LEPA_SYNFM
ID LEPA_SYNFM Reviewed; 598 AA.
AC A0LI00;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 92.
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=Sfum_1361;
OS Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophobacterales;
OC Syntrophobacteraceae; Syntrophobacter.
OX NCBI_TaxID=335543;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10017 / MPOB;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E.G.,
RA Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Kim E., Boone D.R., Brockman F., Culley D., Ferry J., Gunsalus R.,
RA McInerney M.J., Morrison M., Plugge C., Rohlin L., Scholten J., Sieber J.,
RA Stams A.J.M., Worm P., Henstra A.M., Richardson P.;
RT "Complete sequence of Syntrophobacter fumaroxidans MPOB.";
RL Submitted (OCT-2006) 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 inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_00071}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_00071}; 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; CP000478; ABK17052.1; -; Genomic_DNA.
DR RefSeq; WP_011698223.1; NC_008554.1.
DR AlphaFoldDB; A0LI00; -.
DR SMR; A0LI00; -.
DR STRING; 335543.Sfum_1361; -.
DR PRIDE; A0LI00; -.
DR EnsemblBacteria; ABK17052; ABK17052; Sfum_1361.
DR KEGG; sfu:Sfum_1361; -.
DR eggNOG; COG0481; Bacteria.
DR HOGENOM; CLU_009995_3_3_7; -.
DR OMA; HIDFNHE; -.
DR OrthoDB; 182107at2; -.
DR Proteomes; UP000001784; 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 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 inner membrane; Cell membrane; GTP-binding; Hydrolase; Membrane;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..598
FT /note="Elongation factor 4"
FT /id="PRO_1000032064"
FT DOMAIN 2..184
FT /note="tr-type G"
FT BINDING 14..19
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00071"
FT BINDING 131..134
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00071"
SQ SEQUENCE 598 AA; 66704 MW; 46ABF45F126E7D59 CRC64;
MTKIRNFSII AHIDHGKSTL ADRLIQRAGL VTDRQFRDQI LDNMDIERER GITIKSQTVT
LPYRSRNGEE VELNLIDTPG HVDFSYEVSR ALASCEGVLL LVDASQGVQA QTLANLYAAM
EHDLTIIPVI NKIDLLSADI ENTRAQIESE LGLDSSQAVL CSAKEGRGID DVLEAVVDRI
PPPSGKLDAP LSALIFDAHY DSFRGTIVAC RVFDGSVRPG DVIRFMSNGA TYKVEEVGVF
RLSREPKKEL RAGMVGYVIS GVKTVSDTRV GDTITLDSNP VPAPLPGFKE VKPVVFSSIY
PISSDDYLSL ADSLEKYKLN DAALIYQKDS SVALGQGFRC GFLGLLHLEI VQERLEREYD
QSIIMTFPSV QYVLTLEDGS TTMVDNPQYY PDPIRIRTSA EPFIKASIII PERYMGAVMK
LCLDKRGVNP RFNYPTPGRI EISMEMPLAE VVFDFYDKLK TVTQGYGSFD YDLIEHRVSD
LVKLDILVNS EKVDALSLIV HRERAREWAV QVCDRLKEEI PRHQFKIAIQ GAIGGKIIAR
STVNAFRKDV TAKCYGGDIS RKRKLLEKQK KGKKRMKMVG SVMIPQSAFV AVLKADNE
