PHLC_STAAU
ID PHLC_STAAU Reviewed; 330 AA.
AC P09978;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 25-MAY-2022, entry version 119.
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; Synonyms=plc;
OS Staphylococcus aureus.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1280;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=CN6708;
RX PubMed=1830359; DOI=10.1111/j.1365-2958.1991.tb00768.x;
RA Coleman D., Knights J., Russell R., Shanley D., Birkbeck T.H., Dougan G.,
RA Charles I.;
RT "Insertional inactivation of the Staphylococcus aureus beta-toxin by
RT bacteriophage phi 13 occurs by site- and orientation-specific integration
RT of the phi 13 genome.";
RL Mol. Microbiol. 5:933-939(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7941863;
RA Katerov V.E., Golubkov V.I., Totolian A.A., Shalen K., Ensen L., Mikula I.,
RA Smola I.;
RT "The cloning and expression of the gene for Staphylococcus aureus beta-
RT hemolysin.";
RL Zh. Mikrobiol. Epidemiol. Immunobiol. 3:28-33(1994).
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 (By similarity).
CC {ECO:0000250}.
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 -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the neutral sphingomyelinase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB32218.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA43885.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X61716; CAA43885.1; ALT_INIT; Genomic_DNA.
DR EMBL; S72497; AAB32218.1; ALT_INIT; Genomic_DNA.
DR PIR; S15324; S15324.
DR RefSeq; WP_000239607.1; NZ_WWCF01000081.1.
DR PDB; 3I5V; X-ray; 2.80 A; A/B/C/D=35-330.
DR PDBsum; 3I5V; -.
DR AlphaFoldDB; P09978; -.
DR SMR; P09978; -.
DR DIP; DIP-59362N; -.
DR OMA; WGQDHRA; -.
DR EvolutionaryTrace; P09978; -.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
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 3D-structure; Cytolysis; Disulfide bond; Hemolysis; Hydrolase; Signal;
KW Toxin; Virulence.
FT SIGNAL 1..34
FT /evidence="ECO:0000250"
FT CHAIN 35..330
FT /note="Phospholipase C"
FT /id="PRO_0000019903"
FT DISULFID 155..191
FT /evidence="ECO:0000255"
FT STRAND 45..49
FT /evidence="ECO:0007829|PDB:3I5V"
FT TURN 55..57
FT /evidence="ECO:0007829|PDB:3I5V"
FT HELIX 63..71
FT /evidence="ECO:0007829|PDB:3I5V"
FT STRAND 74..78
FT /evidence="ECO:0007829|PDB:3I5V"
FT STRAND 80..85
FT /evidence="ECO:0007829|PDB:3I5V"
FT HELIX 90..100
FT /evidence="ECO:0007829|PDB:3I5V"
FT TURN 101..103
FT /evidence="ECO:0007829|PDB:3I5V"
FT TURN 111..113
FT /evidence="ECO:0007829|PDB:3I5V"
FT STRAND 119..124
FT /evidence="ECO:0007829|PDB:3I5V"
FT STRAND 136..141
FT /evidence="ECO:0007829|PDB:3I5V"
FT STRAND 143..150
FT /evidence="ECO:0007829|PDB:3I5V"
FT HELIX 156..160
FT /evidence="ECO:0007829|PDB:3I5V"
FT STRAND 164..172
FT /evidence="ECO:0007829|PDB:3I5V"
FT STRAND 175..183
FT /evidence="ECO:0007829|PDB:3I5V"
FT HELIX 195..212
FT /evidence="ECO:0007829|PDB:3I5V"
FT TURN 213..215
FT /evidence="ECO:0007829|PDB:3I5V"
FT STRAND 222..227
FT /evidence="ECO:0007829|PDB:3I5V"
FT STRAND 232..234
FT /evidence="ECO:0007829|PDB:3I5V"
FT HELIX 235..243
FT /evidence="ECO:0007829|PDB:3I5V"
FT STRAND 250..253
FT /evidence="ECO:0007829|PDB:3I5V"
FT TURN 260..262
FT /evidence="ECO:0007829|PDB:3I5V"
FT HELIX 264..269
FT /evidence="ECO:0007829|PDB:3I5V"
FT STRAND 279..284
FT /evidence="ECO:0007829|PDB:3I5V"
FT STRAND 291..297
FT /evidence="ECO:0007829|PDB:3I5V"
FT STRAND 305..307
FT /evidence="ECO:0007829|PDB:3I5V"
FT STRAND 314..316
FT /evidence="ECO:0007829|PDB:3I5V"
FT STRAND 319..322
FT /evidence="ECO:0007829|PDB:3I5V"
FT STRAND 325..329
FT /evidence="ECO:0007829|PDB:3I5V"
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
