ID   DRP35_STAES             Reviewed;         325 AA.
AC   Q8CQ97;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Lactonase drp35;
DE            EC=3.1.1.-;
GN   Name=drp35; OrderedLocusNames=SE_0263;
OS   Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12228 / FDA PCI 1200;
RX   PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA   Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA   Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA   Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT   "Genome-based analysis of virulence genes in a non-biofilm-forming
RT   Staphylococcus epidermidis strain (ATCC 12228).";
RL   Mol. Microbiol. 49:1577-1593(2003).
CC   -!- FUNCTION: Exhibits lactonase activity. Acts in cells with perturbed
CC       membrane integrity and is possibly related to the membrane homeostasis
CC       (By similarity). {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC       Note=Binds 2 Ca(2+) ions per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SMP-30/CGR1 family. {ECO:0000305}.
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DR   EMBL; AE015929; AAO03860.1; -; Genomic_DNA.
DR   RefSeq; NP_763818.1; NC_004461.1.
DR   RefSeq; WP_001829433.1; NZ_WBME01000037.1.
DR   AlphaFoldDB; Q8CQ97; -.
DR   SMR; Q8CQ97; -.
DR   STRING; 176280.SE_0263; -.
DR   EnsemblBacteria; AAO03860; AAO03860; SE_0263.
DR   GeneID; 50017657; -.
DR   KEGG; sep:SE_0263; -.
DR   PATRIC; fig|176280.10.peg.241; -.
DR   eggNOG; COG3386; Bacteria.
DR   HOGENOM; CLU_036110_2_0_9; -.
DR   OMA; VWVLNHR; -.
DR   Proteomes; UP000001411; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 2.120.10.30; -; 1.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR013658; SGL.
DR   Pfam; PF08450; SGL; 1.
PE   3: Inferred from homology;
KW   Calcium; Cytoplasm; Hydrolase; Metal-binding.
FT   CHAIN           1..325
FT                   /note="Lactonase drp35"
FT                   /id="PRO_0000259754"
FT   ACT_SITE        234
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255"
FT   BINDING         46
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         108
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         110
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         128
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         131
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         133
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         136
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         183
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         234
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         235
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   325 AA;  36143 MW;  5BF377C7E6A774C8 CRC64;
     MANQKLPTLK YTGKSESAVP IVSESELQTV TAEPWVKISD KGLQLEGLNF NREGQLFLLD
     VFEGNIFKVN PATKEVTTKF QSVKDNPAAI KVHKDGRLFI CYLGDFKTTG GIFATTEKGE
     QIEEIISDLN TEYCIDDMVF DSKGGFYFTD FRGYSTQPLG GVYYVDPDFK TVTPIIQNIS
     VANGIALSTD EKVLWVTETT TNRLHRIALE NDGVTIAPFG ATIPYYFTGH EGPDSCCIDS
     DDNLYVAMYG QGRVLVFNKR GYPIGQILMP GRDDGKMLRT THPQFIPGTN QLIICTNDIE
     NHSEGGSMLY TVNGFAKGYE SYQFQ