ID   RNE_BUCBP               Reviewed;         410 AA.
AC   Q89AH3;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Putative ribonuclease E;
DE            Short=RNase E;
DE            EC=3.1.26.12;
GN   Name=rne; OrderedLocusNames=bbp_317;
OS   Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=224915;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bp;
RX   PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA   van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA   Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA   Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT   "Reductive genome evolution in Buchnera aphidicola.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).
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 (By
CC       similarity). {ECO:0000250|UniProtKB:P21513}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endonucleolytic cleavage of single-stranded RNA in A- and U-
CC         rich regions.; EC=3.1.26.12;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P21513};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:P21513};
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 (By similarity). {ECO:0000250|UniProtKB:P21513}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P21513}. Cell
CC       inner membrane {ECO:0000250|UniProtKB:P21513}; Peripheral membrane
CC       protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the RNase E/G family. RNase E subfamily.
CC       {ECO:0000305}.
CC   -!- CAUTION: This sequence is much shorter than orthologs. {ECO:0000305}.
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DR   EMBL; AE016826; AAO27039.1; -; Genomic_DNA.
DR   RefSeq; WP_011091440.1; NC_004545.1.
DR   AlphaFoldDB; Q89AH3; -.
DR   SMR; Q89AH3; -.
DR   STRING; 224915.bbp_317; -.
DR   EnsemblBacteria; AAO27039; AAO27039; bbp_317.
DR   GeneID; 56470856; -.
DR   KEGG; bab:bbp_317; -.
DR   eggNOG; COG1530; Bacteria.
DR   HOGENOM; CLU_003468_5_3_6; -.
DR   OMA; TAYRTNM; -.
DR   OrthoDB; 1209444at2; -.
DR   Proteomes; UP000000601; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004540; F:ribonuclease 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:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.50.140; -; 1.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR019307; RNA-bd_AU-1/RNase_E/G.
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.
FT   CHAIN           1..410
FT                   /note="Putative ribonuclease E"
FT                   /id="PRO_0000097372"
FT   DOMAIN          39..119
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT   BINDING         303
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P21513"
FT   BINDING         346
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P21513"
SQ   SEQUENCE   410 AA;  47312 MW;  0BF3F415144E5FCE CRC64;
     MRRMLINAIE IKKLRIALID GQQLYDLNVE NIDKKQRKSN IYKGKIVRIE PSLEAAFVDY
     GEKKNGFLPL KEISRNYFPN NCSNYRHLHI KNILKEGQEC IVQIDKEERG TKGALLTTFI
     SLAGNYLVLM PNCPHLEGIS RKIEGIDRFH LKKIISMLMV PENMGIIIRT SGVGRSIETL
     QLDLNFRVKN WYTIKKSAEI NTAPCLIHKE SNIVIRTLRD YLKKDIQEII VDNPEILELA
     RDYMFNMNCS YFEKKIKLYT GSDPLFSYYK IESQINALLR RIVKLPSGGS IIIDYTEALT
     AIDINSSQST KGVNIEETAF NTNYEAVREI ARQLRLRDLG GLIVIDFIDM SVLKHQKMIE
     LHLHQVLQKD RARVQVGSIS QFGLLEMSRQ CLGSPLKKIN HNYLFEMQKC