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P11889 (PHL2_BACCE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Sphingomyelinase C

Short name=SMase
EC=3.1.4.12
Alternative name(s):
Cereolysin B
SMPLC
Sphingomyelin phosphodiesterase
Gene names
Name:sph
OrganismBacillus cereus
Taxonomic identifier1396 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length333 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Required, with sphingomyelinase, to effect target cell lysis (hemolysis).

Catalytic activity

Sphingomyelin + H2O = N-acylsphingosine + phosphocholine.

Cofactor

Magnesium.

Enzyme regulation

Activated by cobalt and manganese ions.

Subcellular location

Secreted.

Sequence similarities

Belongs to the neutral sphingomyelinase family.

Ontologies

Keywords
   Biological processCytolysis
Hemolysis
   Cellular componentSecreted
   DomainSignal
   Molecular functionHydrolase
   PTMDisulfide bond
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processhemolysis in other organism

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionsphingomyelin phosphodiesterase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727 Ref.2
Chain28 – 333306Sphingomyelinase C
PRO_0000019900

Amino acid modifications

Disulfide bond150 ↔ 186 By similarity

Experimental info

Sequence conflict331Q → E AA sequence Ref.2

Secondary structure

...................................................... 333
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P11889 [UniParc].

Last modified October 1, 1989. Version 1.
Checksum: A48E01702B1CAB3D

FASTA33336,873
        10         20         30         40         50         60 
MKGKLLKGVL SLGVGLGALY SGTSAQAEAS TNQNDTLKVM THNVYMLSTN LYPNWGQTER 

        70         80         90        100        110        120 
ADLIGAADYI KNQDVVILNE VFDNSASDRL LGNLKKEYPN QTAVLGRSSG SEWDKTLGNY 

       130        140        150        160        170        180 
SSSTPEDGGV AIVSKWPIAE KIQYVFAKGC GPDNLSNKGF VYTKIKKNDR FVHVIGTHLQ 

       190        200        210        220        230        240 
AEDSMCGKTS PASVRTNQLK EIQDFIKNKN IPNNEYVLIG GDMNVNKINA ENNNDSEYAS 

       250        260        270        280        290        300 
MFKTLNASVP SYTGHTATWD ATTNSIAKYN FPDSPAEYLD YIIASKDHAN PSYIENKVLQ 

       310        320        330 
PKSPQWTVTS WFQKYTYNDY SDDYPVEATI SMK 

« Hide

References

[1]"Nucleotide sequence and expression in Escherichia coli of the gene coding for sphingomyelinase of Bacillus cereus."
Yamada A., Tsukagoshi N., Udaka S., Sasaki T., Makino S., Nakamura S., Little C., Tomita M., Ikezawa H.
Eur. J. Biochem. 175:213-220(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: IAM 1208.
[2]"Sphingomyelinase is part of the 'enterotoxin complex' produced by Bacillus cereus."
Granum P.E., Nissen H.
FEMS Microbiol. Lett. 110:97-100(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 28-41.
Strain: 1230-88.
[3]"Secondary structure of sphingomyelinase from Bacillus cereus."
Tomita M., Nakai K., Yamada A., Taguchi R., Ikezawa H.
J. Biochem. 108:811-815(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: SECONDARY STRUCTURE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X12711 Genomic DNA. Translation: CAA31214.1.
PIRB32042.
S01130.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2DDRX-ray1.40A/B/C/D28-333[»]
2DDSX-ray1.80A/B/C/D28-333[»]
2DDTX-ray1.80A/B28-333[»]
2UYRX-ray2.40X28-333[»]
ProteinModelPortalP11889.
SMRP11889. Positions 34-332.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKP11889.

Family and domain databases

Gene3D3.60.10.10. 1 hit.
InterProIPR005135. Endo/exonuclease/phosphatase.
IPR017766. Sphingomyelinase/PLipase_C.
[Graphical view]
PfamPF03372. Exo_endo_phos. 1 hit.
[Graphical view]
SUPFAMSSF56219. SSF56219. 1 hit.
TIGRFAMsTIGR03395. sphingomy. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP11889.

Entry information

Entry namePHL2_BACCE
AccessionPrimary (citable) accession number: P11889
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: July 9, 2014
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references