LEPA_MYCPU
ID LEPA_MYCPU Reviewed; 597 AA.
AC Q98QW3;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2004, sequence version 2.
DT 03-AUG-2022, entry version 120.
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=MYPU_2470;
OS Mycoplasmopsis pulmonis (strain UAB CTIP) (Mycoplasma pulmonis).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasmopsis.
OX NCBI_TaxID=272635;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAB CTIP;
RX PubMed=11353084; DOI=10.1093/nar/29.10.2145;
RA Chambaud I., Heilig R., Ferris S., Barbe V., Samson D., Galisson F.,
RA Moszer I., Dybvig K., Wroblewski H., Viari A., Rocha E.P.C., Blanchard A.;
RT "The complete genome sequence of the murine respiratory pathogen Mycoplasma
RT pulmonis.";
RL Nucleic Acids Res. 29:2145-2153(2001).
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=CAC13420.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AL445563; CAC13420.1; ALT_INIT; Genomic_DNA.
DR PIR; G90542; G90542.
DR RefSeq; WP_041363992.1; NC_002771.1.
DR AlphaFoldDB; Q98QW3; -.
DR SMR; Q98QW3; -.
DR STRING; 272635.MYPU_2470; -.
DR PRIDE; Q98QW3; -.
DR EnsemblBacteria; CAC13420; CAC13420; CAC13420.
DR KEGG; mpu:MYPU_2470; -.
DR eggNOG; COG0481; Bacteria.
DR HOGENOM; CLU_009995_3_3_14; -.
DR OrthoDB; 182107at2; -.
DR BioCyc; MPUL272635:G1GT6-248-MON; -.
DR Proteomes; UP000000528; 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 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 3: Inferred from homology;
KW Cell membrane; GTP-binding; Hydrolase; Membrane; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..597
FT /note="Elongation factor 4"
FT /id="PRO_0000176306"
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 597 AA; 67551 MW; 90B522ADC9BDBF4D CRC64;
MNKSKIRNFS IIAHIDHGKS TLADRILEIT QTVSTRELKA QHLDSMDLEQ ERGITIKLNA
VQIKYKDYIF HLIDTPGHVD FTYEVSRSLA ASEGALLLVD ATQGIEAQTL ANAYLALENN
LKIIPIINKI DLPSADPERI KGEIEEVIGI SAKDTILISA KSGLNVEKVL EEIVDKISYP
IDADDDKPLK ALVFDSYFDA YRGVILLVRI FEGKIAVNDQ FKFISTNKQF HVIELGVRTP
TEVKKPFLES GEVGWIAASI RDAKDVSVGD TLTLVKNPTK EALPGYKKVK AVVFTGFYPI
DGKDYPVLKE SLEKISLSDS SITWELESSK ALGFGFRVGF LGMLHMEVLQ ERLKREFNID
IIATAPSVEY KVYLTNNKVE IVSNPSDLPD RNYIKNIKEP FIRSFILVTE EFIGGIMELC
QSKRGVYVNI EYIDKRVKII YELPLSEIIL DFFDKLKSIS KGYASFDYEF IEYRDADLVK
VDILLNKEKV DAFSFISHRE NAYERSKELA LKLKDVIPKQ SFEIPIQAII GAKVIARETI
KAYRKDVTAK LYGGDVTRRQ KLLKKQKEGK KRMKSIGSVE VPQEAFLSVL KSNMDKK
