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LEPA_STAA8
ID   LEPA_STAA8              Reviewed;         607 AA.
AC   Q2FXY7;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 101.
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};
GN   OrderedLocusNames=SAOUHSC_01688;
OS   Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 8325 / PS 47;
RA   Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT   "The Staphylococcus aureus NCTC 8325 genome.";
RL   (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL   Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL   D.C. (2006).
RN   [2]
RP   RIBOSOME-BINDING.
RX   PubMed=12690106; DOI=10.1074/jbc.m302109200;
RA   Colca J.R., McDonald W.G., Waldon D.J., Thomasco L.M., Gadwood R.C.,
RA   Lund E.T., Cavey G.S., Mathews W.R., Adams L.D., Cecil E.T., Pearson J.D.,
RA   Bock J.H., Mott J.E., Shinabarger D.L., Xiong L., Mankin A.S.;
RT   "Cross-linking in the living cell locates the site of action of
RT   oxazolidinone antibiotics.";
RL   J. Biol. Chem. 278:21972-21979(2003).
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; CP000253; ABD30762.1; -; Genomic_DNA.
DR   RefSeq; WP_000368341.1; NZ_LS483365.1.
DR   RefSeq; YP_500198.1; NC_007795.1.
DR   AlphaFoldDB; Q2FXY7; -.
DR   SMR; Q2FXY7; -.
DR   STRING; 1280.SAXN108_1610; -.
DR   EnsemblBacteria; ABD30762; ABD30762; SAOUHSC_01688.
DR   GeneID; 3921800; -.
DR   KEGG; sao:SAOUHSC_01688; -.
DR   PATRIC; fig|93061.5.peg.1537; -.
DR   eggNOG; COG0481; Bacteria.
DR   HOGENOM; CLU_009995_3_3_9; -.
DR   OMA; MVQIAIQ; -.
DR   PRO; PR:Q2FXY7; -.
DR   Proteomes; UP000008816; 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; IBA:GO_Central.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0045727; P:positive regulation of translation; IBA:GO_Central.
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   1: Evidence at protein level;
KW   Cell membrane; GTP-binding; Hydrolase; Membrane; Nucleotide-binding;
KW   Protein biosynthesis; Reference proteome.
FT   CHAIN           1..607
FT                   /note="Elongation factor 4"
FT                   /id="PRO_0000265708"
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   607 AA;  68175 MW;  9BCFFC5A06AAF6EB CRC64;
     MDNEQRLKRR ENIRNFSIIA HIDHGKSTLA DRILENTKSV ETRDMQDQLL DSMDLERERG
     ITIKLNAVRL KYEAKDGNTY TFHLIDTPGH VDFTYEVSRS LAACEGAILV VDAAQGIEAQ
     TLANVYLALD NELELLPVIN KIDLPAAEPE RVKQEIEDMI GLDQDDVVLA SAKSNIGIEE
     ILEKIVEVVP APDGDPEAPL KALIFDSEYD PYRGVISSIR IVDGVVKAGD KIRMMATGKE
     FEVTEVGINT PKQLPVDELT VGDVGYIIAS IKNVDDSRVG DTITLASRPA SEPLQGYKKM
     NPMVYCGLFP IDNKNYNDLR EALEKLQLND ASLEFEPESS QALGFGYRTG FLGMLHMEII
     QERIEREFGI ELIATAPSVI YQCVLRDGSE VTVDNPAQMP DRDKIDKIFE PYVRATMMVP
     NDYVGAVMEL CQRKRGQFIN MDYLDDIRVN IVYELPLAEV VFDFFDQLKS NTKGYASFDY
     EFIENKESNL VKMDILLNGD KVDALSFIVH RDFAYERGKA LVEKLKTLIP RQQFEVPVQA
     AIGQKIVART NIKSMGKNVL AKCYGGDISR KRKLLEKQKA GKAKMKAVGN VEIPQDAFLA
     VLKMDDE
 
 
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