LEPA_MESH2
ID LEPA_MESH2 Reviewed; 598 AA.
AC Q9ZHZ8; Q601X2;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 3.
DT 03-AUG-2022, entry version 129.
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=mhp079;
OS Mesomycoplasma hyopneumoniae (strain 232) (Mycoplasma hyopneumoniae).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mesomycoplasma.
OX NCBI_TaxID=295358;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=232;
RX PubMed=15489423; DOI=10.1128/jb.186.21.7123-7133.2004;
RA Minion F.C., Lefkowitz E.J., Madsen M.L., Cleary B.J., Swartzell S.M.,
RA Mahairas G.G.;
RT "The genome sequence of Mycoplasma hyopneumoniae strain 232, the agent of
RT swine mycoplasmosis.";
RL J. Bacteriol. 186:7123-7133(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-173.
RA Lin H.N., Shiuan D.;
RL Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC98966.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AE017332; AAV27401.1; -; Genomic_DNA.
DR EMBL; AF046228; AAC98966.1; ALT_FRAME; Genomic_DNA.
DR RefSeq; WP_011205917.1; NC_006360.1.
DR AlphaFoldDB; Q9ZHZ8; -.
DR SMR; Q9ZHZ8; -.
DR STRING; 295358.mhp079; -.
DR EnsemblBacteria; AAV27401; AAV27401; mhp079.
DR KEGG; mhy:mhp079; -.
DR eggNOG; COG0481; Bacteria.
DR HOGENOM; CLU_009995_3_3_14; -.
DR OMA; MVQIAIQ; -.
DR PhylomeDB; Q9ZHZ8; -.
DR Proteomes; UP000006822; 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_0000176299"
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"
FT CONFLICT 152
FT /note="A -> T (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 598 AA; 67341 MW; 695F3BF7DA26A499 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 YILAKIFLPE EFLGQIMGLC
QDKRGIYVDL EYIDDFRRRL IYKLPLVEVI FDFFDRLKSL SKGYASFEYE VIDYQVSKLQ
KLDILLNGQK IDALSMIVHK DFAYPKARDL TQKLKEIIPR HSFEVPVQAV IGSKVIARET
IKAYRKDVTA KLYGGDVTRR KKLLEKQKAG KKRMKSFGVV DVPQEAFLAI LKTNINEK
