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Protein

Sphingomyelinase C

Gene

sph

Organism
Bacillus cereus
Status
Reviewed-Annotation score: 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

Enzyme regulationi

Activated by cobalt and manganese ions.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Cytolysis, Hemolysis

Enzyme and pathway databases

BRENDAi3.1.4.12. 648.
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

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 271 PublicationAdd BLAST27
ChainiPRO_000001990028 – 333Sphingomyelinase CAdd BLAST306

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi150 ↔ 186By similarity

Keywords - PTMi

Disulfide bond

Interactioni

Protein-protein interaction databases

STRINGi226900.BC0671.

Structurei

Secondary structure

1333
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi36 – 46Combined sources11
Turni49 – 51Combined sources3
Helixi57 – 66Combined sources10
Beta strandi74 – 81Combined sources8
Helixi84 – 94Combined sources11
Turni95 – 97Combined sources3
Beta strandi113 – 119Combined sources7
Beta strandi122 – 126Combined sources5
Beta strandi131 – 136Combined sources6
Beta strandi138 – 145Combined sources8
Beta strandi151 – 153Combined sources3
Beta strandi159 – 167Combined sources9
Beta strandi170 – 178Combined sources9
Helixi184 – 186Combined sources3
Helixi191 – 209Combined sources19
Beta strandi217 – 222Combined sources6
Turni228 – 230Combined sources3
Helixi237 – 245Combined sources9
Beta strandi251 – 254Combined sources4
Turni261 – 263Combined sources3
Helixi265 – 270Combined sources6
Beta strandi280 – 285Combined sources6
Beta strandi292 – 298Combined sources7
Beta strandi306 – 310Combined sources5
Beta strandi313 – 317Combined sources5
Beta strandi320 – 323Combined sources4
Beta strandi326 – 331Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11889.

Family & Domainsi

Sequence similaritiesi

Belongs to the neutral sphingomyelinase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4108QYW. Bacteria.
ENOG410ZQ24. LUCA.

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

        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)DescriptionActionsGraphical viewLength
Sequence conflicti33Q → E AA sequence (PubMed:8319899).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X12711 Genomic DNA. Translation: CAA31214.1.
PIRiB32042.
S01130.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X12711 Genomic DNA. Translation: CAA31214.1.
PIRiB32042.
S01130.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi226900.BC0671.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4108QYW. Bacteria.
ENOG410ZQ24. LUCA.

Enzyme and pathway databases

BRENDAi3.1.4.12. 648.
SABIO-RKP11889.

Miscellaneous databases

EvolutionaryTraceiP11889.

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.
ProtoNetiSearch...

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: November 2, 2016
This is version 101 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.