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YBEY_CAUVN
ID   YBEY_CAUVN              Reviewed;         157 AA.
AC   B8GX09;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 82.
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=CCNA_00052;
OS   Caulobacter vibrioides (strain NA1000 / CB15N) (Caulobacter crescentus).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Caulobacter.
OX   NCBI_TaxID=565050;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NA1000 / CB15N;
RX   PubMed=20472802; DOI=10.1128/jb.00255-10;
RA   Marks M.E., Castro-Rojas C.M., Teiling C., Du L., Kapatral V.,
RA   Walunas T.L., Crosson S.;
RT   "The genetic basis of laboratory adaptation in Caulobacter crescentus.";
RL   J. Bacteriol. 192:3678-3688(2010).
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=ACL93519.3; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; CP001340; ACL93519.3; ALT_INIT; Genomic_DNA.
DR   RefSeq; YP_002515427.3; NC_011916.1.
DR   AlphaFoldDB; B8GX09; -.
DR   SMR; B8GX09; -.
DR   PRIDE; B8GX09; -.
DR   EnsemblBacteria; ACL93519; ACL93519; CCNA_00052.
DR   GeneID; 7332142; -.
DR   KEGG; ccs:CCNA_00052; -.
DR   PATRIC; fig|565050.3.peg.52; -.
DR   HOGENOM; CLU_106710_0_1_5; -.
DR   OMA; RMRIHPL; -.
DR   OrthoDB; 1830156at2; -.
DR   PhylomeDB; B8GX09; -.
DR   Proteomes; UP000001364; 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   Reference proteome; Ribosome biogenesis; rRNA processing; Zinc.
FT   CHAIN           1..157
FT                   /note="Endoribonuclease YbeY"
FT                   /id="PRO_1000199960"
FT   BINDING         114
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00009"
FT   BINDING         118
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00009"
FT   BINDING         124
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00009"
SQ   SEQUENCE   157 AA;  17193 MW;  7E162D9FF2B7A080 CRC64;
     MTITVDIEIE DEAWTTAEAD AEALVWRAAQ AVLDAHEDIE GQGIVILLTD DDSVQALNRD
     FRKKDYATNV LSFPSPPNPE GQIGDIALAY GVCAREAAEQ GKPLAHHLQH LVAHGVLHLL
     GYDHERDDEA EAMEALEREI LAGLDVPDPY ASDEEGR
 
 
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