DRP35_STAHJ
ID DRP35_STAHJ Reviewed; 325 AA.
AC Q4L9R6;
DT 14-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Lactonase drp35;
DE EC=3.1.1.-;
GN Name=drp35; OrderedLocusNames=SH0300;
OS Staphylococcus haemolyticus (strain JCSC1435).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=279808;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCSC1435;
RX PubMed=16237012; DOI=10.1128/jb.187.21.7292-7308.2005;
RA Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C.,
RA Hiramatsu K.;
RT "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT extreme plasticity of its genome and the evolution of human-colonizing
RT staphylococcal species.";
RL J. Bacteriol. 187:7292-7308(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}.
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DR EMBL; AP006716; BAE03609.1; -; Genomic_DNA.
DR RefSeq; WP_011274629.1; NC_007168.1.
DR AlphaFoldDB; Q4L9R6; -.
DR SMR; Q4L9R6; -.
DR STRING; 279808.SH0300; -.
DR EnsemblBacteria; BAE03609; BAE03609; SH0300.
DR KEGG; sha:SH0300; -.
DR eggNOG; COG3386; Bacteria.
DR HOGENOM; CLU_036110_2_0_9; -.
DR OMA; VWVLNHR; -.
DR OrthoDB; 966287at2; -.
DR Proteomes; UP000000543; 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_0000259756"
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; 36131 MW; 5A87BC5C387114C6 CRC64;
MTNQSLPKLT YTGASKSAVP IISESELQTV TAEPWLKISD EGLQLEGLVF DRDHNLFLCE
VFGGKIFKVD IDTKKVSTAF QSTKQNPAAV KIHKDGRLFT CYLGDFESTG GIFATDEHGE
QFEEIISELN TEYCIDDMVF DSKGGFYFTD FRGYSTNPKG GVYYVSPDFK TVTPVIQNIS
VANGVALSTD EKILWVTETT TNRLHRIQLE DDGVTIAPFG ATIPYYFTGH EGPDSVCIDS
DDNLYVAMYG QGRVLVFNKR GYPIGQILMP GRDEGKMLRS THPQFIPGTN QLLICTNDIE
NDSEGGSMIY TVEAFAKGHE SYQFQ