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   27-MAR-2024, entry version 120.
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; Pseudomonadota; 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; Evidence={ECO:0000255|HAMAP-
CC         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; Evidence={ECO:0000255|HAMAP-
CC         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; 563178.BUAP5A_341; -.
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   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:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008995; F:ribonuclease E activity; IEA:InterPro.
DR   GO; GO:0004521; F:RNA endonuclease activity; IEA:UniProtKB-UniRule.
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   CDD; cd04453; S1_RNase_E; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   Gene3D; 3.40.1260.20; Ribonuclease E, catalytic domain; 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; IPR048583; RNase_E_G_thioredoxin-like.
DR   InterPro; IPR003029; S1_domain.
DR   NCBIfam; TIGR00757; RNaseEG; 1.
DR   PANTHER; PTHR30001; RIBONUCLEASE; 1.
DR   PANTHER; PTHR30001:SF1; RIBONUCLEASE E_G-LIKE PROTEIN, CHLOROPLASTIC; 1.
DR   Pfam; PF10150; RNase_E_G; 1.
DR   Pfam; PF20833; RNase_E_G_Thio; 1.
DR   Pfam; PF00575; S1; 1.
DR   SMART; SM00316; S1; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 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
//