Y325_BUCBP
ID Y325_BUCBP Reviewed; 265 AA.
AC Q89AG7;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Uncharacterized metal-dependent hydrolase bbp_325 {ECO:0000305};
DE EC=3.1.-.- {ECO:0000305};
GN OrderedLocusNames=bbp_325;
OS Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=224915;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bp;
RX PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT "Reductive genome evolution in Buchnera aphidicola.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250|UniProtKB:P0AFQ7};
CC Note=Binds 2 divalent metal cations per subunit.
CC {ECO:0000250|UniProtKB:P0AFQ7};
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC TatD-type hydrolase family. {ECO:0000305}.
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DR EMBL; AE016826; AAO27047.1; -; Genomic_DNA.
DR RefSeq; WP_011091448.1; NC_004545.1.
DR AlphaFoldDB; Q89AG7; -.
DR SMR; Q89AG7; -.
DR STRING; 224915.bbp_325; -.
DR EnsemblBacteria; AAO27047; AAO27047; bbp_325.
DR GeneID; 56470864; -.
DR KEGG; bab:bbp_325; -.
DR eggNOG; COG0084; Bacteria.
DR HOGENOM; CLU_031506_4_0_6; -.
DR OMA; DGPYEYR; -.
DR OrthoDB; 915852at2; -.
DR Proteomes; UP000000601; Chromosome.
DR GO; GO:0004536; F:deoxyribonuclease activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd01310; TatD_DNAse; 1.
DR InterPro; IPR018228; DNase_TatD-rel_CS.
DR InterPro; IPR015991; Hydrolase_TatD-type.
DR InterPro; IPR032466; Metal_Hydrolase.
DR InterPro; IPR001130; TatD-like.
DR Pfam; PF01026; TatD_DNase; 1.
DR PIRSF; PIRSF005902; DNase_TatD; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
DR TIGRFAMs; TIGR00010; TIGR00010; 1.
DR PROSITE; PS01137; TATD_1; 1.
DR PROSITE; PS01091; TATD_3; 1.
PE 3: Inferred from homology;
KW Hydrolase; Metal-binding; Reference proteome.
FT CHAIN 1..265
FT /note="Uncharacterized metal-dependent hydrolase bbp_325"
FT /id="PRO_0000202004"
FT BINDING 7
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0AFQ7"
FT BINDING 9
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0AFQ7"
FT BINDING 95
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0AFQ7"
FT BINDING 95
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0AFQ7"
FT BINDING 131
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0AFQ7"
FT BINDING 156
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0AFQ7"
FT BINDING 206
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0AFQ7"
SQ SEQUENCE 265 AA; 30677 MW; 11D540CAEA377962 CRC64;
MFLIDSHCHL DLLNYNKIHT GIQDVLNKSK KKHVNVILTV STSIENFCYL LKFIKGNRNV
LLSCGIHPHY IPENKNEILK LKKYSNNEKV VAIGETGLDY YRNNDNKKLQ QILFREHIKT
SITLKKPLLI HTRNSINDTI NILKEENSKQ CIGVLHSFTE DMHSARILLN MGFYISFSGI
VTFKNSKIVH ETAKFVPIDR ILIETDSPYL SPVPYRGIEN QPAYLYDTML YIAQLKNMSP
ECFAIQTTKN FLKLFNLPSY FTNMS