ID   PHLC_STAA8              Reviewed;         330 AA.
AC   Q2FWP1; Q2FWW0;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 2.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=Phospholipase C;
DE            EC=3.1.4.3;
DE   AltName: Full=Beta-hemolysin;
DE   AltName: Full=Beta-toxin;
DE   AltName: Full=Sphingomyelinase;
DE            Short=SMase;
DE   Flags: Precursor;
GN   Name=hlb; OrderedLocusNames=SAOUHSC_02163/SAOUHSC_02240;
OS   Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 8325 / PS 47;
RA   Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT   "The Staphylococcus aureus NCTC 8325 genome.";
RL   (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL   Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL   D.C. (2006).
RN   [2]
RP   PROTEIN SEQUENCE OF 35-53, AND CHARACTERIZATION.
RX   PubMed=8914839; DOI=10.1006/abbi.1996.0486;
RA   Dziewanowska K., Edwards V.M., Deringer J.R., Bohach G.A., Guerra D.J.;
RT   "Comparison of the beta-toxins from Staphylococcus aureus and
RT   Staphylococcus intermedius.";
RL   Arch. Biochem. Biophys. 335:102-108(1996).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND INDUCTION.
RC   STRAIN=RN4220;
RX   PubMed=20472795; DOI=10.1128/jb.01452-09;
RA   Sibbald M.J., Winter T., van der Kooi-Pol M.M., Buist G., Tsompanidou E.,
RA   Bosma T., Schafer T., Ohlsen K., Hecker M., Antelmann H., Engelmann S.,
RA   van Dijl J.M.;
RT   "Synthetic effects of secG and secY2 mutations on exoproteome biogenesis in
RT   Staphylococcus aureus.";
RL   J. Bacteriol. 192:3788-3800(2010).
CC   -!- FUNCTION: Bacterial hemolysins are exotoxins that attack blood cell
CC       membranes and cause cell rupture. Beta-hemolysin is a phospholipase C
CC       with specific activity toward sphingomyelins. Has a high specificity
CC       for sphingomyelin, hydrolyzes lysophosphatidylcholine at a much lower
CC       rate, but has no activity towards phosphatidylcholine,
CC       phosphatidylethanolamine, or phosphatidylserine.
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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 6.5-7.5.;
CC   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20472795}.
CC   -!- INDUCTION: Less protein is secreted in a secG or double secG/secY2
CC       mutant (at protein level). {ECO:0000269|PubMed:20472795}.
CC   -!- SIMILARITY: Belongs to the neutral sphingomyelinase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABD31209.1; Type=Miscellaneous discrepancy; Note=Integration of phage DNA that disrupted the sequence.; Evidence={ECO:0000305};
CC       Sequence=ABD31281.1; Type=Miscellaneous discrepancy; Note=Integration of phage DNA that disrupted the sequence.; Evidence={ECO:0000305};
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DR   EMBL; CP000253; ABD31209.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP000253; ABD31281.1; ALT_SEQ; Genomic_DNA.
DR   AlphaFoldDB; Q2FWP1; -.
DR   SMR; Q2FWP1; -.
DR   STRING; 1280.SAXN108_2108; -.
DR   EnsemblBacteria; ABD31209; ABD31209; SAOUHSC_02163.
DR   EnsemblBacteria; ABD31281; ABD31281; SAOUHSC_02240.
DR   eggNOG; COG3568; Bacteria.
DR   HOGENOM; CLU_196849_0_0_9; -.
DR   Proteomes; UP000008816; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0034480; F:phosphatidylcholine phospholipase C activity; IEA:UniProtKB-EC.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR   CDD; cd09078; nSMase; 1.
DR   Gene3D; 3.60.10.10; -; 1.
DR   InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR   InterPro; IPR005135; Endo/exonuclease/phosphatase.
DR   InterPro; IPR017766; Sphingomyelinase/PLipase_C.
DR   Pfam; PF03372; Exo_endo_phos; 1.
DR   SUPFAM; SSF56219; SSF56219; 1.
DR   TIGRFAMs; TIGR03395; sphingomy; 1.
PE   1: Evidence at protein level;
KW   Cytolysis; Direct protein sequencing; Disulfide bond; Hemolysis; Hydrolase;
KW   Reference proteome; Secreted; Signal; Toxin; Virulence.
FT   SIGNAL          1..34
FT                   /evidence="ECO:0000255"
FT   CHAIN           35..330
FT                   /note="Phospholipase C"
FT                   /id="PRO_0000247956"
FT   DISULFID        155..191
FT                   /evidence="ECO:0000255"
FT   CONFLICT        51
FT                   /note="Y -> T (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   330 AA;  37238 MW;  9F4148E23091020D CRC64;
     MVKKTKSNSL KKVATLALAN LLLVGALTDN SAKAESKKDD TDLKLVSHNV YMLSTVLYPN
     WGQYKRADLI GQSSYIKNND VVIFNEAFDN GASDKLLSNV KKEYPYQTPV LGRSQSGWDK
     TEGSYSSTVA EDGGVAIVSK YPIKEKIQHV FKSGCGFDND SNKGFVYTKI EKNGKNVHVI
     GTHTQSEDSR CGAGHDRKIR AEQMKEISDF VKKKNIPKDE TVYIGGDLNV NKGTPEFKDM
     LKNLNVNDVL YAGHNSTWDP QSNSIAKYNY PNGKPEHLDY IFTDKDHKQP KQLVNEVVTE
     KPKPWDVYAF PYYYVYNDFS DHYPIKAYSK