LEPA_POLNS
ID LEPA_POLNS Reviewed; 601 AA.
AC B1XTL2;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 82.
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}; OrderedLocusNames=Pnec_0411;
OS Polynucleobacter necessarius subsp. necessarius (strain STIR1).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Polynucleobacter.
OX NCBI_TaxID=452638;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=STIR1;
RX PubMed=24167248; DOI=10.1073/pnas.1316687110;
RA Boscaro V., Felletti M., Vannini C., Ackerman M.S., Chain P.S.,
RA Malfatti S., Vergez L.M., Shin M., Doak T.G., Lynch M., Petroni G.;
RT "Polynucleobacter necessarius, a model for genome reduction in both free-
RT living and symbiotic bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:18590-18595(2013).
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 + 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: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}.
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DR EMBL; CP001010; ACB43689.1; -; Genomic_DNA.
DR RefSeq; WP_012357456.1; NC_010531.1.
DR AlphaFoldDB; B1XTL2; -.
DR SMR; B1XTL2; -.
DR STRING; 452638.Pnec_0411; -.
DR EnsemblBacteria; ACB43689; ACB43689; Pnec_0411.
DR KEGG; pne:Pnec_0411; -.
DR eggNOG; COG0481; Bacteria.
DR HOGENOM; CLU_009995_3_3_4; -.
DR OMA; MVQIAIQ; -.
DR OrthoDB; 182107at2; -.
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 Gene3D; 3.40.50.300; -; 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; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR PANTHER; PTHR43512; PTHR43512; 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; SSF50447; SSF50447; 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 inner membrane; Cell membrane; GTP-binding; Hydrolase; Membrane;
KW Nucleotide-binding; Protein biosynthesis.
FT CHAIN 1..601
FT /note="Elongation factor 4"
FT /id="PRO_1000092424"
FT DOMAIN 2..184
FT /note="tr-type G"
FT BINDING 14..19
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00071"
FT BINDING 131..134
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00071"
SQ SEQUENCE 601 AA; 66094 MW; 4C41FFCA086FF096 CRC64;
MDLIRNFSII AHIDHGKSTL ADRIIQLCGG LSDREMEAQV LDSMDIERER GITIKAQTAA
LNYKAKDGKI YNINLIDTPG HVDFSYEVSR SLSACEGALL VVDASQGVEA QTVANCYMAL
GLGVEVVPVL NKIDLPQADP ERAKKEIEDV IGIDASEAVT CSAKTGLGVA DVIEEMIARV
PPPTGNAEDP LQALIIDSWF DNYVGVVMLV RIVNGTLKPK DKITLMANGS SHLVEHVGVF
SPKSVDRPEL SAGQVGFVIA GIKELKAAKV GDTVTHSPGQ QGRVPASEPL PGFKEVKPQV
FAGLYPVESS EYDQLRESLE KLQLNDAALL YEPEVSQALG FGFRCGFLGL LHMEIVQERL
ERQYGMNLIT TAPTVVYQVE QSSGSIISVD NPSKMPEASK INTILEPIVT VNLYMPQEYV
GSIITLCVGK RGIQMDMNYL GRQVKLTYEL PMAEIVLDFF DKMKSISRGY ASMDYEFKEY
RPADVVKVDI LINGERVDAL SVIVHRSNSQ SRGREVVAKM RDIIPRQMFD VAIQAAIGSN
IVARENVKAL RKNVLAKCYG GDISRKRKLL EKQKEGKKRM KQVGNVEIPQ EAFLAILQVE
D
