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LEPA_EHRCJ
ID   LEPA_EHRCJ              Reviewed;         598 AA.
AC   Q3YSC2;
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=Ecaj_0340;
OS   Ehrlichia canis (strain Jake).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Ehrlichia.
OX   NCBI_TaxID=269484;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Jake;
RX   PubMed=16707693; DOI=10.1128/jb.01837-05;
RA   Mavromatis K., Doyle C.K., Lykidis A., Ivanova N., Francino M.P., Chain P.,
RA   Shin M., Malfatti S., Larimer F., Copeland A., Detter J.C., Land M.,
RA   Richardson P.M., Yu X.J., Walker D.H., McBride J.W., Kyrpides N.C.;
RT   "The genome of the obligately intracellular bacterium Ehrlichia canis
RT   reveals themes of complex membrane structure and immune evasion
RT   strategies.";
RL   J. Bacteriol. 188:4015-4023(2006).
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; CP000107; AAZ68383.1; -; Genomic_DNA.
DR   RefSeq; WP_011304461.1; NC_007354.1.
DR   AlphaFoldDB; Q3YSC2; -.
DR   SMR; Q3YSC2; -.
DR   STRING; 269484.Ecaj_0340; -.
DR   EnsemblBacteria; AAZ68383; AAZ68383; Ecaj_0340.
DR   KEGG; ecn:Ecaj_0340; -.
DR   eggNOG; COG0481; Bacteria.
DR   HOGENOM; CLU_009995_3_3_5; -.
DR   OMA; MVQIAIQ; -.
DR   OrthoDB; 182107at2; -.
DR   Proteomes; UP000000435; 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   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; Reference proteome.
FT   CHAIN           1..598
FT                   /note="Elongation factor 4"
FT                   /id="PRO_0000224759"
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   598 AA;  66867 MW;  34D6AEE26F4893EE CRC64;
     MDESNIRNFA IIAHIDHGKS TLADRLIEEC NGLDKREMKD QVLDSMDIER ERGITIKAQT
     VRLVYKAKDG QTYYLNLMDT PGHVDFSYEV SRSLAACEGS LLVVDSSQGV EAQTLANVYK
     AIDSDHEIIP VLNKIDLASS DPEKVKLQIE DMIGIDASES LLVSAKSGVG IQDVLEAIVS
     KLPSPCGKSD SPLKAILVDT WYDTYLGIVI LLRIKDGVIK KGMKIVMMSN NAVYQVDNVG
     IFTPHKKIVD QLSVGEIGFI TASIKELSDC KIGDTITEEQ RRCDAPLPGF RTSHPVVFCS
     IFPNEAGEFD RLREALKKLQ LNDASFTFEI EVSNALGYGF RCGFLGMLHL EVIQERLERE
     FNLDLTATAP GVIYKVTTKS GEIREVHNPH DFGETQDIAN IKEPWICATI MVPDQYLGVI
     MSLCNNKRGE KLDLSYSGNT ALLKYRLPLS EVVFDFYDRI KSLSKGYASL DWEMDEYLDS
     EIAKLSILIN SEPVDALACI IHKSKVEQRG REICLRLKDL IPRQQYKIAI QAAIGGRIIA
     RETISPYRKD VTAKLYGGDV TRRMKLLEKQ KKGKKKLRSI GNVNVPHNAF IQALKIID
 
 
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