ID F6GG20_LACS5 Unreviewed; 136 AA.
AC F6GG20;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
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=Lacal_1009 {ECO:0000313|EMBL:AEH00857.1};
OS Lacinutrix sp. (strain 5H-3-7-4).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Lacinutrix.
OX NCBI_TaxID=983544 {ECO:0000313|EMBL:AEH00857.1, ECO:0000313|Proteomes:UP000008297};
RN [1] {ECO:0000313|EMBL:AEH00857.1, ECO:0000313|Proteomes:UP000008297}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5H-3-7-4 {ECO:0000313|EMBL:AEH00857.1,
RC ECO:0000313|Proteomes:UP000008297};
RX PubMed=21725025; DOI=10.1128/JB.05518-11;
RA Klippel B., Lochner A., Bruce D.C., Walston Davenport K., Detter C.,
RA Goodwin L.A., Han J., Han S., Hauser L., Land M.L., Nolan M.,
RA Ovchinnikova G., Pennacchio L., Pitluck S., Tapia R., Woyke T.,
RA Wiebusch S., Basner A., Abe F., Horikoshi K., Keller M., Antranikian G.;
RT "Complete genome sequences of Krokinobacter sp. strain 4H-3-7-5 and
RT Lacinutrix sp. strain 5H-3-7-4, polysaccharide-degrading members of the
RT family Flavobacteriaceae.";
RL J. Bacteriol. 193:4545-4546(2011).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002825; AEH00857.1; -; Genomic_DNA.
DR RefSeq; WP_013869637.1; NC_015638.1.
DR AlphaFoldDB; F6GG20; -.
DR STRING; 983544.Lacal_1009; -.
DR KEGG; lan:Lacal_1009; -.
DR eggNOG; COG0319; Bacteria.
DR HOGENOM; CLU_106710_3_3_10; -.
DR OrthoDB; 9811984at2; -.
DR Proteomes; UP000008297; 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:0006508; P:proteolysis; IEA:UniProtKB-KW.
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 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.
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}; Metalloprotease {ECO:0000313|EMBL:AEH00857.1};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_00009};
KW Protease {ECO:0000313|EMBL:AEH00857.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008297};
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 136 AA; 16034 MW; 285F78C2CAD60E97 CRC64;
MISFNYENNF KLPNEAKIST WISSVILQEN CIEEEINYVF CDDEYLHKLN VEFLNHDTLT
DIISFDYSVG KNLQGDIFIS TERVEDNAKD FNVSFETELQ RVLVHGILHY CGYKDKSDSE
AKLMREKENF YLNLLK
//
