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Database: UniProt
Entry: A0A139JQX5_9MOLU
LinkDB: A0A139JQX5_9MOLU
Original site: A0A139JQX5_9MOLU 
ID   A0A139JQX5_9MOLU        Unreviewed;       606 AA.
AC   A0A139JQX5;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   05-DEC-2018, entry version 14.
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=AXA84_0168 {ECO:0000313|EMBL:KXT29352.1}, AXA84_0230
GN   {ECO:0000313|EMBL:KXT29244.1}, DH96_01185
GN   {ECO:0000313|EMBL:RAM57904.1};
OS   Candidatus Phytoplasma oryzae.
OC   Bacteria; Tenericutes; Mollicutes; Acholeplasmatales;
OC   Acholeplasmataceae; Candidatus Phytoplasma;
OC   16SrXI (Rice yellow dwarf group).
OX   NCBI_TaxID=203274 {ECO:0000313|EMBL:KXT29244.1, ECO:0000313|Proteomes:UP000070069};
RN   [1] {ECO:0000313|EMBL:RAM57904.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NGS-S10 {ECO:0000313|EMBL:RAM57904.1};
RA   Kawicha P., Dickinson M., Hodgetts J.;
RT   "Genome study of Napier grass stunt phytoplasma.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KXT29244.1, ECO:0000313|Proteomes:UP000070069}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mbita1 {ECO:0000313|EMBL:KXT29244.1};
RA   Fischer A., Santa-Cruz I., Wambua L., Olds C., Midega C.,
RA   Dickinson M., Kawicha P., Khan Z., Masiga D., Jores J., Bernd S.;
RT   "A draft genome sequence of Candidatus Phytoplasma oryzae strain
RT   Mbita1, the causative agent of Napier Grass stunt disease in Kenya.";
RL   Submitted (FEB-2016) 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:
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-
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:KXT29244.1}.
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DR   EMBL; LTBM01000005; KXT29244.1; -; Genomic_DNA.
DR   EMBL; LTBM01000002; KXT29352.1; -; Genomic_DNA.
DR   EMBL; JHUK01000002; RAM57904.1; -; Genomic_DNA.
DR   RefSeq; WP_066540136.1; NZ_LTBM01000005.1.
DR   EnsemblBacteria; KXT29244; KXT29244; AXA84_0230.
DR   EnsemblBacteria; KXT29352; KXT29352; AXA84_0168.
DR   PATRIC; fig|203274.3.peg.273; -.
DR   Proteomes; UP000070069; 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; 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; 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; 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:UP000070069};
KW   GTP-binding {ECO:0000256|HAMAP-Rule:MF_00071};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00071,
KW   ECO:0000313|EMBL:KXT29244.1};
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:UP000070069}.
FT   DOMAIN       11    193       Tr-type G. {ECO:0000259|PROSITE:PS51722}.
FT   NP_BIND      23     28       GTP. {ECO:0000256|HAMAP-Rule:MF_00071}.
FT   NP_BIND     140    143       GTP. {ECO:0000256|HAMAP-Rule:MF_00071}.
SQ   SEQUENCE   606 AA;  68862 MW;  84265A7155D8414C CRC64;
     MNFEEINKKK SKIRNFSIIA HIDHGKSTLA DRILEMTNTI EKRSMKSQYL DSMALERERG
     ITIKLNSVEI IYKSKNQIEY IMHLIDTPGH VDFNYEVSRS LAACEGVLLI VDSTQGIQAQ
     TLSNVNLALE NNLTIIPILN KIDLPYADVE KTKKEMKDIL GLDPDSIILA SGKTGFGVDK
     ILENIIEKIN PPDGDVQAPL QALIFDSIFD TYKGVIPSIR IMNGILKKGD KIRFIASRAI
     YEVMEVGIFN PKPTKRNFLS VGDVGYLSAF IKNIDDVQVG DTITLSRNNA VLPLPGYRKV
     NPVVFCGLYP VDSSKYSSLK SALQKLKLND SSLSYEIESS NFLGLGFRIG FLGLLHMEIT
     KERIVREFNI EVIITAPSVI FHVFTAHKKI IIDNLSKWPK NQSIEKIEEP YIRSFIKCPE
     IYVGDVMEIA QNKRGRLQDI QYLDNQKVML KYLLPFSEVI YNFFDKLKSA TKGYASFDYE
     MDKYYPSKLK KVDILLNSEI VDALSFIVYE DFAFNKAKNI CQKLKELIPQ QMFEIIIQAA
     IGKKVITRET IKSLRKNVID KCYGGDVSRK KKLLAKQKKG KKKMKNLGKV ILPQKAFLAI
     LSSYEK
//
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