ID V6J0P0_9BACL Unreviewed; 607 AA.
AC V6J0P0;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
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=P343_00935 {ECO:0000313|EMBL:EST13380.1};
OS Sporolactobacillus laevolacticus DSM 442.
OC Bacteria; Bacillota; Bacilli; Bacillales; Sporolactobacillaceae;
OC Sporolactobacillus.
OX NCBI_TaxID=1395513 {ECO:0000313|EMBL:EST13380.1, ECO:0000313|Proteomes:UP000018296};
RN [1] {ECO:0000313|EMBL:EST13380.1, ECO:0000313|Proteomes:UP000018296}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 442 {ECO:0000313|EMBL:EST13380.1,
RC ECO:0000313|Proteomes:UP000018296};
RX PubMed=24371202;
RA Wang H., Wang L., Ju J., Yu B., Ma Y.;
RT "Genome Sequence of Sporolactobacillus laevolacticus DSM442, an Efficient
RT Polymer-Grade D-Lactate Producer from Agricultural Waste Cottonseed as a
RT Nitrogen Source.";
RL Genome Announc. 1:e01100-13(2013).
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:EST13380.1}.
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DR EMBL; AWTC01000001; EST13380.1; -; Genomic_DNA.
DR RefSeq; WP_023508506.1; NZ_AWTC01000001.1.
DR AlphaFoldDB; V6J0P0; -.
DR STRING; 1395513.P343_00935; -.
DR PATRIC; fig|1395513.3.peg.186; -.
DR eggNOG; COG0481; Bacteria.
DR OrthoDB; 9801591at2; -.
DR Proteomes; UP000018296; 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; cd03699; EF4_II; 1.
DR CDD; cd16260; EF4_III; 1.
DR CDD; cd01890; LepA; 1.
DR CDD; cd03709; lepA_C; 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; 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 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; PF03144; GTP_EFTU_D2; 1.
DR Pfam; PF06421; LepA_C; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SMART; SM00838; EFG_C; 1.
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 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|ARBA:ARBA00023136, 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000018296}.
FT DOMAIN 10..192
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT BINDING 22..27
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00071"
FT BINDING 139..142
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00071"
SQ SEQUENCE 607 AA; 67650 MW; 620BD4B508823DC1 CRC64;
MSDKKDTRQS HIRNFSIIAH IDHGKSTLAD RILEATQALT QREMKAQALD AMDLERERGI
TIKLNAVELN YKAPDGETYI FHLIDTPGHV DFSYEVSRSL AACEGALLVV DAAQGVEAQT
LANVYLALEN NLEIIPVINK VDLPNADPDR VKNEIEEVIG LDASEAVLAS AKTGLGTDEI
LKQIIDKIPA PAGDPEAPLK ALIFDSLYDA YRGVVVYIRV VEGTVRVGDK IKMMANGKTF
EVLEVGVSTP KIENRDVLSV GDVGFLTASI KSVHDTQVGD TVTHADQPAS EALPGYRRMN
PMVYCGLYPI DTARYDDLRE ALGRLELNDS ALQYEPETSE ALGFGFRCGF LGLLHMDIVQ
ERLEREFNID LIATAPSVIY NVKLTDGSSV RVGNPSEMPE RKFISEIEEP YVKATIMTPN
DYVGAIMELC QRKRGEFQTM EYLDANRTNV IYDLPLSEIM YDFFDFLKSS TKGYASLDYE
MDGYRTSDLL KMDILLNGEK VDALSVIVHQ EFAYDRGKAI VEKLKELIPR QQFEVPIQAA
IGQKIISRST IKALRKNVLA KCYGGDVSRK RKLLEKQKEG KKRMKAVGSV EVPQEAFMAV
FKMSHDD
//
