ID   DRP35_STAAC             Reviewed;         324 AA.
AC   Q5HCK9;
DT   14-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 2.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Lactonase drp35;
DE            EC=3.1.1.-;
GN   Name=drp35; OrderedLocusNames=SACOL2712;
OS   Staphylococcus aureus (strain COL).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93062;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=COL;
RX   PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA   Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA   Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA   Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA   Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA   Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA   Fraser C.M.;
RT   "Insights on evolution of virulence and resistance from the complete genome
RT   analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT   a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT   strain.";
RL   J. Bacteriol. 187:2426-2438(2005).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAW37360.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000046; AAW37360.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; Q5HCK9; -.
DR   SMR; Q5HCK9; -.
DR   EnsemblBacteria; AAW37360; AAW37360; SACOL2712.
DR   KEGG; sac:SACOL2712; -.
DR   HOGENOM; CLU_036110_2_0_9; -.
DR   Proteomes; UP000000530; 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..324
FT                   /note="Lactonase drp35"
FT                   /id="PRO_0000259746"
FT   ACT_SITE        235
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255"
FT   BINDING         47
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         109
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         111
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         129
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         132
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         134
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         137
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         184
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"
FT   BINDING         236
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   324 AA;  35964 MW;  A2C94FCB38F2F4AC CRC64;
     MMSQQDLPTL FYSGKSNSAV PIISESELQT ITAEPWLEIS KKGLQLEGLN FDRQGQLFLL
     DVFEGNIFKI NPETKEIKRP FVSHKANPAA IKIHKDGRLF VCYLGDFKST GGIFAATENG
     DNLQDIIEDL STAYCIDDMV FDSKGGFYFT DFRGYSTNPL GGVYYVSPDF RTVTPIIQNI
     SVANGIALST DEKVLWVTET TANRLHRIAL EDDGVTIQPF GATIPYYFTG HEGPDSCCID
     SDDNLYVAMY GQGRVLVFNK RGYPIGQILI PGRDEGHMLR STHPQFIPGT NQLIICSNDI
     EMGGGSMLYT VNGFAKGHQS FQFQ