LEPA_PHYMT
ID LEPA_PHYMT Reviewed; 605 AA.
AC B3QZT9;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 79.
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=ATP_00289;
OS Phytoplasma mali (strain AT).
OC Bacteria; Tenericutes; Mollicutes; Acholeplasmatales; Acholeplasmataceae;
OC Candidatus Phytoplasma; 16SrX (Apple proliferation group).
OX NCBI_TaxID=482235;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AT;
RX PubMed=18582369; DOI=10.1186/1471-2164-9-306;
RA Kube M., Schneider B., Kuhl H., Dandekar T., Heitmann K., Migdoll A.M.,
RA Reinhardt R., Seemueller E.;
RT "The linear chromosome of the plant-pathogenic mycoplasma 'Candidatus
RT Phytoplasma mali'.";
RL BMC Genomics 9:306-306(2008).
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; CU469464; CAP18476.1; -; Genomic_DNA.
DR AlphaFoldDB; B3QZT9; -.
DR SMR; B3QZT9; -.
DR STRING; 37692.ATP_00289; -.
DR EnsemblBacteria; CAP18476; CAP18476; ATP_00289.
DR KEGG; pml:ATP_00289; -.
DR eggNOG; COG0481; Bacteria.
DR HOGENOM; CLU_009995_3_3_14; -.
DR OMA; MVQIAIQ; -.
DR Proteomes; UP000002020; 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; 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 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; PF03144; GTP_EFTU_D2; 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..605
FT /note="Elongation factor 4"
FT /id="PRO_1000190822"
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 605 AA; 68533 MW; 90E02DA66C550DDA CRC64;
MQIKKINNKQ KRIRNFSIIA HVDHGKSTLA DRILEITNTV EKRLMQKQFL DSMDLEKERG
ITIKLNAVQI IFNDKKGDEY IMHLIDTPGH VDFNYEVSRA LAACEGVILV IDATQGIQAQ
TLTNFYLAIE NNLLIIPVIN KIDLPNADVN KVRREIKDTL GIEPENTILV SGKTGVGVTE
ILEKVVSNIP SPRGDINEPF QSLVFDSFFD PYKGVVSLIR VFSGKIQKGD QIRFMSNNEV
YEVSEVGVYS PFQTPKPFLF VGEVGYLSAS IKNIDKVRVG DTITNHKNPT KQRLPGYRKI
QPVVFCGLYP ITCSKYETLK SALEKLKLND ASLTFEPETS VALGLGFRIG FLGLLHMEII
QERISREFDI EAITTAPSVI YHVYTKKGTK ILVDNPSKWP NTQIIERVEE PFIKATIICP
QIYIGTVMTL SQSKRGQLKD ISYLDKNIAM IIYFFPLSEI MYNYFDKLKS VTKGYASFEY
EIDSYRSSSL QKMDILLNGE VIDALSIIIH KDFAYSRGKV ICSKLIECIP KQMFEVPIQV
AIGKRVIVRE NIKSMRKDVI SKCYGGDVSR KKKLLSKQKE GKKKMKNLGK VKLPQKAFLA
ILSTE
