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P33377 (PHL3_BACCE) Reviewed, UniProtKB/Swiss-Prot

Last modified October 19, 2011. Version 60. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:cerB
OrganismBacillus cereus
Taxonomic identifier1396 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length333 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

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

Catalytic activity

Sphingomyelin + H2O = N-acylsphingosine + choline phosphate.

Cofactor

Magnesium.

Enzyme regulation

Activated by cobalt and manganese ions.

Subcellular location

Secreted.

Post-translational modification

The N-terminus is blocked.

Sequence similarities

Belongs to the neutral sphingomyelinase family.

Ontologies

Keywords
   Biological processCytolysis
Hemolysis
   Cellular componentSecreted
   DomainSignal
   Molecular functionHydrolase
   PTMDisulfide bond
Gene Ontology (GO)
   Biological processcytolysis

Inferred from electronic annotation. Source: UniProtKB-KW

hemolysis 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: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626 Potential
Chain27 – 333307Sphingomyelinase C
PRO_0000019901

Amino acid modifications

Disulfide bond150 ↔ 186 By similarity

Sequences

Sequence LengthMass (Da)Tools
P33377 [UniParc].

Last modified February 1, 1994. Version 1.
Checksum: 05F8AEA5ECC4A3B8

FASTA33336,821
        10         20         30         40         50         60 
MKGKLLKGVL SLGVGLGALY SGTSAQAEAS TNQNDTLKVM THNVYMLSTN LYPNWGQTER 

        70         80         90        100        110        120 
ADLFGAADYI 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 FPDSLAEYLD YIIASKDHAN PSYIENKVLQ 

       310        320        330 
PKSPQWTVTS WFKNIRIMIT LIIIQVEATI SMK 

« Hide

References

[1]"A Bacillus cereus cytolytic determinant, cereolysin AB, which comprises the phospholipase C and sphingomyelinase genes: nucleotide sequence and genetic linkage."
Gilmore M.S., Cruz-Rodz A.L., Leimeister-Waechter M., Kreft J., Goebel W.
J. Bacteriol. 171:744-753(1989) [PubMed: 2536680] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: GP-4.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M24149 Genomic DNA. Translation: AAA91820.1.

3D structure databases

ProteinModelPortalP33377.
SMRP33377. Positions 34-332.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

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

Entry information

Entry namePHL3_BACCE
AccessionPrimary (citable) accession number: P33377
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: October 19, 2011
This is version 60 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