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P11889

- PHL2_BACCE

UniProt

P11889 - PHL2_BACCE

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Protein

Sphingomyelinase C

Gene

sph

Organism
Bacillus cereus
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

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
Complete GO annotation...

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-KW
Complete GO annotation...

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 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKGKLLKGVL SLGVGLGALY SGTSAQAEAS TNQNDTLKVM THNVYMLSTN
60 70 80 90 100
LYPNWGQTER ADLIGAADYI KNQDVVILNE VFDNSASDRL LGNLKKEYPN
110 120 130 140 150
QTAVLGRSSG SEWDKTLGNY SSSTPEDGGV AIVSKWPIAE KIQYVFAKGC
160 170 180 190 200
GPDNLSNKGF VYTKIKKNDR FVHVIGTHLQ AEDSMCGKTS PASVRTNQLK
210 220 230 240 250
EIQDFIKNKN IPNNEYVLIG GDMNVNKINA ENNNDSEYAS MFKTLNASVP
260 270 280 290 300
SYTGHTATWD ATTNSIAKYN FPDSPAEYLD YIIASKDHAN PSYIENKVLQ
310 320 330
PKSPQWTVTS WFQKYTYNDY SDDYPVEATI SMK
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 29, 2014
This is version 92 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