ID A0A0G1WMN7_9BACT Unreviewed; 760 AA.
AC A0A0G1WMN7;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 13-SEP-2023, 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=UY63_C0005G0038 {ECO:0000313|EMBL:KKW19855.1};
OS Parcubacteria group bacterium GW2011_GWA2_51_10.
OC Bacteria.
OX NCBI_TaxID=1618855 {ECO:0000313|EMBL:KKW19855.1, ECO:0000313|Proteomes:UP000034456};
RN [1] {ECO:0000313|EMBL:KKW19855.1, ECO:0000313|Proteomes:UP000034456}
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: 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:KKW19855.1}.
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DR EMBL; LCQS01000005; KKW19855.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1WMN7; -.
DR STRING; 1618855.UY63_C0005G0038; -.
DR PATRIC; fig|1618855.3.peg.260; -.
DR Proteomes; UP000034456; 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; 2.
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; IPR026350; GxxExxY.
DR InterPro; IPR038363; LepA_C_sf.
DR InterPro; IPR013842; LepA_CTD.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR NCBIfam; TIGR04256; GxxExxY; 1.
DR NCBIfam; TIGR01393; lepA; 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; 2.
DR Pfam; PF06421; LepA_C; 1.
DR Pfam; PF13366; PDDEXK_3; 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:KKW19855.1};
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..350
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 297..300
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00071"
SQ SEQUENCE 760 AA; 84884 MW; 94407499B5ED08F8 CRC64;
MSSNIRNFSI ISHIDHGKST LADRMLELTA TIAPREMHEQ VLDRMELERE RGITIKMAPV
RMLWHPHRRL TQNETQKDAE WIQGDDFLYK DLTYKIRGIF FDVRKKLGLG HKEQIYHNAL
EIEFKKNGLV FESKKNIPIL YDGNNIGLYQ PDFVVEGKVL IELKALPEIS RPQTEQLWSY
LKGCEYKVAL LVNYGSKDLE IKRIVYDKSR PSSSALSALS ALSLRESAGV SNQVEEYVLN
LIDTPGHVDF AYEVSRALSA VEGVVLLVDS TQGVEAQTLS VLSVAKNLGL EIIPVVSKID
APNARVSDIV SEVALLLNCP ESSILRASGK TGEGVAHILN TIVEKIPPPK STGAGVQALI
FDFGYSDHRG VIVYARVFGG KIAKGDSLRF CAAQTDFQAL EVGWLTPRET PSEVLHEGEI
GYIVTGIKKA GIASVGDTLT SVRNPSHALP GYSPPAPVIW ASVYPESQDD LVLLRQSLER
LRLSDSSLSY EEESSGIMGK GFRCGFLGML HLEIIIERLR REFALNLVVT MPTTVYRITH
TNGKVEDIYS PAHFPDEGTA KRVEELWSKV SVIAPPEYYG AISQLLYDHE AEIGETATLP
DGKMQVYADM PLRELMRGFF DKLKSVSSGF ASLSYELLGF RDADVVRLDV LVADEIVPAF
ARIVSRRRVQ HESEAIVKKL EELLPRQLFV LKIQAKAMGR IIAARRVSAL RKDVTGYLYG
GDITRKMKLL EKQKRGKKKM LARGKVDIPH DVFLRVIRDS
//