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LEPA1_LACPL
ID   LEPA1_LACPL             Reviewed;         611 AA.
AC   Q88VN0; F9UPX4;
DT   19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Elongation factor 4 1 {ECO:0000255|HAMAP-Rule:MF_00071};
DE            Short=EF-4 1 {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 1 {ECO:0000255|HAMAP-Rule:MF_00071};
GN   Name=lepA1 {ECO:0000255|HAMAP-Rule:MF_00071}; OrderedLocusNames=lp_2015;
OS   Lactiplantibacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)
OS   (Lactobacillus plantarum).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactiplantibacillus.
OX   NCBI_TaxID=220668;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1;
RX   PubMed=12566566; DOI=10.1073/pnas.0337704100;
RA   Kleerebezem M., Boekhorst J., van Kranenburg R., Molenaar D., Kuipers O.P.,
RA   Leer R., Tarchini R., Peters S.A., Sandbrink H.M., Fiers M.W.E.J.,
RA   Stiekema W., Klein Lankhorst R.M., Bron P.A., Hoffer S.M.,
RA   Nierop Groot M.N., Kerkhoven R., De Vries M., Ursing B., De Vos W.M.,
RA   Siezen R.J.;
RT   "Complete genome sequence of Lactobacillus plantarum WCFS1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:1990-1995(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1;
RX   PubMed=22156394; DOI=10.1128/jb.06275-11;
RA   Siezen R.J., Francke C., Renckens B., Boekhorst J., Wels M.,
RA   Kleerebezem M., van Hijum S.A.;
RT   "Complete resequencing and reannotation of the Lactobacillus plantarum
RT   WCFS1 genome.";
RL   J. Bacteriol. 194:195-196(2012).
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; AL935263; CCC79263.1; -; Genomic_DNA.
DR   RefSeq; WP_003640703.1; NC_004567.2.
DR   RefSeq; YP_004889777.1; NC_004567.2.
DR   AlphaFoldDB; Q88VN0; -.
DR   SMR; Q88VN0; -.
DR   STRING; 220668.lp_2015; -.
DR   EnsemblBacteria; CCC79263; CCC79263; lp_2015.
DR   GeneID; 57025571; -.
DR   GeneID; 66449798; -.
DR   KEGG; lpl:lp_2015; -.
DR   PATRIC; fig|220668.9.peg.1702; -.
DR   eggNOG; COG0481; Bacteria.
DR   HOGENOM; CLU_009995_3_3_9; -.
DR   OMA; MVQIAIQ; -.
DR   PhylomeDB; Q88VN0; -.
DR   BioCyc; LPLA220668:G1GW0-1725-MON; -.
DR   Proteomes; UP000000432; 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; 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   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; 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..611
FT                   /note="Elongation factor 4 1"
FT                   /id="PRO_0000176286"
FT   DOMAIN          11..193
FT                   /note="tr-type G"
FT   BINDING         23..28
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00071"
FT   BINDING         140..143
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00071"
SQ   SEQUENCE   611 AA;  68345 MW;  34A20EC7AF339D33 CRC64;
     MDKATMQDRQ QHIRNFSIVA HIDHGKSTLA DRILELTDTI SKREMQDQVL DSMDLERERG
     ITIKLNAVEL HYQAKDGETY IFHLIDTPGH VDFTYEVSRS LAACEGAVLV VDAAQGVEAQ
     TLANVYLAID DDLEIVPVIN KIDLPSAEPE KVRKEIEDDI GIDAEDAVLA SAKAGIGIED
     LLEQIVHKIP APQGDLDAPL KALVFDSVYD DYRGVVLSVR IHEGIVRPGD RIRLMNSGSE
     YEVTEVGVNS PKPLARDYLM AGDVGYITAS IKDIQDTRVG DTVTNAKNPA EKPLAGYREM
     NPMVYAGIYP TDNAKFTDLR EALEKLKLND AALEFEAESS QALGFGFRCG FLGLLHMDVI
     QERLEREFNL ELITTAPSVT YHVRMTDGTE KKVENPAEMP EASAIKEIRE PYVKAQIMVP
     NDYVGAVMEL AQRKRGEFDT MEYLDSNRVN VVYHIPLSEI IFDFFDKLKS NTRGYASLDY
     DLDGYRASDL VKIDILLNGD QVDALSFIAH RDFAPARGRE IAAKLKTIIP RQNFEIPVQA
     TIGSKVIART NIKAYRKDVT AHLYGGDRTR RMKLLEKQKA GKKRMKAVGK VEIPQEAFMA
     VLKTDEDEKP N
 
 
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