DRP35_STAAW
ID DRP35_STAAW Reviewed; 324 AA.
AC Q8NUH4;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Lactonase drp35;
DE EC=3.1.1.-;
GN Name=drp35; OrderedLocusNames=MW2608;
OS Staphylococcus aureus (strain MW2).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=196620;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MW2;
RX PubMed=12044378; DOI=10.1016/s0140-6736(02)08713-5;
RA Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y.,
RA Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
RT "Genome and virulence determinants of high virulence community-acquired
RT MRSA.";
RL Lancet 359:1819-1827(2002).
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; BA000033; BAB96473.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8NUH4; -.
DR SMR; Q8NUH4; -.
DR EnsemblBacteria; BAB96473; BAB96473; BAB96473.
DR KEGG; sam:MW2608; -.
DR HOGENOM; CLU_036110_2_0_9; -.
DR OMA; VWVLNHR; -.
DR Proteomes; UP000000418; 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_0000259750"
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; 36097 MW; 0E34B97250D463F4 CRC64;
MMSQQDLPTL FYSGKSNSAV PIISESELQT ITAEPWLEIS KKGLQLEGLN FDRQGQLFLL
DVFEGNIFKI NPETKEIKRP FVSHKANPAA IKIHKDGRLF VCYLGDFKST GGIFAATENG
DNIQDIIEDF STTYCIDDMV FDSKGGFYFT DFRGYSTNPL GGVYYVAPDF RTVTPIIQNI
SVANGIALSK DEKVLWVTET TANRLHRIAL EDDGVTIQPF GATIPYYFTG HEGPDSCCID
SDDNLYVAMY GQGRVLVFNK RGYPIGQILI PGRDEGHMLR STHPQFIPDT NQLIICSNDI
EMGGGSMLYT VNGFAKGHQS FQFQ