LEPA_XANOP
ID LEPA_XANOP Reviewed; 596 AA.
AC B2SRY0;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 86.
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=PXO_01714;
OS Xanthomonas oryzae pv. oryzae (strain PXO99A).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=360094;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PXO99A;
RX PubMed=18452608; DOI=10.1186/1471-2164-9-204;
RA Salzberg S.L., Sommer D.D., Schatz M.C., Phillippy A.M., Rabinowicz P.D.,
RA Tsuge S., Furutani A., Ochiai H., Delcher A.L., Kelley D., Madupu R.,
RA Puiu D., Radune D., Shumway M., Trapnell C., Aparna G., Jha G., Pandey A.,
RA Patil P.B., Ishihara H., Meyer D.F., Szurek B., Verdier V., Koebnik R.,
RA Dow J.M., Ryan R.P., Hirata H., Tsuyumu S., Won Lee S., Seo Y.-S.,
RA Sriariyanum M., Ronald P.C., Sonti R.V., Van Sluys M.-A., Leach J.E.,
RA White F.F., Bogdanove A.J.;
RT "Genome sequence and rapid evolution of the rice pathogen Xanthomonas
RT oryzae pv. oryzae PXO99A.";
RL BMC Genomics 9:204-204(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 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; CP000967; ACD59682.1; -; Genomic_DNA.
DR RefSeq; WP_012445254.1; NC_010717.2.
DR AlphaFoldDB; B2SRY0; -.
DR SMR; B2SRY0; -.
DR STRING; 360094.PXO_01714; -.
DR PRIDE; B2SRY0; -.
DR EnsemblBacteria; ACD59682; ACD59682; PXO_01714.
DR GeneID; 57848139; -.
DR KEGG; xop:PXO_01714; -.
DR eggNOG; COG0481; Bacteria.
DR HOGENOM; CLU_009995_3_3_6; -.
DR OMA; MVQIAIQ; -.
DR Proteomes; UP000001740; 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 inner membrane; Cell membrane; GTP-binding; Hydrolase; Membrane;
KW Nucleotide-binding; Protein biosynthesis.
FT CHAIN 1..596
FT /note="Elongation factor 4"
FT /id="PRO_1000117033"
FT DOMAIN 2..184
FT /note="tr-type G"
FT BINDING 14..19
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00071"
FT BINDING 131..134
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00071"
SQ SEQUENCE 596 AA; 65749 MW; 034481E072508D7D CRC64;
MRNIRNFSII AHVDHGKSTL ADRIIQLCGG LQAREMEAQV LDSNPIERER GITIKAQSVS
LPYTAKDGQV YHLNFIDTPG HVDFSYEVSR SLAACEGALL VVDAAQGVEA QSVANCYTAV
EQGLEVVPVL NKIDLPTADV DRAKAEIEAV IGIDAEDAVA VSAKTGLNID LVLEAIVHRI
PPPTPRDTDK LQALIIDSWF DNYLGVVSLV RVMQGEIKPG SKILVMSTGR THLVDKVGVF
TPKRKELSAL GAGEVGWINA SIKDVHGAPV GDTLTLAADP APHALPGFQE MQPRVFAGLF
PVDAEDYPDL REALDKLRLN DAALRFEPES SEAMGFGFRC GFLGMLHMEI VQERLEREYN
LNLISTAPTV VYEVLKTDGS VIPMDNPSKL PPLNNVEEIR EPIIRANILT PPDYVGNIIT
LCEEKRGSQI GINYLGSQVQ ISYELPMAEV VLDFFDKLKS VSRGYASLDY HFLRFDPGPF
VRVDTLINGD KVDALSIIVH RSYADRRGRE LCEKMKDLIP RQMFDVAIQA AVGSQIISRS
TVKAMRKNVL AKCYGGDVSR KKKLLEKQKE GKKRMKQVGR VEIPQEAFLA VLQMDK
