(data stored in ACNUC7421 zone)

SWISSPROT: LEPA_RHOPS

ID   LEPA_RHOPS              Reviewed;         603 AA.
AC   Q13E78;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 2.
DT   08-MAY-2019, entry version 77.
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=RPD_0373;
OS   Rhodopseudomonas palustris (strain BisB5).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisB5;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Pelletier D.A., Kyrpides N.,
RA   Lykidis A., Oda Y., Harwood C.S., Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisB5.";
RL   Submitted (MAR-2006) 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:
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-
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   -!- SEQUENCE CAUTION:
CC       Sequence=ABE37611.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; CP000283; ABE37611.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_041805577.1; NC_007958.1.
DR   SMR; Q13E78; -.
DR   STRING; 316057.RPD_0373; -.
DR   PRIDE; Q13E78; -.
DR   EnsemblBacteria; ABE37611; ABE37611; RPD_0373.
DR   KEGG; rpd:RPD_0373; -.
DR   eggNOG; ENOG4105C4S; Bacteria.
DR   eggNOG; COG0481; LUCA.
DR   HOGENOM; HOG000020624; -.
DR   KO; K03596; -.
DR   OrthoDB; 182107at2; -.
DR   BioCyc; RPAL316057:RPD_RS01925-MONOMER; -.
DR   Proteomes; UP000001818; 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   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; TF_GTP-bd_dom.
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; 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;
DR   PRODOM; Q13E78.
DR   SWISS-2DPAGE; Q13E78.
KW   Cell inner membrane; Cell membrane; Complete proteome; GTP-binding;
KW   Hydrolase; Membrane; Nucleotide-binding; Protein biosynthesis.
FT   CHAIN         1    603       Elongation factor 4.
FT                                /FTId=PRO_0000265694.
FT   DOMAIN        7    191       tr-type G.
FT   NP_BIND      19     24       GTP. {ECO:0000255|HAMAP-Rule:MF_00071}.
FT   NP_BIND     138    141       GTP. {ECO:0000255|HAMAP-Rule:MF_00071}.
SQ   SEQUENCE   603 AA;  66646 MW;  FE53AE2C68E19660 CRC64;
     MTTVPIDNIR NFSIVAHIDH GKSTLADRLI QITGGMSDRE MAGKEQVLDS MDIERERGIT
     IKAQTVRLNY RAKDGKDYIF NLMDTPGHVD FAYEVSRSLA ACEGSLLVVD ASQGVEAQTL
     ANVYHALDAG HEIVPVLNKV DLPAAEPDKV KQQIEDVIGL DASDAVMISA KTGLGVPDVL
     EAIVTRLPPP KGDRGATLKA LLVDSWYDVY LGVVVLVRVV DGVMKKGQRI RMMGTGAAYD
     VERVGFFTPK MTAVDELGPG EIGFITAAIK EVADTRVGDT ITDDRKPITE MLPGFKPAIP
     VVFCGLFPVD ADDFETLRAA MGKLRLNDAS FSFEMETSAA LGFGFRCGFL GLLHLEIIQE
     RLSREFDLNL IATAPSVIYK MKLNDGSEIE IHNPVDMPDV VKIAEIEEPW IEATILTPDE
     YLGSVLKLCQ DRRGNQKELT YVGARAMVKY DLPLNEVVFD FYDRLKSVSK GYASFDYHLT
     DYKPADLVKM QILVNAEPVD ALSMLVHRTR AEGRGRAMVE KMKELIPPHM FVIPIQAAIG
     GKIIARETVR ALRKDVTAKC YGGDITRKRK LLEKQKEGKK KMRQFGKVDI PQEAFIAALK
     VDS
//

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