ID   LEPA_MESH7              Reviewed;         598 AA.
AC   Q4A8T9;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 106.
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=MHP7448_0073;
OS   Mesomycoplasma hyopneumoniae (strain 7448) (Mycoplasma hyopneumoniae).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mesomycoplasma.
OX   NCBI_TaxID=262722;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=7448;
RX   PubMed=16077101; DOI=10.1128/jb.187.16.5568-5577.2005;
RA   Vasconcelos A.T.R., Ferreira H.B., Bizarro C.V., Bonatto S.L.,
RA   Carvalho M.O., Pinto P.M., Almeida D.F., Almeida L.G.P., Almeida R.,
RA   Alves-Junior L., Assuncao E.N., Azevedo V.A.C., Bogo M.R., Brigido M.M.,
RA   Brocchi M., Burity H.A., Camargo A.A., Camargo S.S., Carepo M.S.,
RA   Carraro D.M., de Mattos Cascardo J.C., Castro L.A., Cavalcanti G.,
RA   Chemale G., Collevatti R.G., Cunha C.W., Dallagiovanna B., Dambros B.P.,
RA   Dellagostin O.A., Falcao C., Fantinatti-Garboggini F., Felipe M.S.S.,
RA   Fiorentin L., Franco G.R., Freitas N.S.A., Frias D., Grangeiro T.B.,
RA   Grisard E.C., Guimaraes C.T., Hungria M., Jardim S.N., Krieger M.A.,
RA   Laurino J.P., Lima L.F.A., Lopes M.I., Loreto E.L.S., Madeira H.M.F.,
RA   Manfio G.P., Maranhao A.Q., Martinkovics C.T., Medeiros S.R.B.,
RA   Moreira M.A.M., Neiva M., Ramalho-Neto C.E., Nicolas M.F., Oliveira S.C.,
RA   Paixao R.F.C., Pedrosa F.O., Pena S.D.J., Pereira M., Pereira-Ferrari L.,
RA   Piffer I., Pinto L.S., Potrich D.P., Salim A.C.M., Santos F.R., Schmitt R.,
RA   Schneider M.P.C., Schrank A., Schrank I.S., Schuck A.F., Seuanez H.N.,
RA   Silva D.W., Silva R., Silva S.C., Soares C.M.A., Souza K.R.L., Souza R.C.,
RA   Staats C.C., Steffens M.B.R., Teixeira S.M.R., Urmenyi T.P.,
RA   Vainstein M.H., Zuccherato L.W., Simpson A.J.G., Zaha A.;
RT   "Swine and poultry pathogens: the complete genome sequences of two strains
RT   of Mycoplasma hyopneumoniae and a strain of Mycoplasma synoviae.";
RL   J. Bacteriol. 187:5568-5577(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; AE017244; AAZ53450.1; -; Genomic_DNA.
DR   RefSeq; WP_011289989.1; NC_007332.1.
DR   AlphaFoldDB; Q4A8T9; -.
DR   SMR; Q4A8T9; -.
DR   EnsemblBacteria; AAZ53450; AAZ53450; MHP7448_0073.
DR   KEGG; mhp:MHP7448_0073; -.
DR   HOGENOM; CLU_009995_3_3_14; -.
DR   OMA; MVQIAIQ; -.
DR   OrthoDB; 182107at2; -.
DR   Proteomes; UP000000553; 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.
FT   CHAIN           1..598
FT                   /note="Elongation factor 4"
FT                   /id="PRO_0000224774"
FT   DOMAIN          4..181
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         128..131
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00071"
SQ   SEQUENCE   598 AA;  67311 MW;  50ED3C96528F8503 CRC64;
     MDNKKIRNFA IIAHIDHGKS TLADRILEFT NTVSKRDLKE QHLDSMDLEK ERGITIKLNA
     VQIRYNSYIF HLIDTPGHVD FTYEVSRSLA ATEGALLLVD ASQGIQAQTL ANVYLALENN
     LEIIPIINKI DLPSANVDKV KAEIENTIGI SAENAILISA KNGIGIEKVL EAIVNLIPPP
     QASDEKDPLK ALVFDSYFDI YRGVIIFIRV VTGKISVGDT FKFMANNLKF SVIELGISSP
     NQVKKEALFA GEVGWVAASI RNAKDVEVGD TITLVENPAK SPLPGYKKLV PVMYTGFYPV
     DSQQYNLLKD SLEKISLSDS SIIYEPESSK ALGFGFRIGF LGLLHMEILQ ERLEREFNLS
     IIATAPSVEF QITRTNGQVQ IISNPSLFPE PNFISEIREP FILAKIFLPE EFLGQIMGLC
     QDKRGIYVDL EYIDDFRRRL IYKLPLVEVI FDFFDRLKSL SKGYASFEYE VIDYQVSKLQ
     KLDILLNGQK IDALSMIVHK DFAYPKARDL TQKLKEIIPR HSFEVPVQAV IGSKVIARET
     IKAYRKDVTA KLYGGDVTRR KKLLEKQKAG KKRMKSFGVV DVPQEAFLAI LKTNVNEK