.30.70.2570; -; 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; TF_GTP-bd_dom.
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; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF54980; SSF54980; 2.
DR   TIGRFAMs; TIGR01393; lepA; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS00301; G_TR_1; 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:UP000029462};
KW   Elongation factor {ECO:0000313|EMBL:GAL60282.1};
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:UP000029462}.
FT   DOMAIN        2    184       Tr-type G. {ECO:0000259|PROSITE:PS51722}.
FT   NP_BIND      14     19       GTP. {ECO:0000256|HAMAP-Rule:MF_00071}.
FT   NP_BIND     131    134       GTP. {ECO:0000256|HAMAP-Rule:MF_00071}.
SQ   SEQUENCE   599 AA;  66357 MW;  63ADD2D276DB4A0B CRC64;
     MKNIRNFSII AHIDHGKSTL SDRIIQLCGG LSDREMEAQV LDSMDLERER GITIKAQSVT
     LDYKAADGET YQLNFIDTPG HVDFSYEVSR SLAACEGALL VVDAGQGVEA QTLANCYTAM
     EMDLEVVPVL NKIDLPAADP ERVAEEIEDI VGIDAADAVR CSAKTGVGVG DVLERLVRDI
     PPPQGDPEGP LQALIIDSWF DNYLGVVSLV RINNGTMRKG DKIKVMSTGQ TYNADRLGIF
     TPKQVDRTEL KCGEVGWLVC AIKDILGAPV GDTLTTARNP ADKALPGFKK VKPQVYAGLF
     PVSSDDYENF RDALGKLSLN DASLFYEPES STALGFGFRC GFLGLLHMEI IQERLEREYD
     LDLITTAPTV VYEVVTTSKE TVYVDSPSKL PPLNNIQELR EPIAECHMLL PQEYLGNVIT
     LCIEKRGVQT NMVYHGKQVA LTYEIPMAEV VLDFFDRLKS TSRGYASLDY NFKRFQASNM
     VRVDVLINGE RVDALALITH NDNAPYRGRE LVEKMKELIP RQQFDIAIQA AIGNHVIARS
     TVKQLRKNVL AKCYGGDVSR KKKLLQKQKD GKKRMKQVGN VELPQEAFLA ILHVGKDGK
//
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