(data stored in SCRATCH3701 zone)

SWISSPROT: LEPA_RICTY

ID   LEPA_RICTY              Reviewed;         600 AA.
AC   Q68X95;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   11-DEC-2019, entry version 93.
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=RT0266;
OS   Rickettsia typhi (strain ATCC VR-144 / Wilmington).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=257363;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-144 / Wilmington;
RX   PubMed=15317790; DOI=10.1128/jb.186.17.5842-5855.2004;
RA   McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E.,
RA   McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E.,
RA   Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A., Hong C.,
RA   Yu X.-J., Walker D.H., Weinstock G.M.;
RT   "Complete genome sequence of Rickettsia typhi and comparison with sequences
RT   of other Rickettsiae.";
RL   J. Bacteriol. 186:5842-5855(2004).
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; AE017197; AAU03747.1; -; Genomic_DNA.
DR   RefSeq; WP_011190732.1; NC_006142.1.
DR   SMR; Q68X95; -.
DR   STRING; 257363.RT0266; -.
DR   EnsemblBacteria; AAU03747; AAU03747; RT0266.
DR   KEGG; rty:RT0266; -.
DR   eggNOG; ENOG4105C4S; Bacteria.
DR   eggNOG; COG0481; LUCA.
DR   HOGENOM; HOG000020624; -.
DR   KO; K03596; -.
DR   OMA; KPMVFCG; -.
DR   OrthoDB; 182107at2; -.
DR   BioCyc; RTYP257363:G1G0L-271-MONOMER; -.
DR   Proteomes; UP000000604; 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   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; Q68X95.
DR   SWISS-2DPAGE; Q68X95.
KW   Cell inner membrane; Cell membrane; GTP-binding; Hydrolase; Membrane;
KW   Nucleotide-binding; Protein biosynthesis.
FT   CHAIN           1..600
FT                   /note="Elongation factor 4"
FT                   /id="PRO_0000176335"
FT   DOMAIN          5..187
FT                   /note="tr-type G"
FT   NP_BIND         17..22
FT                   /note="GTP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00071"
FT   NP_BIND         134..137
FT                   /note="GTP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00071"
SQ   SEQUENCE   600 AA;  67101 MW;  B512FBCEA0D96FAD CRC64;
     MNNQKYIRNF SIIAHIDHGK STLADRLIEH CGGLNAREMS QQVLDSMDIE KERGITIKAQ
     TVRLVYKAKN GNTYYLNLMD TPGHVDFSYE VSRSLAACEG SLLVVDSTQG VEAQTLANVY
     QAIANDHEIV PVLNKIDLAA SEPEHVKKQI EDIIGIDASE AVLISAKNGI GIDSVLEAII
     NKLPSPKESS TDTLKALLVD SWYDPYLGVV ILVRIIDGTL RKNMRVKMIG TNSVYTVEHV
     GFFTPKKHIS DVLYAGEIGF FTASIKRVSD CKVGDTITDE KKSCEQALPG FKPNIPVVFC
     GFYPTDSAEF EHLKDSLAKL RLNDASFEYE MESSSALGVG FRCGFLGLLH LEIIQERLSR
     EFNLDLITTA PSVIYKIYML DGESLEIHNP ADLPDLQKIA SMEEPWIKAT IMVPDEFIGT
     VLSLCKEKRG IQLDHSYISN RAKIVYKLPL NEIVYDFYDR LKSCSKGYAS FEWQMDVYEL
     SDLVNLRILV NGEVVDALST IVHRSRAEQR GRALCVRLKD LIPRQQIDIA IQASVGNRII
     ARETIKALRK DVLSKCYGGD ISRKRKLLEK QKAGKKKMRQ YGNIEIPQSA FIAALQIGGE
//

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