ID   YBEY_CLOB6              Reviewed;         166 AA.
AC   C3L3F6;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=Endoribonuclease YbeY {ECO:0000255|HAMAP-Rule:MF_00009};
DE            EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_00009};
GN   Name=ybeY {ECO:0000255|HAMAP-Rule:MF_00009}; OrderedLocusNames=CLJ_B3205;
OS   Clostridium botulinum (strain 657 / Type Ba4).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=515621;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=657 / Type Ba4;
RA   Shrivastava S., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A.,
RA   Smith T.J., Sutton G., Brettin T.S.;
RT   "Genome sequence of Clostridium botulinum Ba4 strain 657.";
RL   Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Single strand-specific metallo-endoribonuclease involved in
CC       late-stage 70S ribosome quality control and in maturation of the 3'
CC       terminus of the 16S rRNA. {ECO:0000255|HAMAP-Rule:MF_00009}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00009};
CC       Note=Binds 1 zinc ion. {ECO:0000255|HAMAP-Rule:MF_00009};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00009}.
CC   -!- SIMILARITY: Belongs to the endoribonuclease YbeY family.
CC       {ECO:0000255|HAMAP-Rule:MF_00009}.
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DR   EMBL; CP001083; ACQ54360.1; -; Genomic_DNA.
DR   RefSeq; WP_003359975.1; NC_012658.1.
DR   AlphaFoldDB; C3L3F6; -.
DR   SMR; C3L3F6; -.
DR   EnsemblBacteria; ACQ54360; ACQ54360; CLJ_B3205.
DR   KEGG; cbi:CLJ_B3205; -.
DR   HOGENOM; CLU_106710_3_0_9; -.
DR   OMA; RMRIHPL; -.
DR   Proteomes; UP000002333; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004521; F:endoribonuclease activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.390.30; -; 1.
DR   HAMAP; MF_00009; Endoribonucl_YbeY; 1.
DR   InterPro; IPR023091; MetalPrtase_cat_dom_sf_prd.
DR   InterPro; IPR002036; YbeY.
DR   InterPro; IPR020549; YbeY_CS.
DR   PANTHER; PTHR46986; PTHR46986; 1.
DR   Pfam; PF02130; YbeY; 1.
DR   TIGRFAMs; TIGR00043; TIGR00043; 1.
DR   PROSITE; PS01306; UPF0054; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Endonuclease; Hydrolase; Metal-binding; Nuclease;
KW   Ribosome biogenesis; rRNA processing; Zinc.
FT   CHAIN           1..166
FT                   /note="Endoribonuclease YbeY"
FT                   /id="PRO_1000201729"
FT   BINDING         132
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00009"
FT   BINDING         136
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00009"
FT   BINDING         142
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00009"
SQ   SEQUENCE   166 AA;  19801 MW;  24BB57DD7D62C3D0 CRC64;
     MIYIDNRQNK IKVNEEFENK IKEIIDYALK EEKVNIDYEI SVVFIDNNSI KEINKDYRNI
     DKATDVLSFP MLDYEEGKVF KDVYLNYEFD ESDLDEGNLI LGDIALSLEK AEEQSKEFGH
     SFLRETCYLT IHSVLHLLGY DHMEEEEKAI MRQREEEILK SFNLRR