PHL1_BACCE
ID PHL1_BACCE Reviewed; 333 AA.
AC P09599;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 25-MAY-2022, entry version 105.
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=sph;
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=SE-1;
RX PubMed=2848222; DOI=10.1093/nar/16.21.10370;
RA Johansen T., Haugli F.B., Ikezawa H., Little C.;
RT "Bacillus cereus strain SE-1: nucleotide sequence of the sphingomyelinase C
RT gene.";
RL Nucleic Acids Res. 16:10370-10370(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=VKM B-164;
RX PubMed=8387306;
RA Kuzmin N.P., Gavrilenko I.V., Krukov V.M., Karpov A.V.;
RT "Nucleotide sequence of phospholipase C and sphingomyelinase genes from
RT Bacillus cereus BKM-B164.";
RL Bioorg. Khim. 19:133-138(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-188.
RC STRAIN=SE-1;
RX PubMed=3137122; DOI=10.1016/0378-1119(88)90466-0;
RA Johansen T., Holm T., Guddal P.H., Sletten K., Haugli F.B., Little C.;
RT "Cloning and sequencing of the gene encoding the phosphatidylcholine-
RT preferring phospholipase C of Bacillus cereus.";
RL Gene 65:293-304(1988).
CC -!- FUNCTION: Required, with sphingomyelinase, to effect target cell lysis
CC (hemolysis).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a sphingomyelin + H2O = an N-acylsphing-4-enine + H(+) +
CC phosphocholine; 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 -!- SIMILARITY: Belongs to the neutral sphingomyelinase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA45501.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X64141; CAA45503.1; -; Genomic_DNA.
DR EMBL; X12854; CAA31333.1; -; Genomic_DNA.
DR EMBL; X64140; CAA45501.1; ALT_INIT; Genomic_DNA.
DR PIR; S01950; S01950.
DR RefSeq; WP_000676778.1; NZ_MIFD01000014.1.
DR AlphaFoldDB; P09599; -.
DR SMR; P09599; -.
DR STRING; 1396.DJ87_4437; -.
DR GeneID; 59156455; -.
DR eggNOG; COG3568; Bacteria.
DR BRENDA; 3.1.4.12; 648.
DR SABIO-RK; P09599; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004767; F:sphingomyelin phosphodiesterase activity; IEA:UniProtKB-EC.
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 3: Inferred from homology;
KW Cytolysis; Disulfide bond; Hemolysis; Hydrolase; Secreted; Signal.
FT SIGNAL 1..27
FT CHAIN 28..333
FT /note="Sphingomyelinase C"
FT /id="PRO_0000019899"
FT DISULFID 150..186
FT /evidence="ECO:0000250"
SQ SEQUENCE 333 AA; 36949 MW; 035EF97D690C8378 CRC64;
MKGKLLKGVL SFGIGLGVLY GGSSVQADTS TDQNNTLKVM THNVYMLSTN LYPNWGQSQR
ADLIGAADYI KNQDVVILNE VFDNSASDRL LGNLKKEYPN QTAVLGRSNG NEWDKTLGSY
SSSTPEDGGV AIVSKWPIVE KIQYVFAKGC GPDNLSNKGF VYTKIKKNDR FVHVIGTHLQ
AEDSMCGKTS PASVRTNQLK EIQDFIKNKN IPNDEYVLFG GDMNVNKINA ENNSDSEYAS
MFKTLHASIP SYTGHTATWD ATTNSIAKYN FPDSPAEYLD YIIASKDHAN PSFIENKVLQ
PKSPQWTVTS WLKKYTYDDY SDHYPVAATI SMK
