ID A0A0G1IU99_9BACT Unreviewed; 578 AA.
AC A0A0G1IU99;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
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 ORFNames=UW55_C0008G0012 {ECO:0000313|EMBL:KKT62931.1};
OS Candidatus Giovannonibacteria bacterium GW2011_GWA2_44_26.
OC Bacteria; Candidatus Giovannonibacteria.
OX NCBI_TaxID=1618648 {ECO:0000313|EMBL:KKT62931.1, ECO:0000313|Proteomes:UP000033945};
RN [1] {ECO:0000313|EMBL:KKT62931.1, ECO:0000313|Proteomes:UP000033945}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {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:KKT62931.1}.
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DR EMBL; LCIT01000008; KKT62931.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1IU99; -.
DR PATRIC; fig|1618648.3.peg.583; -.
DR Proteomes; UP000033945; 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 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; IPR035647; EFG_III/V.
DR InterPro; IPR000640; EFG_V-like.
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; 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; 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:KKT62931.1};
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|HAMAP-Rule:MF_00071};
KW Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00071}.
FT DOMAIN 1..156
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT BINDING 103..106
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00071"
SQ SEQUENCE 578 AA; 65234 MW; 179B91E510B0AFDD CRC64;
MLEITGTVEK RKMREQFLDM HPLERERGIT IKMQPVRMHY KNYVLNLIDT PGHIDFNYEV
SRALAAVEGA ILLVDATQGV EAQTISNIEL ARSLNLKIIP IVNKIDLAQA RISETKEEIV
NLLGCGEEEI LEVSAKTGDG VENLLEEVVR RVPSPHSSTL GVEAPKTPSV FPRGDVRALI
FDFEYSIHRG VIAHARIFDG EIKKGLKLKL AEAKEIFTVG EVGIFKPELG VRDMLEAGEI
GYIVTGIKEA KIVRVGDTIL KESSNIAPLA GYKEIKPVVF SSIYPEDQDR FEDLRRALER
LKLVDSALFF EEESSGVLGR GFRCGFLGML HLEIVVERLI RDFGVKVIAA TPTVKYRVKT
KQGEAEVYSP HKFPDEHEIL EILEPYIKIE ILAPPEKLSG ILKLLGEHEV KIFFTTKFSE
SRIKIDGEMP LRELMRDFFD ALKSVSQGYA SLGYEFLDLR QADLVRLDVL VAEEIVPAFS
RIVSHARLEH EAEAAVEKLY NILPRALFSL KIQAKAHGRI LASRSLKAMS KDVTGHLYGG
DRSRKMKLWK KQKEGKKRLG VRADYNIPPE VYLKMIRK
//
