LEPA1_RHOBA
ID LEPA1_RHOBA Reviewed; 604 AA.
AC Q7UX15;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Elongation factor 4 1 {ECO:0000255|HAMAP-Rule:MF_00071};
DE Short=EF-4 1 {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 1 {ECO:0000255|HAMAP-Rule:MF_00071};
GN Name=lepA1 {ECO:0000255|HAMAP-Rule:MF_00071}; OrderedLocusNames=RB1630;
OS Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1).
OC Bacteria; Planctomycetes; Planctomycetia; Pirellulales; Pirellulaceae;
OC Rhodopirellula.
OX NCBI_TaxID=243090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10527 / NCIMB 13988 / SH1;
RX PubMed=12835416; DOI=10.1073/pnas.1431443100;
RA Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W.,
RA Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R.,
RA Reinhardt R.;
RT "Complete genome sequence of the marine planctomycete Pirellula sp. strain
RT 1.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003).
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; BX294135; CAD72197.1; -; Genomic_DNA.
DR RefSeq; NP_864516.1; NC_005027.1.
DR RefSeq; WP_011118463.1; NC_005027.1.
DR AlphaFoldDB; Q7UX15; -.
DR SMR; Q7UX15; -.
DR STRING; 243090.RB1630; -.
DR EnsemblBacteria; CAD72197; CAD72197; RB1630.
DR KEGG; rba:RB1630; -.
DR PATRIC; fig|243090.15.peg.762; -.
DR eggNOG; COG0481; Bacteria.
DR HOGENOM; CLU_009995_3_3_0; -.
DR InParanoid; Q7UX15; -.
DR OMA; HIDFNHE; -.
DR OrthoDB; 182107at2; -.
DR Proteomes; UP000001025; 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; IBA:GO_Central.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0045727; P:positive regulation of translation; IBA:GO_Central.
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; 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; 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..604
FT /note="Elongation factor 4 1"
FT /id="PRO_0000176330"
FT DOMAIN 10..191
FT /note="tr-type G"
FT BINDING 22..27
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00071"
FT BINDING 138..141
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00071"
SQ SEQUENCE 604 AA; 66781 MW; A328AAB8B69FEA2D CRC64;
MASKSSRSQE HIRNFCIIAH IDHGKSTLAD RLLESTGTVD NRGKKTQMLD DLALEQQRGI
TIKARAVAMR YKRDGIEYEL NLIDTPGHVD FQYEVSRSLA CCEGALLLVD AFQGVEAQTV
ANAFAAMEHD LTIVPVINKI DLIHARPDEV AEEMMNSLGT DPDECKRVSA KTGEGVAALL
DAIVDSVPAP TGDPKAVLQA MVFDSNYDDF RGAITYIRVM QGTVRKGQKI KFLRAGSVHD
VVELGQFAPS RVPCDELVAG QVGYLICNIK SLGDVHIGDT ISIAGNDPAP ALPGYDRPKR
MVYCGLFPSD GQDFSELRDA LERLAVNDPS FEFEPETSDA LGFGFRCGFL GLLHMEIVQQ
RLEQESDIDL VQTAPNVTYE ITDKRGVTKN IHKPQDVPDP GDIEKFCQPI VRCNVIVPEE
YIGPVMKLCQ ERRGIQKGHE VLGASRAMLT YDIPLAEVIY DLHDRIKSCT RGYGTLDYEM
VGYEEADLCR LDILVNGNRV DALSVVCHRA DADRRGRAVA KKLKSEIERH MFEVAVQAAI
GSRVIARETV PAMRKNVTAK CYGGDITRKR KLLQKQKEGK KRMKAVGNVE ISQKAFMAVL
TDGE
