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Database: UniProt
Entry: M1P2M0_BARAA
LinkDB: M1P2M0_BARAA
Original site: M1P2M0_BARAA 
ID   M1P2M0_BARAA            Unreviewed;       158 AA.
AC   M1P2M0;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 54.
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=BAnh1_01530 {ECO:0000313|EMBL:AGF74045.1};
OS   Bartonella australis (strain Aust/NH1).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Bartonellaceae; Bartonella.
OX   NCBI_TaxID=1094489 {ECO:0000313|EMBL:AGF74045.1, ECO:0000313|Proteomes:UP000011729};
RN   [1] {ECO:0000313|EMBL:AGF74045.1, ECO:0000313|Proteomes:UP000011729}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Aust/NH1 {ECO:0000313|EMBL:AGF74045.1,
RC   ECO:0000313|Proteomes:UP000011729};
RX   PubMed=23555299; DOI=10.1371/journal.pgen.1003393;
RA   Guy L., Nystedt B., Toft C., Zaremba-Niedzwiedzka K., Berglund E.C.,
RA   Granberg F., Naslund K., Eriksson A.S., Andersson S.G.;
RT   "A gene transfer agent and a dynamic repertoire of secretion systems hold
RT   the keys to the explosive radiation of the emerging pathogen Bartonella.";
RL   PLoS Genet. 9:E1003393-E1003393(2013).
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; CP003123; AGF74045.1; -; Genomic_DNA.
DR   RefSeq; WP_015397554.1; NC_020300.1.
DR   AlphaFoldDB; M1P2M0; -.
DR   STRING; 1094489.BAnh1_01530; -.
DR   KEGG; baus:BAnh1_01530; -.
DR   PATRIC; fig|1094489.3.peg.183; -.
DR   eggNOG; COG0319; Bacteria.
DR   HOGENOM; CLU_106710_0_0_5; -.
DR   OrthoDB; 9807740at2; -.
DR   Proteomes; UP000011729; 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; ENDORIBONUCLEASE YBEY, CHLOROPLASTIC; 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   Ribosome biogenesis {ECO:0000256|ARBA:ARBA00022517, ECO:0000256|HAMAP-
KW   Rule:MF_00009}; rRNA processing {ECO:0000256|HAMAP-Rule:MF_00009};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00009}.
FT   BINDING         118
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00009"
FT   BINDING         122
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00009"
FT   BINDING         128
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00009"
SQ   SEQUENCE   158 AA;  18157 MW;  7558F7B3118A6A7C CRC64;
     MIIIDITIQS AKWGSKGVLY DISEKVLTAT MQHFSFNKVT SELSLLFTDD ERMAQINARW
     RDKNKPTNVL SFPAFPLKAG QRPGPMLGDI IIARETVMRE AEKEGKSFRD HLTHMIVHGV
     LHLLGYDHET NDEADQMEEL EREILRKLSI KDPYTELC
//
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