ID A0A0L0LKL5_9BACT Unreviewed; 599 AA.
AC A0A0L0LKL5;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 13-SEP-2023, entry version 30.
DE RecName: Full=Elongation factor 4 {ECO:0000256|HAMAP-Rule:MF_00071};
DE Short=EF-4 {ECO:0000256|HAMAP-Rule:MF_00071};
DE EC=3.6.5.n1 {ECO:0000256|HAMAP-Rule:MF_00071};
DE AltName: Full=Ribosomal back-translocase LepA {ECO:0000256|HAMAP-Rule:MF_00071};
GN Name=lepA {ECO:0000256|HAMAP-Rule:MF_00071,
GN ECO:0000313|EMBL:KND50653.1};
GN ORFNames=ABA06_04305 {ECO:0000313|EMBL:KND50653.1};
OS Parcubacteria bacterium C7867-001.
OC Bacteria; Candidatus Parcubacteria.
OX NCBI_TaxID=1659195 {ECO:0000313|EMBL:KND50653.1, ECO:0000313|Proteomes:UP000037027};
RN [1] {ECO:0000313|EMBL:KND50653.1, ECO:0000313|Proteomes:UP000037027}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C7867-001 {ECO:0000313|EMBL:KND50653.1};
RX PubMed=26257709; DOI=10.3389/fmicb.2015.00713;
RA Nelson W.C., Stegen J.C.;
RT "The reduced genomes of Parcubacteria (OD1) contain signatures of a
RT symbiotic lifestyle.";
RL Front. Microbiol. 6:713-713(2015).
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:0000256|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:0000256|HAMAP-Rule:MF_00071};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_00071};
CC Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_00071};
CC Cytoplasmic side {ECO:0000256|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:0000256|ARBA:ARBA00005454, ECO:0000256|HAMAP-Rule:MF_00071}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KND50653.1}.
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DR EMBL; LFCK01000004; KND50653.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L0LKL5; -.
DR STRING; 1659195.ABA06_04305; -.
DR PATRIC; fig|1659195.3.peg.834; -.
DR Proteomes; UP000037027; Unassembled WGS sequence.
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; cd01890; LepA; 1.
DR Gene3D; 3.30.70.240; -; 1.
DR Gene3D; 3.30.70.2570; Elongation factor 4, C-terminal domain; 1.
DR Gene3D; 3.30.70.870; Elongation Factor G (Translational Gtpase), domain 3; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR HAMAP; MF_00071; LepA; 1.
DR InterPro; IPR006297; EF-4.
DR InterPro; IPR041095; EFG_II.
DR InterPro; IPR035647; EFG_III/V.
DR InterPro; IPR000640; EFG_V-like.
DR InterPro; IPR031157; G_TR_CS.
DR InterPro; IPR038363; LepA_C_sf.
DR InterPro; IPR013842; LepA_CTD.
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 NCBIfam; TIGR01393; lepA; 1.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR43512:SF4; TRANSLATION FACTOR GUF1 HOMOLOG, CHLOROPLASTIC; 1.
DR PANTHER; PTHR43512; TRANSLATION FACTOR GUF1-RELATED; 1.
DR Pfam; PF00679; EFG_C; 1.
DR Pfam; PF14492; EFG_III; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF06421; LepA_C; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF54980; EF-G C-terminal domain-like; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50447; Translation proteins; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_00071};
KW Elongation factor {ECO:0000313|EMBL:KND50653.1};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW Rule:MF_00071};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00071};
KW Membrane {ECO:0000256|HAMAP-Rule:MF_00071};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00071}; Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00071}.
FT DOMAIN 3..185
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT BINDING 15..20
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00071"
FT BINDING 132..135
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00071"
SQ SEQUENCE 599 AA; 66356 MW; 6B942643EA9982D4 CRC64;
MTSQIRNFSI IAHIDHGKST LADRLLERTG TIEARKMRDQ VLDKMDLERE RGITIKMQPA
RMKYKANDGN EYILNLIDTP GHIDFAYEVS RALTAVEGVL LLVDSTQGVQ AQTLTTLSMA
RDAGCTIIPV ISKIDAPASR PEEVKAELAK LLSVSADSVL AVSGRTGAGV EELLQAIVDR
VPAPEKGGTE PRAGIFDFSY STHRGVAVYV RVFDGVFKKG DALTFSAAGK KFVSLDNGIF
TPDETPTESL SSGEIGYIVT GIKEPGVVAV GDTILSERGT LPPLAGFERP RPVVWASVYP
ESQDSLNDLK QALERLRLTD SSLSFEEESS GVLGRGFRCG FLGMLHLEIV TERLRREFTL
SLVVTIPTIE YVVTDTHGKR ERIYTPSKFP AFGDIESIEE PWAKIILITP PDSLSGLLQL
LHEHEANVGD THAYADGRIE LSAEMPLREL MRGFFDRVKN VSSGYASLSY ELLTERPADV
VRLDILVAEE EVPAFARVVS RRRVQEEGER MVEKLHGILP KQLMVTKIQA QALGRILSSR
TLSAMRKDVT GYLYGGDVSR KNKLLQKQKK GKKHRAQFSK NRVDIPEDVF MKMVQESER
//
