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 27-MAR-2024, entry version 114.
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; Pseudomonadota; 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 AlphaFoldDB; Q89AH3; -.
DR SMR; Q89AH3; -.
DR STRING; 224915.bbp_317; -.
DR KEGG; bab:bbp_317; -.
DR eggNOG; COG1530; Bacteria.
DR HOGENOM; CLU_003468_5_3_6; -.
DR OrthoDB; 9804278at2; -.
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:RNA nuclease 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 CDD; cd04453; S1_RNase_E; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 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; 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; 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.
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
//
