YBEY_ACIBY
ID YBEY_ACIBY Reviewed; 158 AA.
AC B0V6T5;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 73.
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=ABAYE0460;
OS Acinetobacter baumannii (strain AYE).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX NCBI_TaxID=509173;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AYE;
RX PubMed=18350144; DOI=10.1371/journal.pone.0001805;
RA Vallenet D., Nordmann P., Barbe V., Poirel L., Mangenot S., Bataille E.,
RA Dossat C., Gas S., Kreimeyer A., Lenoble P., Oztas S., Poulain J.,
RA Segurens B., Robert C., Abergel C., Claverie J.-M., Raoult D., Medigue C.,
RA Weissenbach J., Cruveiller S.;
RT "Comparative analysis of Acinetobacters: three genomes for three
RT lifestyles.";
RL PLoS ONE 3:E1805-E1805(2008).
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; CU459141; CAM85433.1; -; Genomic_DNA.
DR RefSeq; WP_000703572.1; NC_010410.1.
DR AlphaFoldDB; B0V6T5; -.
DR SMR; B0V6T5; -.
DR EnsemblBacteria; CAM85433; CAM85433; ABAYE0460.
DR KEGG; aby:ABAYE0460; -.
DR HOGENOM; CLU_106710_0_1_6; -.
DR OMA; RMRIHPL; -.
DR Proteomes; UP000002446; 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..158
FT /note="Endoribonuclease YbeY"
FT /id="PRO_1000089144"
FT BINDING 119
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"
FT BINDING 129
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00009"
SQ SEQUENCE 158 AA; 17979 MW; 44F0636E63849AA1 CRC64;
MKISLSLQQD FRSPELELKR AQLKKIIETT LRHVGYKEDC EIGIACVDLE ESHQLNLQYR
EKDKPTNVLS FPSDIPEEVL PMLDALPLGD LVICIPVVLQ EALEQKKTAQ NHFAHLLVHG
VLHLLGYDHE TSDEDAEEME GLEIEILAKL NIANPYQE
