ID I4LQZ2_GARVA Unreviewed; 175 AA.
AC I4LQZ2;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 50.
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 ORFNames=CGSMWGv55152_05758 {ECO:0000313|EMBL:EIK79382.1};
OS Gardnerella vaginalis 55152.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Gardnerella.
OX NCBI_TaxID=698955 {ECO:0000313|EMBL:EIK79382.1, ECO:0000313|Proteomes:UP000005936};
RN [1] {ECO:0000313|EMBL:EIK79382.1, ECO:0000313|Proteomes:UP000005936}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=55152 {ECO:0000313|EMBL:EIK79382.1,
RC ECO:0000313|Proteomes:UP000005936};
RX PubMed=22609915; DOI=10.1128/JB.00056-12;
RA Ahmed A., Earl J., Retchless A., Hillier S., Rabe L., Cherpes T.,
RA Powell E., Janto B., Eutsey R., Hiller N.L., Boissy R., Dahlgreen M.,
RA Hall B., Costerton J., Post J.C., Hu F., Ehrlich G.;
RT "Comparative Genomic Analyses of 17 Clinical Isolates of Gardnerella
RT vaginalis Provide Evidence of Multiple Genetically Isolated Clades
RT Consistent with Subspeciation into Genovars.";
RL J. Bacteriol. 194:3922-3937(2012).
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:EIK79382.1}.
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DR EMBL; ADEQ01000017; EIK79382.1; -; Genomic_DNA.
DR RefSeq; WP_004122871.1; NZ_ADEQ01000017.1.
DR AlphaFoldDB; I4LQZ2; -.
DR PATRIC; fig|698955.3.peg.1125; -.
DR Proteomes; UP000005936; 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: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 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:EIK79382.1};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_00009};
KW Protease {ECO:0000313|EMBL:EIK79382.1};
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 115
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00009"
FT BINDING 119
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="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"
SQ SEQUENCE 175 AA; 19599 MW; C27DE92C9EDFB6B3 CRC64;
MSVEVMNETV WQIDPKIFSD LGMWVLQQMR VSVQSDLSIT FVDPEPIASL HEKWMDLEGP
TDVMSFPMDE LTPGSDDKVS EGMLGDLVIC PWVASQQAAA AGHSTMEEML LLTIHGMLHL
LGYDHTTPQE EKQMFGLQRQ LLLTFFAARS GELYDATLPA GAVNELEEYE KNHAK
//
