LEPA_PARXL
ID LEPA_PARXL Reviewed; 597 AA.
AC Q13VM6;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 100.
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=Bxeno_A3325;
GN ORFNames=Bxe_A1083;
OS Paraburkholderia xenovorans (strain LB400).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=266265;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LB400;
RX PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA Chain P.S.G., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M., Lao V.,
RA Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A., Marx C.J.,
RA Parnell J.J., Ramette A., Richardson P., Seeger M., Smith D., Spilker T.,
RA Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B., Tiedje J.M.;
RT "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp genome
RT shaped for versatility.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
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}.
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DR EMBL; CP000270; ABE31863.1; -; Genomic_DNA.
DR RefSeq; WP_011489386.1; NZ_CP008760.1.
DR AlphaFoldDB; Q13VM6; -.
DR SMR; Q13VM6; -.
DR STRING; 266265.Bxe_A1083; -.
DR EnsemblBacteria; ABE31863; ABE31863; Bxe_A1083.
DR KEGG; bxb:DR64_3246; -.
DR KEGG; bxe:Bxe_A1083; -.
DR PATRIC; fig|266265.5.peg.3491; -.
DR eggNOG; COG0481; Bacteria.
DR OMA; MVQIAIQ; -.
DR OrthoDB; 182107at2; -.
DR Proteomes; UP000001817; Chromosome 1.
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 Gene3D; 3.40.50.300; -; 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; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR PANTHER; PTHR43512; PTHR43512; 1.
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; GTP-binding; Hydrolase; Membrane;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..597
FT /note="Elongation factor 4"
FT /id="PRO_0000265645"
FT DOMAIN 2..184
FT /note="tr-type G"
FT BINDING 14..19
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00071"
FT BINDING 131..134
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00071"
SQ SEQUENCE 597 AA; 66051 MW; 5FEB2620703E7706 CRC64;
MDHIRNFSII AHIDHGKSTL ADRIIQICGG LSDREMESQV LDSMDLERER GITIKAQTAA
LTYKARDGQV YNLNMIDTPG HVDFSYEVSR SLSACEGALL VVDASQGVEA QTVANCYTAI
ELGVDVIPVL NKIDLPAANP ENAIAEIEDV IGIDATDATR CSAKTGLGVE DVLEALVAKV
PPPKGDPEAP LQALIIDSWF DNYVGVVMLV RIVNGTLRPK DKIRMMATGA QYPVEHIGVF
TPKSKNLESL SAGQVGFIIA GIKELAAAKV GDTVTLVNRP AAEPLPGFKE VKPQVFAGLY
PVEANQYDAL RDSLEKLKLN DASLMYEPEV SQALGFGFRC GFLGLLHMEI VQERLEREFD
MDLITTAPTV VYEVLQRDGT TIMVENPAKM PEPSKIEEVR EPIVTVNLYM PQDYVGSVIT
LCTQKRGTQI NMQYHGRQVQ LTYEIPMGEV VLDFFDRLKS ISRGYASMDY EFKEYRAADV
VKVDMLINGD KVDALSVIVH RSQSQYRGRE VASKMRELIP RQMYDVAIQA TIGANIIARE
NIKALRKNVL AKCYGGDISR KKKLLEKQKA GKKRMKQVGS VEIPQEAFLA ILRVEDK
