LEPA2_RHOBA
ID LEPA2_RHOBA Reviewed; 598 AA.
AC Q7UE01;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Elongation factor 4 2 {ECO:0000255|HAMAP-Rule:MF_00071};
DE Short=EF-4 2 {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 2 {ECO:0000255|HAMAP-Rule:MF_00071};
GN Name=lepA2 {ECO:0000255|HAMAP-Rule:MF_00071}; OrderedLocusNames=RB11673;
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; BX294153; CAD79254.1; -; Genomic_DNA.
DR RefSeq; NP_870099.1; NC_005027.1.
DR RefSeq; WP_007334775.1; NC_005027.1.
DR AlphaFoldDB; Q7UE01; -.
DR SMR; Q7UE01; -.
DR STRING; 243090.RB11673; -.
DR EnsemblBacteria; CAD79254; CAD79254; RB11673.
DR KEGG; rba:RB11673; -.
DR PATRIC; fig|243090.15.peg.5654; -.
DR eggNOG; COG0481; Bacteria.
DR HOGENOM; CLU_009995_3_3_0; -.
DR InParanoid; Q7UE01; -.
DR OMA; MVQIAIQ; -.
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; 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 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 2"
FT /id="PRO_0000176331"
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; 66813 MW; BAA9E743AA4B2B79 CRC64;
MKHIRNFCII AHIDHGKSTL ADRLIQSCGG VTQREFHDQM LDSMDIERER GITIKSNTVT
LNYTAKDGEA YQLNLIDTPG HVDFSHEVRR SLMACEGALM VVDASQGVEA QTVANLYLAL
EYDLELLPVI NKIDLPAADV DRVRGEIDED LGLDPFVAIP VSAKTGQGIE DVLEGIVKNL
PAPKGDPKAP LKALVFDAFF DKYRGVILQC RVMEGTLKPK DEIHFMHADR DFTVDELGYN
QFKLVPKKEL TAGEVGYIVA GVKTVQDIEI GDTITLANRP ADEPIPGYQP ARQVVFSSVY
PMSTDEYQDL TKALEKLSIN DAALTFEKDS SAALGFGYRC GFLGLLHLDV VQERLQREFD
IGLVISAPSV QYKIKLKDGT TQDVDNPTYW PDPSTIDSVS EPYIKAQILI PEEYVGPVME
LCREHRSESQ TMNYLSAGRL EVTSEMPLGE VLFDFYGKLK MITRGYGSFD YVPIEYRKTD
IVKVDILVNK EPVDALAYLV HRDKSRARAM HYCEQLAEAI PRHQFKIPIQ GAIGGTVIAR
TTIAPYRKDV TAKLYGGDVS RKKKLLEKQK KGKAKMKQFG SVNIPQKAFI SVLRTDKD
