RNE_BUCAI
ID RNE_BUCAI Reviewed; 902 AA.
AC P57429;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Ribonuclease E {ECO:0000255|HAMAP-Rule:MF_00970};
DE Short=RNase E {ECO:0000255|HAMAP-Rule:MF_00970};
DE EC=3.1.26.12 {ECO:0000255|HAMAP-Rule:MF_00970};
GN Name=rne {ECO:0000255|HAMAP-Rule:MF_00970}; OrderedLocusNames=BU347;
OS Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS pisum symbiotic bacterium).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=107806;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=APS;
RX PubMed=10993077; DOI=10.1038/35024074;
RA Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT sp. APS.";
RL Nature 407:81-86(2000).
CC -!- FUNCTION: Endoribonuclease that plays a central role in RNA processing
CC and decay. Required for the maturation of 5S and 16S rRNAs and the
CC majority of tRNAs. Also involved in the degradation of most mRNAs.
CC {ECO:0000255|HAMAP-Rule:MF_00970}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage of single-stranded RNA in A- and U-
CC rich regions.; EC=3.1.26.12; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00970};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00970};
CC Note=Binds 2 Zn(2+) ions per homotetramer. {ECO:0000255|HAMAP-
CC Rule:MF_00970};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00970};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00970};
CC -!- SUBUNIT: Component of the RNA degradosome, which is a multiprotein
CC complex involved in RNA processing and mRNA degradation. Within the RNA
CC degradosome, RNase E assembles into a homotetramer formed by a dimer of
CC dimers. {ECO:0000255|HAMAP-Rule:MF_00970}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00970}. Cell
CC inner membrane {ECO:0000255|HAMAP-Rule:MF_00970}; Peripheral membrane
CC protein {ECO:0000255|HAMAP-Rule:MF_00970}; Cytoplasmic side
CC {ECO:0000255|HAMAP-Rule:MF_00970}.
CC -!- SIMILARITY: Belongs to the RNase E/G family. RNase E subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00970}.
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DR EMBL; BA000003; BAB13052.1; -; Genomic_DNA.
DR RefSeq; NP_240166.1; NC_002528.1.
DR RefSeq; WP_010896079.1; NC_002528.1.
DR AlphaFoldDB; P57429; -.
DR SMR; P57429; -.
DR STRING; 107806.10039018; -.
DR PRIDE; P57429; -.
DR EnsemblBacteria; BAB13052; BAB13052; BAB13052.
DR KEGG; buc:BU347; -.
DR PATRIC; fig|107806.10.peg.359; -.
DR eggNOG; COG1530; Bacteria.
DR HOGENOM; CLU_003468_5_4_6; -.
DR OMA; TQINSAF; -.
DR Proteomes; UP000001806; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0004521; F:endoribonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008995; F:ribonuclease E activity; IEA:InterPro.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006402; P:mRNA catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-UniRule.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-UniRule.
DR Gene3D; 2.40.50.140; -; 1.
DR HAMAP; MF_00970; RNase_E; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR019307; RNA-bd_AU-1/RNase_E/G.
DR InterPro; IPR028878; RNase_E.
DR InterPro; IPR004659; RNase_E/G.
DR InterPro; IPR022967; S1_dom.
DR InterPro; IPR003029; S1_domain.
DR PANTHER; PTHR30001; PTHR30001; 1.
DR Pfam; PF10150; RNase_E_G; 1.
DR Pfam; PF00575; S1; 1.
DR SMART; SM00316; S1; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR TIGRFAMs; TIGR00757; RNaseEG; 1.
DR PROSITE; PS50126; S1; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Cytoplasm; Endonuclease; Hydrolase;
KW Magnesium; Membrane; Metal-binding; Nuclease; Reference proteome;
KW RNA-binding; rRNA processing; rRNA-binding; tRNA processing; tRNA-binding;
KW Zinc.
FT CHAIN 1..902
FT /note="Ribonuclease E"
FT /id="PRO_0000097370"
FT DOMAIN 39..119
FT /note="S1 motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00970"
FT REGION 404..407
FT /note="Required for zinc-mediated homotetramerization and
FT catalytic activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00970"
FT REGION 881..902
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 303
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00970"
FT BINDING 346
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00970"
FT BINDING 404
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00970"
FT BINDING 407
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00970"
SQ SEQUENCE 902 AA; 104007 MW; C3FA00476E3C2E37 CRC64;
MKRMLINATQ QEELRVALVD GQRLYDLDIE HSGSEQKKSN IYKGKITRIE PSLEAAFVDY
GEEKNGFLPL KEISKNYFPE NHIETLGFNI KNVLQEGQEV IVQISKEERG TKGAALTTFI
SLAGSYLVLM PNSPKSGGIS RRIEGNDRIA LKELLTLLEL PEEMSLIIRT AGAGKSIESL
RWDLSLRLQH WKTIQIIAKS RTAPFLIHQE SNIIVRAFRD YLRQDIGEIL IDNPKILDLA
RKHITFLGRP DFVNKIKLYS GEVPLFSYFQ IETQINSAFQ RKVRLPSGGS IMVDSTEALT
AIDINSSRST SGTDIASTAF NTNLEAVDEI SRQLRLRDLG GLIVIDFIDM SAISHQRAIE
NRLREIARDD RARIQIGQIS RFGLLEMSRQ RLSSSLGESS HHICPRCTGT GTIRDNESLS
LSILRLIEEE ALKENTYEVR AIVPVEIACY LLNEKRDAVH AIEKRQAGGK TIIVPSKKMK
TPHYSVSRIR KSESKNYTRY GLSNIRQSKI TSFLKKNLLK KKQKEILDVA NFNFYDNCYN
KIQEAQENIL KKNNYNNILL KVLSNNRNFI FKMITWFKNS FFIKNMLITS DIFKKNTLKN
TNNIFFKKKY SSLNKKNNNQ KKRVILSKLF EANIENIPLK NKKLDTSSAN YLYDNIERKK
NITKKNDLIQ KNIHENSYLK HVLMNRYNVI NIINNNYIFY KIFNRTKIFK NQNTNNSFLK
FSSVTSPIFI FSSVFSLELA LGKVWIKYPI AILDETKKQK KLNRKQILHI SSISETNTIV
NKNNYSGIKK IKHETYSFKK YVKNNIQNQE VTQSQLIKRT KKRNVFILDK KNFLYKRTCN
RKNKIHQSSA PITKISKQSD LNKKEKEFHY NLSMMKSSLR GKNSAGVHSA TNFSNSPVSK
LK
