ID   Y2729_BACC1             Reviewed;         173 AA.
AC   Q737C1;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Putative metal-dependent hydrolase BCE_2729 {ECO:0000255|HAMAP-Rule:MF_01256};
DE            EC=3.-.-.- {ECO:0000255|HAMAP-Rule:MF_01256};
GN   OrderedLocusNames=BCE_2729;
OS   Bacillus cereus (strain ATCC 10987 / NRS 248).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=222523;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10987 / NRS 248;
RX   PubMed=14960714; DOI=10.1093/nar/gkh258;
RA   Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L.,
RA   Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F.,
RA   Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D.;
RT   "The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic
RT   adaptations and a large plasmid related to Bacillus anthracis pXO1.";
RL   Nucleic Acids Res. 32:977-988(2004).
CC   -!- FUNCTION: Possible metal-dependent hydrolase. {ECO:0000255|HAMAP-
CC       Rule:MF_01256}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01256};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01256};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01256}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01256}.
CC   -!- SIMILARITY: Belongs to the metal hydrolase YfiT family.
CC       {ECO:0000255|HAMAP-Rule:MF_01256}.
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DR   EMBL; AE017194; AAS41641.1; -; Genomic_DNA.
DR   RefSeq; WP_000999078.1; NC_003909.8.
DR   AlphaFoldDB; Q737C1; -.
DR   SMR; Q737C1; -.
DR   EnsemblBacteria; AAS41641; AAS41641; BCE_2729.
DR   GeneID; 59159927; -.
DR   KEGG; bca:BCE_2729; -.
DR   HOGENOM; CLU_105789_1_0_9; -.
DR   OMA; GWTIRQV; -.
DR   Proteomes; UP000002527; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.20.120.450; -; 1.
DR   HAMAP; MF_01256; YfiT_hydrol; 1.
DR   InterPro; IPR024775; DinB-like.
DR   InterPro; IPR034660; DinB/YfiT-like.
DR   InterPro; IPR023774; Put_metal_dep_hydrolase_YfiT.
DR   Pfam; PF12867; DinB_2; 1.
DR   SUPFAM; SSF109854; SSF109854; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Hydrolase; Metal-binding; Zinc.
FT   CHAIN           1..173
FT                   /note="Putative metal-dependent hydrolase BCE_2729"
FT                   /id="PRO_0000162367"
FT   BINDING         65
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01256"
FT   BINDING         156
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01256"
FT   BINDING         160
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01256"
SQ   SEQUENCE   173 AA;  20441 MW;  2197E16D59692183 CRC64;
     MNDLRYPIGQ FTYKRPITEE MIDTWIQEIE DLPNELTKAI KDLDQKQLDT PYRVGGWTVR
     QVVHHVVDSH MNSYIRFKLA LTEKNPTIKP YKEEKWAELP DSKLPVDVSL VMLESLHKRW
     VNLLYSLELE DLEKTFNHPE TGETKLAVAI GLYAWHGRHH TAHITSLRKR LNW