ID   YBEY_BORT9              Reviewed;         148 AA.
AC   A1QYL0;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-APR-2009, sequence version 1.
DT   03-AUG-2022, entry version 74.
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=BT0060;
OS   Borrelia turicatae (strain 91E135).
OC   Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borrelia.
OX   NCBI_TaxID=314724;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=91E135;
RA   Porcella S.F., Raffel S.J., Schrumpf M.E., Montgomery B., Smith T.,
RA   Schwan T.G.;
RT   "The genome sequence of Borrelia hermsii and Borrelia turicatae:
RT   comparative analysis of two agents of endemic N. America relapsing fever.";
RL   Submitted (DEC-2004) 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; CP000049; AAX17402.1; -; Genomic_DNA.
DR   RefSeq; WP_011772021.1; NC_008710.1.
DR   AlphaFoldDB; A1QYL0; -.
DR   SMR; A1QYL0; -.
DR   STRING; 314724.BT0060; -.
DR   KEGG; btu:BT0060; -.
DR   eggNOG; COG0319; Bacteria.
DR   HOGENOM; CLU_106710_3_3_12; -.
DR   OMA; RMRIHPL; -.
DR   OrthoDB; 1830156at2; -.
DR   Proteomes; UP000001205; 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..148
FT                   /note="Endoribonuclease YbeY"
FT                   /id="PRO_1000199957"
FT   BINDING         113
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00009"
FT   BINDING         117
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00009"
FT   BINDING         123
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00009"
SQ   SEQUENCE   148 AA;  17761 MW;  173A1F070C3F9F75 CRC64;
     MIKEELNLWA EGVEFKHWDA YYNFILSVLD FLCIKEYELS VILCNNEYIQ KLNSQFRQKS
     EPTDVLSFNY LEESGQIDHK IQGDLIISLE YLEFSSLEFN VELYDELQRN TIHGILHLIG
     YTHKTNDFQN EEMLIIQEKV LRETRRVF