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Database: UniProt
Entry: E4SJT4_LACAR
LinkDB: E4SJT4_LACAR
Original site: E4SJT4_LACAR 
ID   E4SJT4_LACAR            Unreviewed;       174 AA.
AC   E4SJT4;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   27-MAR-2024, entry version 60.
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=LA2_06725 {ECO:0000313|EMBL:ADQ59286.1};
OS   Lactobacillus amylovorus (strain GRL 1112).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=695560 {ECO:0000313|EMBL:ADQ59286.1, ECO:0000313|Proteomes:UP000007033};
RN   [1] {ECO:0000313|EMBL:ADQ59286.1, ECO:0000313|Proteomes:UP000007033}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GRL 1112 {ECO:0000313|EMBL:ADQ59286.1,
RC   ECO:0000313|Proteomes:UP000007033};
RX   PubMed=21131492; DOI=10.1128/JB.01365-10;
RA   Kant R., Paulin L., Alatalo E., de Vos W.M., Palva A.;
RT   "Genome sequence of Lactobacillus amylovorus GRL1112.";
RL   J. Bacteriol. 193:789-790(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}.
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DR   EMBL; CP002338; ADQ59286.1; -; Genomic_DNA.
DR   RefSeq; WP_013438079.1; NC_014724.1.
DR   AlphaFoldDB; E4SJT4; -.
DR   KEGG; lam:LA2_06725; -.
DR   PATRIC; fig|695560.3.peg.1322; -.
DR   HOGENOM; CLU_106710_3_0_9; -.
DR   Proteomes; UP000007033; 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}; Metalloprotease {ECO:0000313|EMBL:ADQ59286.1};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_00009};
KW   Protease {ECO:0000313|EMBL:ADQ59286.1};
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         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         133
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00009"
FT   BINDING         139
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00009"
SQ   SEQUENCE   174 AA;  20176 MW;  149251EF3D1CEB02 CRC64;
     MDPIDITYND EVGFLDDKRR DWQDWIMKLL LLAKKEIGKD NNLEMSINFV DEDCSHEINL
     KYRDKDRPTD VISFAIEDGE DSIDLAAFED DPDFQEDIGD LFMCPSVIKR HSKEYGTGFD
     REFGYTVVHG FLHLNGYDHI KPDEAKEMFG IQGKVLEDYG LPLYPDQLDE GRGK
//
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