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P11889

- PHL2_BACCE

UniProt

P11889 - PHL2_BACCE

Protein

Sphingomyelinase C

Gene

sph

Organism
Bacillus cereus
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 91 (01 Oct 2014)
      Sequence version 1 (01 Oct 1989)
      Previous versions | rss
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    Functioni

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

    Catalytic activityi

    Sphingomyelin + H2O = N-acylsphingosine + phosphocholine.

    Cofactori

    Magnesium.

    Enzyme regulationi

    Activated by cobalt and manganese ions.

    GO - Molecular functioni

    1. sphingomyelin phosphodiesterase activity Source: UniProtKB-EC

    GO - Biological processi

    1. hemolysis in other organism Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Cytolysis, Hemolysis

    Enzyme and pathway databases

    SABIO-RKP11889.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Sphingomyelinase C (EC:3.1.4.12)
    Short name:
    SMase
    Alternative name(s):
    Cereolysin B
    SMPLC
    Sphingomyelin phosphodiesterase
    Gene namesi
    Name:sph
    OrganismiBacillus cereus
    Taxonomic identifieri1396 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 27271 PublicationAdd
    BLAST
    Chaini28 – 333306Sphingomyelinase CPRO_0000019900Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi150 ↔ 186By similarity

    Keywords - PTMi

    Disulfide bond

    Structurei

    Secondary structure

    1
    333
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi36 – 4611
    Turni49 – 513
    Helixi57 – 6610
    Beta strandi74 – 818
    Helixi84 – 9411
    Turni95 – 973
    Beta strandi113 – 1197
    Beta strandi122 – 1265
    Beta strandi131 – 1366
    Beta strandi138 – 1458
    Beta strandi150 – 1534
    Beta strandi159 – 1679
    Beta strandi170 – 1789
    Helixi184 – 1863
    Helixi191 – 20919
    Beta strandi217 – 2226
    Turni228 – 2303
    Helixi237 – 2459
    Beta strandi251 – 2544
    Turni261 – 2633
    Helixi265 – 2706
    Beta strandi280 – 2856
    Beta strandi292 – 2987
    Beta strandi306 – 3105
    Beta strandi313 – 3175
    Beta strandi320 – 3234
    Beta strandi326 – 3316

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliP11889.
    SMRiP11889. Positions 34-332.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP11889.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the neutral sphingomyelinase family.Curated

    Keywords - Domaini

    Signal

    Family and domain databases

    Gene3Di3.60.10.10. 1 hit.
    InterProiIPR005135. Endo/exonuclease/phosphatase.
    IPR017766. Sphingomyelinase/PLipase_C.
    [Graphical view]
    PfamiPF03372. Exo_endo_phos. 1 hit.
    [Graphical view]
    SUPFAMiSSF56219. SSF56219. 1 hit.
    TIGRFAMsiTIGR03395. sphingomy. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P11889-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKGKLLKGVL SLGVGLGALY SGTSAQAEAS TNQNDTLKVM THNVYMLSTN    50
    LYPNWGQTER ADLIGAADYI KNQDVVILNE VFDNSASDRL LGNLKKEYPN 100
    QTAVLGRSSG SEWDKTLGNY SSSTPEDGGV AIVSKWPIAE KIQYVFAKGC 150
    GPDNLSNKGF VYTKIKKNDR FVHVIGTHLQ AEDSMCGKTS PASVRTNQLK 200
    EIQDFIKNKN IPNNEYVLIG GDMNVNKINA ENNNDSEYAS MFKTLNASVP 250
    SYTGHTATWD ATTNSIAKYN FPDSPAEYLD YIIASKDHAN PSYIENKVLQ 300
    PKSPQWTVTS WFQKYTYNDY SDDYPVEATI SMK 333
    Length:333
    Mass (Da):36,873
    Last modified:October 1, 1989 - v1
    Checksum:iA48E01702B1CAB3D
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti33 – 331Q → E AA sequence (PubMed:8319899)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X12711 Genomic DNA. Translation: CAA31214.1.
    PIRiB32042.
    S01130.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X12711 Genomic DNA. Translation: CAA31214.1 .
    PIRi B32042.
    S01130.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2DDR X-ray 1.40 A/B/C/D 28-333 [» ]
    2DDS X-ray 1.80 A/B/C/D 28-333 [» ]
    2DDT X-ray 1.80 A/B 28-333 [» ]
    2UYR X-ray 2.40 X 28-333 [» ]
    ProteinModelPortali P11889.
    SMRi P11889. Positions 34-332.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    SABIO-RK P11889.

    Miscellaneous databases

    EvolutionaryTracei P11889.

    Family and domain databases

    Gene3Di 3.60.10.10. 1 hit.
    InterProi IPR005135. Endo/exonuclease/phosphatase.
    IPR017766. Sphingomyelinase/PLipase_C.
    [Graphical view ]
    Pfami PF03372. Exo_endo_phos. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56219. SSF56219. 1 hit.
    TIGRFAMsi TIGR03395. sphingomy. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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.

    Entry informationi

    Entry nameiPHL2_BACCE
    AccessioniPrimary (citable) accession number: P11889
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1989
    Last sequence update: October 1, 1989
    Last modified: October 1, 2014
    This is version 91 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3