YBEY_NITSB
ID YBEY_NITSB Reviewed; 144 AA.
AC A6Q339;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 78.
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=NIS_0786;
OS Nitratiruptor sp. (strain SB155-2).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Nautiliales;
OC Nitratiruptoraceae; Nitratiruptor; unclassified Nitratiruptor.
OX NCBI_TaxID=387092;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB155-2;
RX PubMed=17615243; DOI=10.1073/pnas.0700687104;
RA Nakagawa S., Takaki Y., Shimamura S., Reysenbach A.-L., Takai K.,
RA Horikoshi K.;
RT "Deep-sea vent epsilon-proteobacterial genomes provide insights into
RT emergence of pathogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12146-12150(2007).
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; AP009178; BAF69898.1; -; Genomic_DNA.
DR RefSeq; WP_012082161.1; NC_009662.1.
DR AlphaFoldDB; A6Q339; -.
DR SMR; A6Q339; -.
DR STRING; 387092.NIS_0786; -.
DR EnsemblBacteria; BAF69898; BAF69898; NIS_0786.
DR KEGG; nis:NIS_0786; -.
DR eggNOG; COG0319; Bacteria.
DR HOGENOM; CLU_106710_3_0_7; -.
DR OMA; CDYATDV; -.
DR OrthoDB; 1830156at2; -.
DR Proteomes; UP000001118; 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..144
FT /note="Endoribonuclease YbeY"
FT /id="PRO_0000321780"
FT BINDING 104
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00009"
FT BINDING 108
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00009"
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"
SQ SEQUENCE 144 AA; 16742 MW; 6FAECEA6D38385C4 CRC64;
MQNRLIEIFN ETDFDQFDIE LMESITSQLT DRPVELMIVD DERMRTLNKT YRDIDKTTDV
LSFPMQEIPN APLGSIVINA DKVLHTAKEL GHSAKDEFAL LYIHGLLHLL GYDHESDNGE
MRAMEEKLII EYNLPKSLII RTYE
