(data stored in ACNUC30630 zone)

SWISSPROT: LEPA_RHOPT

ID   LEPA_RHOPT              Reviewed;         603 AA.
AC   B3Q991;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   11-DEC-2019, entry version 71.
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=Rpal_0355;
OS   Rhodopseudomonas palustris (strain TIE-1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=395960;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TIE-1;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Emerson D.,
RA   Newman D.K., Roden E., Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris TIE-1.";
RL   Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
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}.
DR   EMBL; CP001096; ACE98915.1; -; Genomic_DNA.
DR   RefSeq; WP_011155920.1; NC_011004.1.
DR   SMR; B3Q991; -.
DR   EnsemblBacteria; ACE98915; ACE98915; Rpal_0355.
DR   GeneID; 41374762; -.
DR   KEGG; rpt:Rpal_0355; -.
DR   HOGENOM; HOG000020624; -.
DR   KO; K03596; -.
DR   OMA; KPMVFCG; -.
DR   OrthoDB; 182107at2; -.
DR   BioCyc; RPAL395960:RPAL_RS01775-MONOMER; -.
DR   Proteomes; UP000001725; 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; B3Q991.
DR   SWISS-2DPAGE; B3Q991.
KW   Cell inner membrane; Cell membrane; GTP-binding; Hydrolase; Membrane;
KW   Nucleotide-binding; Protein biosynthesis.
FT   CHAIN           1..603
FT                   /note="Elongation factor 4"
FT                   /id="PRO_1000092435"
FT   DOMAIN          7..191
FT                   /note="tr-type G"
FT   NP_BIND         19..24
FT                   /note="GTP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00071"
FT   NP_BIND         138..141
FT                   /note="GTP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00071"
SQ   SEQUENCE   603 AA;  66745 MW;  96C40653749C7DA6 CRC64;
     MTTAPIDNIR NFSIVAHIDH GKSTLADRLI QITGGMSDRE MAGKEQVLDS MDIERERGIT
     IKAQTVRLKY RAHDGKDYIF NLMDTPGHVD FAYEVSRSLA ACEGSLLVVD ASQGVEAQTL
     ANVYHALDAG HEIVPVLNKV DLPAAEPEKI KQQIEDVIGL DASDAVMISA KTGLGVPDVL
     EAIVTRLPPP KGDRDATLKA LLVDSWYDVY LGVVVLVRVV DGVLKKGQRI RMMGTGAAYD
     VERVGYFTPK MVNVEELGPG EVGFITAAIK EVADTRVGDT ITDDKKPVTD MLPGFKPAIP
     VVFCGLFPVD ADDFETLRAA MGKLRLNDAS FSFEMETSAA LGFGFRCGFL GLLHLEIIQE
     RLSREFDLDL IATAPSVIYK MKLTDGTEME IHNPVDMPDV VKIAEIEEPW IEATILTPDE
     YLGSVLKLCQ DRRGNQKELT YVGARAMVKY DLPLNEVVFD FYDRLKSVSK GYASFDYHLT
     DYKPADLVKM QILVNAEPVD ALSMLVHRTR AEGRGRAMVE KMKELIPPHM FQIPIQAAIG
     GKVIARETVR ALRKDVTAKC YGGDITRKRK LLEKQKEGKK KMRQFGKVDI PQEAFIAALK
     VDS
//

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