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Database: UniProt
Entry: D3UIA8_HELM1
LinkDB: D3UIA8_HELM1
Original site: D3UIA8_HELM1 
ID   D3UIA8_HELM1            Unreviewed;       151 AA.
AC   D3UIA8;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   27-MAR-2024, entry version 69.
DE   RecName: Full=Endoribonuclease YbeY {ECO:0000256|HAMAP-Rule:MF_00009};
DE            EC=3.1.-.- {ECO:0000256|HAMAP-Rule:MF_00009};
GN   Name=ybeY {ECO:0000256|HAMAP-Rule:MF_00009};
GN   OrderedLocusNames=HMU09740 {ECO:0000313|EMBL:CBG40231.1};
OS   Helicobacter mustelae (strain ATCC 43772 / LMG 18044 / NCTC 12198 / 12198)
OS   (Campylobacter mustelae).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=679897 {ECO:0000313|EMBL:CBG40231.1, ECO:0000313|Proteomes:UP000001522};
RN   [1] {ECO:0000313|EMBL:CBG40231.1, ECO:0000313|Proteomes:UP000001522}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43772 / LMG 18044 / NCTC 12198 / 12198
RC   {ECO:0000313|Proteomes:UP000001522};
RX   PubMed=20219135; DOI=10.1186/1471-2164-11-164;
RA   O'Toole P.W., Snelling W.J., Canchaya C., Forde B.M., Hardie K.R.,
RA   Josenhans C., Graham R.L.J., McMullan G., Parkhill J., Belda E.,
RA   Bentley S.D.;
RT   "Comparative genomics and proteomics of Helicobacter mustelae, an
RT   ulcerogenic and carcinogenic gastric pathogen.";
RL   BMC Genomics 11:164-164(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:0000256|HAMAP-Rule:MF_00009}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00009};
CC       Note=Binds 1 zinc ion. {ECO:0000256|HAMAP-Rule:MF_00009};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00009}.
CC   -!- SIMILARITY: Belongs to the endoribonuclease YbeY family.
CC       {ECO:0000256|ARBA:ARBA00010875, ECO:0000256|HAMAP-Rule:MF_00009}.
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DR   EMBL; FN555004; CBG40231.1; -; Genomic_DNA.
DR   RefSeq; WP_013023303.1; NC_013949.1.
DR   AlphaFoldDB; D3UIA8; -.
DR   STRING; 679897.HMU09740; -.
DR   KEGG; hms:HMU09740; -.
DR   eggNOG; COG0319; Bacteria.
DR   HOGENOM; CLU_106710_3_0_7; -.
DR   Proteomes; UP000001522; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0004521; F:RNA endonuclease activity; IEA:UniProtKB-UniRule.
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; Metalloproteases ('zincins'), catalytic domain; 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   NCBIfam; TIGR00043; rRNA maturation RNase YbeY; 1.
DR   PANTHER; PTHR46986; ENDORIBONUCLEASE YBEY, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR46986:SF1; YBEY METALLOENDORIBONUCLEASE; 1.
DR   Pfam; PF02130; YbeY; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   PROSITE; PS01306; UPF0054; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00009};
KW   Endonuclease {ECO:0000256|ARBA:ARBA00022759, ECO:0000256|HAMAP-
KW   Rule:MF_00009};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00009};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00009};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_00009};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001522};
KW   Ribosome biogenesis {ECO:0000256|HAMAP-Rule:MF_00009};
KW   rRNA processing {ECO:0000256|HAMAP-Rule:MF_00009};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00009}.
FT   BINDING         105
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00009"
FT   BINDING         109
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00009"
FT   BINDING         115
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00009"
SQ   SEQUENCE   151 AA;  17067 MW;  A6431CB45C232260 CRC64;
     MSRCLEIDNQ TTTLLETARL EKIAQTLSPQ RMIELLFVDE NMIQGMNKEY RNQDKPTDVL
     SFPLDAMGIA NMPLGSVVIC IPIAQGAAHF FGHSLEEEIA LLFIHGVLHL QGYDHEVDLG
     EHYAAEKQWI EFFSLPSGLI VRTLEEPSKK Q
//
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