ID   PHL3_BACCE              Reviewed;         333 AA.
AC   P33377;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   02-SEP-2026, entry version 102.
DE   RecName: Full=Sphingomyelinase C;
DE            Short=SMase;
DE            EC=3.1.4.12;
DE   AltName: Full=Cereolysin B;
DE   AltName: Full=SMPLC;
DE   AltName: Full=Sphingomyelin phosphodiesterase;
DE   Flags: Precursor;
GN   Name=cerB;
OS   Bacillus cereus.
OC   Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae;
OC   Bacillus; 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).
CC   -!- FUNCTION: Required, with sphingomyelinase, to effect target cell lysis
CC       (hemolysis).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a sphingomyelin + H2O = phosphocholine + an N-acylsphing-4-
CC         enine + H(+); Xref=Rhea:RHEA:19253, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17636, ChEBI:CHEBI:52639,
CC         ChEBI:CHEBI:295975; EC=3.1.4.12;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC   -!- ACTIVITY REGULATION: Activated by cobalt and manganese ions.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- PTM: The N-terminus is blocked.
CC   -!- SIMILARITY: Belongs to the neutral sphingomyelinase family.
CC       {ECO:0000305}.
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DR   EMBL; M24149; AAA91820.1; -; Genomic_DNA.
DR   AlphaFoldDB; P33377; -.
DR   SMR; P33377; -.
DR   SABIO-RK; P33377; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004620; F:glycerophospholipase activity; IEA:TreeGrafter.
DR   GO; GO:0004767; F:sphingomyelin phosphodiesterase activity; IEA:UniProtKB-EC.
DR   CDD; cd09078; nSMase; 1.
DR   FunFam; 3.60.10.10:FF:000063; Sphingomyelinase C; 1.
DR   Gene3D; 3.60.10.10; Endonuclease/exonuclease/phosphatase; 1.
DR   InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR   InterPro; IPR005135; Endo/exonuclease/phosphatase.
DR   InterPro; IPR038772; Sph/SMPD2-like.
DR   InterPro; IPR017766; Sphingomyelinase/PLipase_C.
DR   NCBIfam; TIGR03395; sphingomy; 1.
DR   PANTHER; PTHR16320:SF23; SPHINGOMYELINASE C 1; 1.
DR   PANTHER; PTHR16320; SPHINGOMYELINASE FAMILY MEMBER; 1.
DR   Pfam; PF03372; Exo_endo_phos; 1.
DR   SUPFAM; SSF56219; DNase I-like; 1.
PE   3: Inferred from homology;
KW   Cytolysis; Disulfide bond; Hemolysis; Hydrolase; Secreted; Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..333
FT                   /note="Sphingomyelinase C"
FT                   /id="PRO_0000019901"
FT   DISULFID        150..186
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   333 AA;  36821 MW;  05F8AEA5ECC4A3B8 CRC64;
     MKGKLLKGVL SLGVGLGALY SGTSAQAEAS TNQNDTLKVM THNVYMLSTN LYPNWGQTER
     ADLFGAADYI KNQDVVILNE VFDNSASDRL LGNLKKEYPN QTAVLGRSSG SEWDKTLGNY
     SSSTPEDGGV AIVSKWPIAE KIQYVFAKGC GPDNLSNKGF VYTKIKKNDR FVHVIGTHLQ
     AEDSMCGKTS PASVRTNQLK EIQDFIKNKN IPNNEYVLIG GDMNVNKINA ENNNDSEYAS
     MFKTLNASVP SYTGHTATWD ATTNSIAKYN FPDSLAEYLD YIIASKDHAN PSYIENKVLQ
     PKSPQWTVTS WFKNIRIMIT LIIIQVEATI SMK
//