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Database: UniProt
Entry: B1YVM2
LinkDB: B1YVM2
Original site: B1YVM2 
ID   LEPA_BURA4              Reviewed;         597 AA.
AC   B1YVM2;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   01-OCT-2014, entry version 45.
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};
GN   OrderedLocusNames=BamMC406_1012;
OS   Burkholderia ambifaria (strain MC40-6).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=398577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC40-6;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L.,
RA   Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Lykidis A., Ramette A., Konstantinidis K., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Burkholderia ambifaria MC40-6.";
RL   Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000255|HAMAP-
CC       Rule:MF_00071}.
CC   -!- CATALYTIC ACTIVITY: GTP + H(2)O = GDP + phosphate.
CC       {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-
CC       Rule:MF_00071}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. LepA
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_00071}.
CC   -!- SIMILARITY: Contains 1 tr-type G (guanine nucleotide-binding)
CC       domain. {ECO:0000305}.
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DR   EMBL; CP001025; ACB63503.1; -; Genomic_DNA.
DR   RefSeq; YP_001807719.1; NC_010551.1.
DR   ProteinModelPortal; B1YVM2; -.
DR   SMR; B1YVM2; 1-555.
DR   STRING; 398577.BamMC406_1012; -.
DR   EnsemblBacteria; ACB63503; ACB63503; BamMC406_1012.
DR   GeneID; 6176592; -.
DR   KEGG; bac:BamMC406_1012; -.
DR   PATRIC; 19031388; VBIBurAmb82852_1032.
DR   eggNOG; COG0481; -.
DR   HOGENOM; HOG000020624; -.
DR   KO; K03596; -.
DR   OMA; CYTALEM; -.
DR   OrthoDB; EOG6ZKXQ4; -.
DR   BioCyc; BAMB398577:GH38-1045-MONOMER; -.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0043022; F:ribosome binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0045727; P:positive regulation of translation; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.30.70.240; -; 1.
DR   Gene3D; 3.40.50.300; -; 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; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR009000; Transl_B-barrel.
DR   InterPro; IPR004161; Transl_elong_EFTu/EF1A_2.
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; Complete proteome; GTP-binding;
KW   Hydrolase; Membrane; Nucleotide-binding; Protein biosynthesis.
FT   CHAIN         1    597       Elongation factor 4.
FT                                /FTId=PRO_1000092376.
FT   DOMAIN        2    184       tr-type G.
FT   NP_BIND      14     19       GTP. {ECO:0000255|HAMAP-Rule:MF_00071}.
FT   NP_BIND     131    134       GTP. {ECO:0000255|HAMAP-Rule:MF_00071}.
SQ   SEQUENCE   597 AA;  65967 MW;  8057DBD946165925 CRC64;
     MDHIRNFSII AHIDHGKSTL ADRIIQVCGG LADREMEAQV LDSMDIERER GITIKAQTAA
     LSYRARDGKV YNLNLIDTPG HVDFSYEVSR SLSACEGALL VVDASQGVEA QTVANCYTAI
     ELGVEVVPVL NKIDLPAANP ENAIEEIEDV IGIDATDATR CSAKTGLGVE DVLESLIAKV
     PPPKGDPAAP LQALIIDSWF DNYVGVVMLV RIVNGTLRPK EKIKMMATGA QYPVEHVGVF
     TPKSRNLESL SAGQVGFIIA GIKELTAAKV GDTVTHVAKA ASEPLPGFKE VKPQVFAGLY
     PVEANQYDAL RESLEKLKLN DASLQYEPEV SQALGFGFRC GFLGLLHMEI VQERLEREFD
     MDLITTAPTV VYEVVQSDGS TIMVENPAKM PEPGRIAEVR EPIVTVNLYM PQDYVGSVIT
     LCEQKRGSQI NMQYHGRQVQ LTYEIPMAEI VLDFFDRLKS VSRGYASMDY EFKEYRSSDV
     VKVDMLINGD KVDALSIIVH RSQSQYRGRE VAAKMREIIP RQMYDVAIQA AIGAHIVARE
     NIKALRKNVL AKCYGGDITR KKKLLEKQKE GKKRMKQVGS VEIPQEAFLA ILRVEDK
//
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