ID   PHLD_BACCE              Reviewed;         283 AA.
AC   P33376;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Phospholipase C;
DE            Short=PLC;
DE            EC=3.1.4.3;
DE   AltName: Full=Cereolysin A;
DE   AltName: Full=Phosphatidylcholine cholinephosphohydrolase;
DE   Flags: Precursor;
GN   Name=cerA;
OS   Bacillus cereus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=1396;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=GP-4;
RX   PubMed=2536680; DOI=10.1128/jb.171.2.744-753.1989;
RA   Gilmore M.S., Cruz-Rodz A.L., Leimeister-Waechter M., Kreft J., Goebel W.;
RT   "A Bacillus cereus cytolytic determinant, cereolysin AB, which comprises
RT   the phospholipase C and sphingomyelinase genes: nucleotide sequence and
RT   genetic linkage.";
RL   J. Bacteriol. 171:744-753(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 50-142.
RA   Gilmore M.S., Gilmore K.S., Goebel W.;
RT   "A new strategy for ordered DNA sequencing based on a novel method for the
RT   rapid purification of near-milligram quantities of a cloned restriction
RT   fragment.";
RL   Gene Anal. Tech. 2:108-114(1985).
CC   -!- FUNCTION: Required, with sphingomyelinase, to effect target cell lysis
CC       (hemolysis).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1,2-diacyl-
CC         sn-glycerol + H(+) + phosphocholine; Xref=Rhea:RHEA:10604,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17815,
CC         ChEBI:CHEBI:57643, ChEBI:CHEBI:295975; EC=3.1.4.3;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC       Note=Binds 3 Zn(2+) ions per subunit.;
CC   -!- SUBUNIT: Monomer.
CC   -!- SIMILARITY: Belongs to the bacterial zinc-metallophospholipase C
CC       family. {ECO:0000255|PROSITE-ProRule:PRU00678}.
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DR   EMBL; M24149; AAA91819.1; -; Genomic_DNA.
DR   EMBL; M35411; AAA22524.1; -; Genomic_DNA.
DR   PIR; S18978; PS0197.
DR   AlphaFoldDB; P33376; -.
DR   SMR; P33376; -.
DR   GO; GO:0034480; F:phosphatidylcholine phospholipase C activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR   CDD; cd11009; Zn_dep_PLPC; 1.
DR   Gene3D; 1.10.575.10; -; 1.
DR   InterPro; IPR008947; PLipase_C/P1_nuclease_dom_sf.
DR   InterPro; IPR029002; PLPC/GPLD1.
DR   InterPro; IPR001531; Zn_PLipaseC.
DR   Pfam; PF00882; Zn_dep_PLPC; 1.
DR   PRINTS; PR00479; PRPHPHLPASEC.
DR   SMART; SM00770; Zn_dep_PLPC; 1.
DR   SUPFAM; SSF48537; SSF48537; 1.
DR   PROSITE; PS00384; PROKAR_ZN_DEPEND_PLPC_1; 1.
DR   PROSITE; PS51346; PROKAR_ZN_DEPEND_PLPC_2; 1.
PE   3: Inferred from homology;
KW   Cytolysis; Hemolysis; Hydrolase; Metal-binding; Signal; Zinc; Zymogen.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   PROPEP          25..38
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000023929"
FT   CHAIN           39..283
FT                   /note="Phospholipase C"
FT                   /id="PRO_0000023930"
FT   DOMAIN          39..283
FT                   /note="Zn-dependent PLC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00678"
FT   BINDING         39
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT   BINDING         52
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT   BINDING         93
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT   BINDING         107
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT   BINDING         156
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT   BINDING         160
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT   BINDING         160
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT   BINDING         166
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT   BINDING         180
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT   BINDING         184
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
SQ   SEQUENCE   283 AA;  32373 MW;  24D2E753402A6A44 CRC64;
     MKKKVLALGA AITLVAPLQS VAFAHENDGG QRFGVIPRWS AEDKHKEGVN SHLWIVNRAI
     DIMSRNTTLV KQDRVALLNE WRTELENGIY AADYENPYYD NSTFASHFYD PDNGKTYIPY
     AKQAKETGAK YFKLAGESYK NKDMKQAFFY LGLSLHYLGD VNQPMHAANF TNLSYPQGFH
     SKYENFVDTI KDNYKVTDGN GYWNWKGTNP EDWIHGAAVV AKQDYAGIVN DNTKDWFVRA
     AVSQEYADKW RAEVTPMTGK RLMDAQRVTA GYIQLWFDTY GNR