PHL2_BACCE
ID PHL2_BACCE Reviewed; 333 AA.
AC P11889;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 25-MAY-2022, entry version 115.
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=IAM 1208;
RX PubMed=2841128; DOI=10.1111/j.1432-1033.1988.tb14186.x;
RA Yamada A., Tsukagoshi N., Udaka S., Sasaki T., Makino S., Nakamura S.,
RA Little C., Tomita M., Ikezawa H.;
RT "Nucleotide sequence and expression in Escherichia coli of the gene coding
RT for sphingomyelinase of Bacillus cereus.";
RL Eur. J. Biochem. 175:213-220(1988).
RN [2]
RP PROTEIN SEQUENCE OF 28-41.
RC STRAIN=1230-88;
RX PubMed=8319899; DOI=10.1111/j.1574-6968.1993.tb06301.x;
RA Granum P.E., Nissen H.;
RT "Sphingomyelinase is part of the 'enterotoxin complex' produced by Bacillus
RT cereus.";
RL FEMS Microbiol. Lett. 110:97-100(1993).
RN [3]
RP SECONDARY STRUCTURE.
RX PubMed=2127932; DOI=10.1093/oxfordjournals.jbchem.a123285;
RA Tomita M., Nakai K., Yamada A., Taguchi R., Ikezawa H.;
RT "Secondary structure of sphingomyelinase from Bacillus cereus.";
RL J. Biochem. 108:811-815(1990).
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}.
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DR EMBL; X12711; CAA31214.1; -; Genomic_DNA.
DR PIR; B32042; B32042.
DR PIR; S01130; S01130.
DR PDB; 2DDR; X-ray; 1.40 A; A/B/C/D=28-333.
DR PDB; 2DDS; X-ray; 1.80 A; A/B/C/D=28-333.
DR PDB; 2DDT; X-ray; 1.80 A; A/B=28-333.
DR PDB; 2UYR; X-ray; 2.40 A; X=28-333.
DR PDBsum; 2DDR; -.
DR PDBsum; 2DDS; -.
DR PDBsum; 2DDT; -.
DR PDBsum; 2UYR; -.
DR AlphaFoldDB; P11889; -.
DR SMR; P11889; -.
DR BindingDB; P11889; -.
DR BRENDA; 3.1.4.12; 648.
DR SABIO-RK; P11889; -.
DR EvolutionaryTrace; P11889; -.
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 1: Evidence at protein level;
KW 3D-structure; Cytolysis; Direct protein sequencing; Disulfide bond;
KW Hemolysis; Hydrolase; Secreted; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000269|PubMed:8319899"
FT CHAIN 28..333
FT /note="Sphingomyelinase C"
FT /id="PRO_0000019900"
FT DISULFID 150..186
FT /evidence="ECO:0000250"
FT CONFLICT 33
FT /note="Q -> E (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 36..46
FT /evidence="ECO:0007829|PDB:2DDR"
FT TURN 49..51
FT /evidence="ECO:0007829|PDB:2DDR"
FT HELIX 57..66
FT /evidence="ECO:0007829|PDB:2DDR"
FT STRAND 74..81
FT /evidence="ECO:0007829|PDB:2DDR"
FT HELIX 84..94
FT /evidence="ECO:0007829|PDB:2DDR"
FT TURN 95..97
FT /evidence="ECO:0007829|PDB:2DDR"
FT STRAND 113..119
FT /evidence="ECO:0007829|PDB:2DDR"
FT STRAND 122..126
FT /evidence="ECO:0007829|PDB:2UYR"
FT STRAND 131..136
FT /evidence="ECO:0007829|PDB:2DDR"
FT STRAND 138..145
FT /evidence="ECO:0007829|PDB:2DDR"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:2DDR"
FT STRAND 159..167
FT /evidence="ECO:0007829|PDB:2DDR"
FT STRAND 170..178
FT /evidence="ECO:0007829|PDB:2DDR"
FT HELIX 184..186
FT /evidence="ECO:0007829|PDB:2DDR"
FT HELIX 191..209
FT /evidence="ECO:0007829|PDB:2DDR"
FT STRAND 217..222
FT /evidence="ECO:0007829|PDB:2DDR"
FT TURN 228..230
FT /evidence="ECO:0007829|PDB:2DDR"
FT HELIX 237..245
FT /evidence="ECO:0007829|PDB:2DDR"
FT STRAND 251..254
FT /evidence="ECO:0007829|PDB:2DDR"
FT TURN 261..263
FT /evidence="ECO:0007829|PDB:2DDR"
FT HELIX 265..270
FT /evidence="ECO:0007829|PDB:2DDR"
FT STRAND 280..285
FT /evidence="ECO:0007829|PDB:2DDR"
FT STRAND 292..298
FT /evidence="ECO:0007829|PDB:2DDR"
FT STRAND 306..310
FT /evidence="ECO:0007829|PDB:2DDR"
FT STRAND 313..317
FT /evidence="ECO:0007829|PDB:2DDR"
FT STRAND 320..323
FT /evidence="ECO:0007829|PDB:2UYR"
FT STRAND 326..331
FT /evidence="ECO:0007829|PDB:2DDR"
SQ SEQUENCE 333 AA; 36873 MW; A48E01702B1CAB3D CRC64;
MKGKLLKGVL SLGVGLGALY SGTSAQAEAS TNQNDTLKVM THNVYMLSTN LYPNWGQTER
ADLIGAADYI KNQDVVILNE VFDNSASDRL LGNLKKEYPN QTAVLGRSSG SEWDKTLGNY
SSSTPEDGGV AIVSKWPIAE KIQYVFAKGC GPDNLSNKGF VYTKIKKNDR FVHVIGTHLQ
AEDSMCGKTS PASVRTNQLK EIQDFIKNKN IPNNEYVLIG GDMNVNKINA ENNNDSEYAS
MFKTLNASVP SYTGHTATWD ATTNSIAKYN FPDSPAEYLD YIIASKDHAN PSYIENKVLQ
PKSPQWTVTS WFQKYTYNDY SDDYPVEATI SMK
