ID A0A0N0CSV5_9LACO Unreviewed; 159 AA.
AC A0A0N0CSV5;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
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 ECO:0000313|EMBL:KOY76296.1};
GN ORFNames=RZ71_07460 {ECO:0000313|EMBL:KOY76296.1}, RZ78_12640
GN {ECO:0000313|EMBL:KPN82152.1};
OS Apilactobacillus kunkeei.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Apilactobacillus.
OX NCBI_TaxID=148814 {ECO:0000313|EMBL:KOY76296.1, ECO:0000313|Proteomes:UP000037778};
RN [1] {ECO:0000313|Proteomes:UP000037778, ECO:0000313|Proteomes:UP000050269}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LAko {ECO:0000313|EMBL:KOY76296.1,
RC ECO:0000313|Proteomes:UP000037778}, and LMbo
RC {ECO:0000313|EMBL:KPN82152.1, ECO:0000313|Proteomes:UP000050269};
RX PubMed=25953738; DOI=10.1093/gbe/evv079;
RA Tamarit D., Ellegaard K.M., Wikander J., Olofsson T., Vasquez A.,
RA Andersson S.G.;
RT "Functionally Structured Genomes in Lactobacillus kunkeei Colonizing the
RT Honey Crop and Food Products of Honeybees and Stingless Bees.";
RL Genome Biol. Evol. 7:1455-1473(2015).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KOY76296.1}.
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DR EMBL; JXCY01000006; KOY76296.1; -; Genomic_DNA.
DR EMBL; JXDF01000017; KPN82152.1; -; Genomic_DNA.
DR RefSeq; WP_053791815.1; NZ_JXDF01000017.1.
DR PATRIC; fig|148814.10.peg.813; -.
DR OrthoDB; 9807740at2; -.
DR Proteomes; UP000037778; Unassembled WGS sequence.
DR Proteomes; UP000050269; Unassembled WGS sequence.
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:UP000037778};
KW Ribosome biogenesis {ECO:0000256|ARBA:ARBA00022517, ECO:0000256|HAMAP-
KW Rule:MF_00009};
KW rRNA processing {ECO:0000256|ARBA:ARBA00022552, ECO:0000256|HAMAP-
KW Rule:MF_00009};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00009}.
FT BINDING 125
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00009"
FT BINDING 129
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00009"
FT BINDING 135
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00009"
SQ SEQUENCE 159 AA; 18354 MW; A168F20D6ACC00BB CRC64;
MDLEIYDKTK DGVDQKHIDL VEDVLQFASK ALDLKDNTEM SVTFVNNDEI KEINSKYRGV
DRATDVISFA IEDGDDDFPL IMDDEMAAEI PENIGDIFVS IDKVAEQAEF LDHSYERELG
FLVVHGFLHL NGYDHMKQED EDVMFPLQRK IMDDYGLKR
//
