LEPA_CORJK
ID LEPA_CORJK Reviewed; 616 AA.
AC Q4JWS1;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 98.
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=jk0577;
OS Corynebacterium jeikeium (strain K411).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=306537;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K411;
RX PubMed=15968079; DOI=10.1128/jb.187.13.4671-4682.2005;
RA Tauch A., Kaiser O., Hain T., Goesmann A., Weisshaar B., Albersmeier A.,
RA Bekel T., Bischoff N., Brune I., Chakraborty T., Kalinowski J., Meyer F.,
RA Rupp O., Schneiker S., Viehoever P., Puehler A.;
RT "Complete genome sequence and analysis of the multiresistant nosocomial
RT pathogen Corynebacterium jeikeium K411, a lipid-requiring bacterium of the
RT human skin flora.";
RL J. Bacteriol. 187:4671-4682(2005).
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; CR931997; CAI36736.1; -; Genomic_DNA.
DR RefSeq; WP_005296435.1; NC_007164.1.
DR AlphaFoldDB; Q4JWS1; -.
DR SMR; Q4JWS1; -.
DR STRING; 306537.jk0577; -.
DR PRIDE; Q4JWS1; -.
DR EnsemblBacteria; CAI36736; CAI36736; jk0577.
DR GeneID; 56650058; -.
DR KEGG; cjk:jk0577; -.
DR eggNOG; COG0481; Bacteria.
DR HOGENOM; CLU_009995_3_3_11; -.
DR OMA; MVQIAIQ; -.
DR OrthoDB; 182107at2; -.
DR Proteomes; UP000000545; 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; 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; 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..616
FT /note="Elongation factor 4"
FT /id="PRO_0000224754"
FT DOMAIN 17..203
FT /note="tr-type G"
FT BINDING 29..34
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00071"
FT BINDING 150..153
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00071"
SQ SEQUENCE 616 AA; 68445 MW; 1639DB3997A8F695 CRC64;
MAAKQKNYAT ETFTDPERIR NFCIIAHIDH GKSTLADRIL QMSGVVEDRD MRDQYLDNMD
IERERGITIK AQNVRLPWVP KTGAHAGEEL VMHLIDTPGH VDFTYEVSRA LEACEGCILL
VDAAQGIEAQ TLANLYLAME NDLEIIPVLN KIDLPAADPD KYALEIAHII GCEPEDVLRV
SGKTGEGVSE LLDRVCELVP APVGDADAPA RAMIFDSVYD IYRGVVTYVR MMDGKLESRQ
KIQMMSTGAT HETLEIGVVS PEPTKTKGLG VGEVGYIITG VKDVRQSKVG DTITWAVNGA
ETPLKGYQEP TPMVYSGLFP ISADQYPDLR EAIEKLQLND ASLTFEPETS VALGFGFRCG
FLGLLHMEIT RARLEREFDL DLISTAPSVV YRVVKEDGSE VMVRNPSDWP GGKMREIYEP
IVKMTVIVPA EFLGATMELC QSKRGQMGGM DYLSEDRVEL RYTMPLGEII FDFFDQLKSR
TKGYASLNYE EAGEQLADLV KVDILLQGDP VDAFSAIVHR ENAHWYGNKM TVKLKELIPR
QQFEVPVQAA IGSKIIAREN IRALRKDVLS KCYGGDVSRK RKLLEKQKEG KKRMKAIGSV
SVPQEAFVAA LSTDAD
