ID LEPA_YERPE Reviewed; 599 AA.
AC Q8ZD74; Q0WDH5;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 01-MAY-2013, entry version 91.
DE RecName: Full=Elongation factor 4;
DE Short=EF-4;
DE EC=3.6.5.n1;
DE AltName: Full=Ribosomal back-translocase LepA;
GN Name=lepA; OrderedLocusNames=YPO2716, y1295, YP_2520;
OS Yersinia pestis.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Yersinia.
OX NCBI_TaxID=632;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CO-92 / Biovar Orientalis;
RX PubMed=11586360; DOI=10.1038/35097083;
RA Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G.,
RA Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L.,
RA Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M.,
RA Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G.,
RA Feltwell T., Hamlin N., Holroyd S., Jagels K., Karlyshev A.V.,
RA Leather S., Moule S., Oyston P.C.F., Quail M.A., Rutherford K.M.,
RA Simmonds M., Skelton J., Stevens K., Whitehead S., Barrell B.G.;
RT "Genome sequence of Yersinia pestis, the causative agent of plague.";
RL Nature 413:523-527(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIM10+ / Biovar Mediaevalis;
RX PubMed=12142430; DOI=10.1128/JB.184.16.4601-4611.2002;
RA Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P.,
RA Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C.,
RA Fetherston J.D., Lindler L.E., Brubaker R.R., Plano G.V.,
RA Straley S.C., McDonough K.A., Nilles M.L., Matson J.S., Blattner F.R.,
RA Perry R.D.;
RT "Genome sequence of Yersinia pestis KIM.";
RL J. Bacteriol. 184:4601-4611(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=91001 / Biovar Mediaevalis;
RX PubMed=15368893; DOI=10.1093/dnares/11.3.179;
RA Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D.,
RA Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z.,
RA Jin L., Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J.,
RA Yang H., Wang J., Huang P., Yang R.;
RT "Complete genome sequence of Yersinia pestis strain 91001, an isolate
RT avirulent to humans.";
RL DNA Res. 11:179-197(2004).
CC -!- FUNCTION: Required for accurate and efficient protein synthesis
CC under certain stress conditions. May act as a fidelity factor of
CC the translation reaction, by catalyzing a one-codon backward
CC translocation of tRNAs on improperly translocated ribosomes. Back-
CC translocation proceeds from a post-translocation (POST) complex to
CC a pre-translocation (PRE) complex, thus giving elongation factor G
CC a second chance to translocate the tRNAs correctly. Binds to
CC ribosomes in a GTP-dependent manner (By similarity).
CC -!- CATALYTIC ACTIVITY: GTP + H(2)O = GDP + phosphate.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane
CC protein; Cytoplasmic side (By similarity).
CC -!- SIMILARITY: Belongs to the GTP-binding elongation factor family.
CC LepA subfamily.
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DR EMBL; AL590842; CAL21335.1; -; Genomic_DNA.
DR EMBL; AE009952; AAM84869.1; -; Genomic_DNA.
DR EMBL; AE017042; AAS62718.1; -; Genomic_DNA.
DR PIR; AD0331; AD0331.
DR RefSeq; NP_668618.1; NC_004088.1.
DR RefSeq; NP_993841.1; NC_005810.1.
DR RefSeq; YP_002347663.1; NC_003143.1.
DR ProteinModelPortal; Q8ZD74; -.
DR SMR; Q8ZD74; 1-555.
DR STRING; 214092.YPO2716; -.
DR PRIDE; Q8ZD74; -.
DR DNASU; 1146242; -.
DR EnsemblBacteria; AAM84869; AAM84869; y1295.
DR EnsemblBacteria; AAS62718; AAS62718; YP_2520.
DR GeneID; 1146242; -.
DR GeneID; 1175546; -.
DR GeneID; 2763941; -.
DR KEGG; ype:YPO2716; -.
DR KEGG; ypk:y1295; -.
DR KEGG; ypm:YP_2520; -.
DR eggNOG; COG0481; -.
DR HOGENOM; HOG000020624; -.
DR KO; K03596; -.
DR OMA; KCYGGDA; -.
DR ProtClustDB; PRK05433; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:HAMAP.
DR GO; GO:0003924; F:GTPase activity; IEA:HAMAP.
DR GO; GO:0043022; F:ribosome binding; IEA:HAMAP.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:HAMAP.
DR GO; GO:0006184; P:GTP catabolic process; IEA:GOC.
DR GO; GO:0045727; P:positive regulation of translation; IEA:HAMAP.
DR GO; GO:0006414; P:translational elongation; IEA:GOC.
DR Gene3D; 3.30.70.240; -; 1.
DR HAMAP; MF_00071; LepA; 1; -.
DR InterPro; IPR006297; EF-4.
DR InterPro; IPR000795; EF_GTP-bd_dom.
DR InterPro; IPR009022; EFG_III-V.
DR InterPro; IPR000640; EFG_V.
DR InterPro; IPR013842; LepA_GTP-bd_C.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR004161; Transl_elong_EFTu/EF1A_2.
DR InterPro; IPR009000; Transl_elong_init/rib_B-barrel.
DR PANTHER; PTHR23115:SF40; PTHR23115:SF40; 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; SSF54980; EFG_III_V; 2.
DR SUPFAM; SSF50447; Translat_factor; 1.
DR TIGRFAMs; TIGR01393; lepA; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS00301; EFACTOR_GTP; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Complete proteome; GTP-binding;
KW Hydrolase; Membrane; Nucleotide-binding; Protein biosynthesis;
KW Reference proteome.
FT CHAIN 1 599 Elongation factor 4.
FT /FTId=PRO_0000176381.
FT NP_BIND 14 19 GTP (By similarity).
FT NP_BIND 131 134 GTP (By similarity).
SQ SEQUENCE 599 AA; 66709 MW; BAF32CD792DB5BDB CRC64;
MKHIRNFSII AHIDHGKSTL SDRIIQICGG LSEREMAAQV LDSMDLERER GITIKAQSVT
LDYHSKDGQT YQLNFIDTPG HVDFSYEVSR SLAACEGALL VVDAGQGVEA QTLANCYTAM
EMDLEVVPVL NKIDLPAADP ERVAEEIEDI VGIDATDAIR CSAKTGVGVP DVLERLVRDI
PAPEGDPNGP LQALIIDSWF DNYLGVVSLI RIKNGSLRKG DKVKVMSTGQ SYNADRLGIF
TPKRVDRDVL NCGEVGWLVC AIKDILGAPV GDTLTLTRNP AEKSLPGFKK VKPQVYAGLF
PISSDDYESF RDALGKLSLN DASLFYEPES STALGFGFRC GFLGLLHMEI IQERLEREYD
LELITTAPTV VYEVITTNQE TVYVDSPSKL PALNNIEELR EPIAECHMLL PQEYLGNVIT
LCIEKRGTQT NMVYHGKQVA LTYEIPMAEV VLDFFDRLKS TSRGYASLDY NFKRFQTSDM
VRVDVLINNE RVDALALITH RDNAQYRGRD LVEKMKELIP RQQFDIAIQA AIGNHIIARS
TVKQLRKNVL AKCYGGDVSR KKKLLQKQKD GKKRMKQVGN VELPQEAFLA ILHVGKDSK
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