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YBEY_BURCM
ID   YBEY_BURCM              Reviewed;         175 AA.
AC   Q0BC19;
DT   17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 2.
DT   03-AUG-2022, entry version 88.
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=Bamb_2748;
OS   Burkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia cepacia
OS   (strain AMMD)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=339670;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-244 / AMMD;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Bruce D., Chain P.,
RA   Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Parke J., Coenye T., Konstantinidis K.,
RA   Ramette A., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Burkholderia cepacia AMMD.";
RL   Submitted (AUG-2006) 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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABI88304.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000440; ABI88304.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; Q0BC19; -.
DR   SMR; Q0BC19; -.
DR   STRING; 339670.Bamb_2748; -.
DR   EnsemblBacteria; ABI88304; ABI88304; Bamb_2748.
DR   KEGG; bam:Bamb_2748; -.
DR   eggNOG; COG0319; Bacteria.
DR   Proteomes; UP000000662; Chromosome 1.
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..175
FT                   /note="Endoribonuclease YbeY"
FT                   /id="PRO_0000284174"
FT   BINDING         137
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00009"
FT   BINDING         141
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00009"
FT   BINDING         147
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00009"
SQ   SEQUENCE   175 AA;  19403 MW;  EB45AB689E554F5C CRC64;
     MTLHVGAEPA PREEEIAEMA DEPRELEFDL SVQYGDEVTG DVRKACPKRK LIAEWIEPAL
     FSSAQLTVRF VGEEEGRTLN DGYRHKDYPT NVLTFAYDPL PDGTVIGDLV LCCPVVEKEA
     QEQGKPLAAH YAHLLVHGAL HAQGYDHETS EEDAAEMEAL EVAILAKLGF PNPYQ
 
 
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