ID   DRP35_STAAU             Reviewed;         324 AA.
AC   Q9S0S3;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 2.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=Lactonase drp35;
DE            EC=3.1.1.-;
GN   Name=drp35;
OS   Staphylococcus aureus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC   STRAIN=912;
RX   PubMed=10529367; DOI=10.1006/bbrc.1999.1388;
RA   Murakami H., Matsumaru H., Kanamori M., Hayashi H., Ohta T.;
RT   "Cell wall-affecting antibiotics induce expression of a novel gene, drp35,
RT   in Staphylococcus aureus.";
RL   Biochem. Biophys. Res. Commun. 264:348-351(1999).
CC   -!- FUNCTION: Exhibits lactonase activity. Acts in cells with perturbed
CC       membrane integrity and is possibly related to the membrane homeostasis.
CC       Contributes to bacitracin resistance (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   -!- INDUCTION: Induced by cell wall-affecting antibiotics such as
CC       oxacillin, vancomycin, fosfomycin, and bacitracin.
CC       {ECO:0000269|PubMed:10529367}.
CC   -!- SIMILARITY: Belongs to the SMP-30/CGR1 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA86894.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AB030228; BAA86894.1; ALT_INIT; Genomic_DNA.
DR   PIR; JC7119; JC7119.
DR   AlphaFoldDB; Q9S0S3; -.
DR   SMR; Q9S0S3; -.
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   GO; GO:0046677; P:response to antibiotic; 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   2: Evidence at transcript level;
KW   Antibiotic resistance; Calcium; Cytoplasm; Hydrolase; Metal-binding.
FT   CHAIN           1..324
FT                   /note="Lactonase drp35"
FT                   /id="PRO_0000259744"
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;  35978 MW;  A2CB3FCE38F2F4A9 CRC64;
     MMSQQDLPTL FYSGKSNSAV PIISESELQT ITAEPWLEIS KKGLQLEGLN FDRQGQLFLL
     DVFEGNIFKI NPETKEIKRP FVSHKANPAA IKIHKDGRLF VCYLGDFKST GGIFAATENG
     DNLQDIIEDL STAYCIDDMV FDSKGGFYFT DFRGYSTNPL GGVYYVSPDF RTVTPIIQNI
     SVANGIALST DEKVLWVTET TAKRLHRIAL EDDGVTIQPF GATIPYYFTG HEGPDSCCID
     SDDNLYVAMY GQGRVLVFNK RGYPIGQILI PGRDEGHMLR STHPQFIPGT NQLIICSNDI
     EMGGGSMLYT VNGFAKGHQS FQFQ