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LEPA_DEHM1
ID   LEPA_DEHM1              Reviewed;         605 AA.
AC   Q3Z864;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 105.
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=DET0859;
OS   Dehalococcoides mccartyi (strain ATCC BAA-2266 / KCTC 15142 / 195)
OS   (Dehalococcoides ethenogenes (strain 195)).
OC   Bacteria; Chloroflexi; Dehalococcoidia; Dehalococcoidales;
OC   Dehalococcoidaceae; Dehalococcoides.
OX   NCBI_TaxID=243164;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-2266 / KCTC 15142 / 195;
RX   PubMed=15637277; DOI=10.1126/science.1102226;
RA   Seshadri R., Adrian L., Fouts D.E., Eisen J.A., Phillippy A.M., Methe B.A.,
RA   Ward N.L., Nelson W.C., DeBoy R.T., Khouri H.M., Kolonay J.F., Dodson R.J.,
RA   Daugherty S.C., Brinkac L.M., Sullivan S.A., Madupu R., Nelson K.E.,
RA   Kang K.H., Impraim M., Tran K., Robinson J.M., Forberger H.A., Fraser C.M.,
RA   Zinder S.H., Heidelberg J.F.;
RT   "Genome sequence of the PCE-dechlorinating bacterium Dehalococcoides
RT   ethenogenes.";
RL   Science 307:105-108(2005).
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 membrane {ECO:0000255|HAMAP-Rule:MF_00071};
CC       Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_00071};
CC       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; CP000027; AAW39867.1; -; Genomic_DNA.
DR   RefSeq; WP_010936586.1; NC_002936.3.
DR   AlphaFoldDB; Q3Z864; -.
DR   SMR; Q3Z864; -.
DR   STRING; 243164.DET0859; -.
DR   EnsemblBacteria; AAW39867; AAW39867; DET0859.
DR   GeneID; 60794837; -.
DR   KEGG; det:DET0859; -.
DR   eggNOG; COG0481; Bacteria.
DR   HOGENOM; CLU_009995_3_3_0; -.
DR   OMA; MVQIAIQ; -.
DR   OrthoDB; 182107at2; -.
DR   Proteomes; UP000008289; Chromosome.
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; 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; PF06421; LepA_C; 1.
DR   PRINTS; PR00315; ELONGATNFCT.
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 membrane; GTP-binding; Hydrolase; Membrane; Nucleotide-binding;
KW   Protein biosynthesis; Reference proteome.
FT   CHAIN           1..605
FT                   /note="Elongation factor 4"
FT                   /id="PRO_0000224756"
FT   DOMAIN          4..186
FT                   /note="tr-type G"
FT   BINDING         16..21
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00071"
FT   BINDING         133..136
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00071"
SQ   SEQUENCE   605 AA;  66928 MW;  33FE1A242C82EB17 CRC64;
     MSQSATRNFC IIAHIDHGKS TLADRLIEMT GTLRHDEMCE QVMDSMELER ERGITIKAKA
     IRLRYLSKDS HEYRLNLIDT PGHVDFSYEV SRTIAACEGA ILVIDATQGI QAQTLANVYL
     AIEYNLEIIP VINKIDLPGA DIPRVMGEIK SVLGYDEDAV IQISAKLGLG VPELLEAIVA
     RVPAPKGDGK LPLRALIFDS HYDPYKGVVA YLRVADGNIN KGDDLRLMGQ GTEFKVLEAG
     YFAPAQVAAL RLDVGDVGYV ATGLKSVGEC RVGDTVTLQH GGAIQPLIGY HPAKAMVFAG
     IYPTQTDDYH ELREAMEKLS LNDASLSYEP ESSPLLGHGF RCGFLGLLHL DIIVERLERE
     FNLSLVVTSP GVSLTVTRTS GEVLTVVNPN EMPLPHEIAS IEEPWVSVVI ITPSKYIGTV
     MDLVRENYGV YKNTEYLGQL AMSELGQRVQ LHYDMPLRSI LTTFHDQLKS RTQGYASLDY
     EFVGYRIANL SKIDVLVNDV AVDAFSRIIP PDKAHEIGEA LVKKLKEMIP RQLYQVTLQA
     AIGSKIVARA DISAKRKDVI AKCYGGDITR KRKLLDKQKE GKKKMRQIGK VEVPKEAFLS
     VLKLQ
 
 
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