ID U3P9C1_LEIXC Unreviewed; 611 AA.
AC U3P9C1;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 24-JAN-2024, entry version 43.
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=O159_14340 {ECO:0000313|EMBL:AGW41497.1};
OS Leifsonia xyli subsp. cynodontis DSM 46306.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Leifsonia.
OX NCBI_TaxID=1389489 {ECO:0000313|EMBL:AGW41497.1, ECO:0000313|Proteomes:UP000016743};
RN [1] {ECO:0000313|EMBL:AGW41497.1, ECO:0000313|Proteomes:UP000016743}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 46306 {ECO:0000313|EMBL:AGW41497.1};
RX PubMed=24201198;
RA Monteiro-Vitorello C.B., Zerillo M.M., Van Sluys M.A., Camargo L.E.,
RA Kitajima J.P.;
RT "Complete Genome Sequence of Leifsonia xyli subsp. cynodontis Strain
RT DSM46306, a Gram-Positive Bacterial Pathogen of Grasses.";
RL Genome Announc. 1:e00915-13(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}.
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DR EMBL; CP006734; AGW41497.1; -; Genomic_DNA.
DR AlphaFoldDB; U3P9C1; -.
DR STRING; 1389489.O159_14340; -.
DR KEGG; lxy:O159_14340; -.
DR PATRIC; fig|1389489.3.peg.1378; -.
DR eggNOG; COG0481; Bacteria.
DR HOGENOM; CLU_009995_3_3_11; -.
DR Proteomes; UP000016743; Chromosome.
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; 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; 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|HAMAP-Rule:MF_00071};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00071};
KW Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00071}.
FT DOMAIN 12..193
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT BINDING 24..29
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00071"
FT BINDING 140..143
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00071"
SQ SEQUENCE 611 AA; 67009 MW; 5DD73CD5AF86C124 CRC64;
MNALEPAATD PALIRNFCII AHIDHGKSTL ADRMLQITGV VTERGMRAQY LDRMDIERER
GITIKSQAVR MPWGLDGDSY ALNMIDTPGH VDFTYEVSRS LAACEGAILL VDAAQGIEAQ
TLANLYLALE NDLTVIPVLN KIDLPAADPD KYAAELASLI GGKPDDVLRV SGKTGAGVDE
LLDRVVQEIP APVGAADAPA RAMIFDSVYD SYRGVVTYVR MVDGRLGPRE RIQMMSTRAT
HEILEIGVSS PEPTASKGLA VGEVGYLITG VKDVRQSKVG DTVTSASKPA ADPLPGYTEP
KPMVFSGLYP IDGSDYPELR EALDKLKLSD AALVYEPETS VALGFGFRCG FLGLLHLEII
TERLSREFGL DLITTAPSVI YEVTTEDRKV ITVTNPSEYP TGKIERVEEP IVKAAILAPK
DYVGVIMELC QSRRGTLLGM EYLGEDRVEI RYTMPLGEIV FDFFDNLKSR TAGYASLDYE
PAGEHEADLV KVDILLQGEQ VDAFSAIVHR EKAYAYGTMM AGRLRELIPR QQFEVPIQAA
IGARIIAREN IRAIRKDVLA KCYGGDITRK RKLLEKQKEG KKRMKMVGRV EVPQEAFIAA
LSGEVGKKDK K
//