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LEPA_STAEQ
ID   LEPA_STAEQ              Reviewed;         607 AA.
AC   Q5HNW2;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 109.
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=SERP1152;
OS   Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176279;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35984 / RP62A;
RX   PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA   Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA   Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA   Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA   Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA   Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA   Fraser C.M.;
RT   "Insights on evolution of virulence and resistance from the complete genome
RT   analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT   a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT   strain.";
RL   J. Bacteriol. 187:2426-2438(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; CP000029; AAW54487.1; -; Genomic_DNA.
DR   RefSeq; WP_001831284.1; NC_002976.3.
DR   AlphaFoldDB; Q5HNW2; -.
DR   SMR; Q5HNW2; -.
DR   STRING; 176279.SERP1152; -.
DR   EnsemblBacteria; AAW54487; AAW54487; SERP1152.
DR   GeneID; 50018613; -.
DR   KEGG; ser:SERP1152; -.
DR   eggNOG; COG0481; Bacteria.
DR   HOGENOM; CLU_009995_3_3_9; -.
DR   OMA; MVQIAIQ; -.
DR   OrthoDB; 182107at2; -.
DR   Proteomes; UP000000531; 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; IPR041095; EFG_II.
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; PF14492; EFG_III; 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..607
FT                   /note="Elongation factor 4"
FT                   /id="PRO_0000176347"
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;  68275 MW;  DA714C861EBC589F CRC64;
     MDKQERYNRR ENIRNFSIIA HIDHGKSTLA DRILENTKSV ETREMQDQLL DSMDLERERG
     ITIKLNAVRL KYEAKDGETY TFHLIDTPGH VDFTYEVSRS LAACEGAILV VDAAQGIEAQ
     TLANVYLALD NDLELLPVVN KIDLPAAEPD RVKQELEDVI GIDQEDVVLA SAKSNIGIEE
     ILEKIVDVVP APDGDPEAPL KALIFDSEYD PYRGVISSIR IIDGVVKAGD RIKMMATGKE
     FEVTEVGINT PKQLPVEELT VGDVGYIIAS IKNVDDSRVG DTITLAERPA DKPLQGYKKM
     NPMVFCGLFP IDNKDYNDLR EALEKLQLND ASLEFEPESS QALGFGYRTG FLGMLHMEII
     QERIEREFGI ELIATAPSVI YQCILKDGSE VSVDNPAQMP ERDKIEHIYE PFVKATMMVP
     NDYVGAVMEL CQRKRGQFIN MDYLDDIRVN IVYEIPLSEV VFDFFDQLKS NTKGYASFDY
     EFIENKESNL VKMDILLNGD KVDALSFIVH RDFAYERGKA LVEKLKTLIP RQQFEVPVQA
     AIGQKIVART NIKSMGKNVL SKCYGGDISR KRKLLEKQKA GKAKMKAVGN VEIPQDAFLA
     VLKMDDE
 
 
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