LEPA_RUMCH
ID LEPA_RUMCH Reviewed; 602 AA.
AC B8I3E6;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Elongation factor 4 {ECO:0000255|HAMAP-Rule:MF_00071};
DE Short=EF-4 {ECO:0000255|HAMAP-Rule:MF_00071};
DE EC=3.6.5.n1 {ECO:0000255|HAMAP-Rule:MF_00071};
DE AltName: Full=Ribosomal back-translocase LepA {ECO:0000255|HAMAP-Rule:MF_00071};
GN Name=lepA {ECO:0000255|HAMAP-Rule:MF_00071}; OrderedLocusNames=Ccel_1941;
OS Ruminiclostridium cellulolyticum (strain ATCC 35319 / DSM 5812 / JCM 6584 /
OS H10) (Clostridium cellulolyticum).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Oscillospiraceae;
OC Ruminiclostridium.
OX NCBI_TaxID=394503;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35319 / DSM 5812 / JCM 6584 / H10;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Saunders E., Brettin T.,
RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Ivanova N., Zhou J., Richardson P.;
RT "Complete sequence of Clostridium cellulolyticum H10.";
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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:0000255|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:0000255|HAMAP-Rule:MF_00071};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00071};
CC Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_00071};
CC Cytoplasmic side {ECO:0000255|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:0000255|HAMAP-Rule:MF_00071}.
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DR EMBL; CP001348; ACL76289.1; -; Genomic_DNA.
DR RefSeq; WP_015925393.1; NC_011898.1.
DR AlphaFoldDB; B8I3E6; -.
DR SMR; B8I3E6; -.
DR STRING; 394503.Ccel_1941; -.
DR EnsemblBacteria; ACL76289; ACL76289; Ccel_1941.
DR KEGG; cce:Ccel_1941; -.
DR eggNOG; COG0481; Bacteria.
DR HOGENOM; CLU_009995_3_3_9; -.
DR OMA; MVQIAIQ; -.
DR OrthoDB; 182107at2; -.
DR Proteomes; UP000001349; 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; cd03709; lepA_C; 1.
DR Gene3D; 3.30.70.2570; -; 1.
DR Gene3D; 3.40.50.300; -; 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 PANTHER; PTHR43512; PTHR43512; 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; SSF50447; SSF50447; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54980; SSF54980; 2.
DR TIGRFAMs; TIGR01393; lepA; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 3: Inferred from homology;
KW Cell membrane; GTP-binding; Hydrolase; Membrane; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..602
FT /note="Elongation factor 4"
FT /id="PRO_1000118045"
FT DOMAIN 7..189
FT /note="tr-type G"
FT BINDING 19..24
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00071"
FT BINDING 136..139
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00071"
SQ SEQUENCE 602 AA; 67660 MW; 01D0A7DAA9C87075 CRC64;
MPSERQKYIR NFCIIAHIDH GKSTLADRLL EKTGVLTSRE MQEQVLDNME LERERGITIK
AQAVRMVYKA SDGHEYIYNL IDTPGHVDFN YEVSRSLAAC EGAILVVDAA QGIEAQTLAN
VYLALEHNLE IMPVINKIDL PSAQPEVVKK EIEDVIGLDA SQAPMISAKN GLNIEEVLEK
IVDMIPCPEA DEKAPLRALI FDSFYDSYKG VIVYIRVKEG TLKTGDTIRL MYTKKEFLVT
ELGYLKPGGL SPADELKAGD VGYIAASIKN VRDTRVGDTI TLVENPAKEP LPGYKKVNSM
VFCGIYPADG SKYGDLRDAL DRLQLNDAAL TFEPESSVAL GFGFRCGFLG LLHMEIIQER
LEREYNFDLV TTAPSVIYRV TTTDGDVIEI DNPTNLPPVT EIDSMEEPMV KATIMVPTEY
VGNIMDLSQE RRGIYKDMSY IDEGRAMLTY EMPLNEIIYD FFDALKSRTK GYASFDYELV
GYKESDLVKL DIMLNGEIVD ALSFIVHREK SVARGRRMAE KLKESIPRQM FEIPIQACIG
GKIIARETVK AFRKDVLSKC YGGDISRKRK LLEKQKEGKK RMRQVGSVEV PQEAFMSVLK
LD
