(data stored in SCRATCH9089 zone)

SWISSPROT: LEPA_PASMU

ID   LEPA_PASMU              Reviewed;         598 AA.
AC   P57806;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   27-APR-2001, sequence version 1.
DT   11-DEC-2019, entry version 129.
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=PM0063;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
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; AE004439; AAK02147.1; -; Genomic_DNA.
DR   RefSeq; WP_005722312.1; NC_002663.1.
DR   SMR; P57806; -.
DR   PRIDE; P57806; -.
DR   EnsemblBacteria; AAK02147; AAK02147; PM0063.
DR   GeneID; 29388825; -.
DR   KEGG; pmu:PM0063; -.
DR   eggNOG; ENOG4105C4S; Bacteria.
DR   eggNOG; COG0481; LUCA.
DR   HOGENOM; HOG000020624; -.
DR   KO; K03596; -.
DR   OMA; KPMVFCG; -.
DR   BioCyc; PMUL272843:G1FZ8-67-MONOMER; -.
DR   Proteomes; UP000000809; 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; P57806.
DR   SWISS-2DPAGE; P57806.
KW   Cell inner membrane; Cell membrane; GTP-binding; Hydrolase; Membrane;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..598
FT                   /note="Elongation factor 4"
FT                   /id="PRO_0000176315"
FT   DOMAIN          2..184
FT                   /note="tr-type G"
FT   NP_BIND         14..19
FT                   /note="GTP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00071"
FT   NP_BIND         131..134
FT                   /note="GTP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00071"
SQ   SEQUENCE   598 AA;  66211 MW;  4D41723C2AEBFD10 CRC64;
     MKNIRNFSII AHIDHGKSTL SDRLIQTCGG LSDREMEAQV LDSMDLERER GITIKAQSVT
     LNYKAKDGET YQLNFIDTPG HVDFSYEVSR SLAACEGALL VVDAGQGVEA QTLANCYTAI
     EMNLEVVPIL NKIDLPAADP ERVAEEIEDI VGIDAMEAVR CSAKTGVGIE DVLEEIVHKI
     PAPEGDPNAP LQALIIDSWF DNYLGVVSLV RIKNGTLRKG DKIKVMSTGQ SYNVDRLGIF
     TPKQVDTTIL NCGEVGWVVC AIKDILGAPV GDTLTSHNNP ASSVLPGFKK VKPQVYAGLF
     PISSDDYEAF RDALGKLSLN DASLFYEPEN STALGFGFRC GFLGLLHMEI IQERLEREYD
     LDLITTAPTV VYEVEKTDGE VIYVDSPSKL PPLNNITEIR EPIAECNMLL PQTYLGNVIT
     LCVEKRGVQT NMVYHGNQVA LTYEIPMGEV VLDFFDRLKS TSRGYASLDY GFKRFQAADM
     VRVDIMINGE RVDALALIVH KDNAPYRGRE LVEKMRELIP RQQFDIAIQA AIGNHIIARS
     TVKQLRKNVL AKCYGGDVSR KKKLLQKQKE GKKRMKSLGN VEVPQEAFLA ILHVGKDK
//

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