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P14262 (PLC_BACCE) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 83. 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:
1-phosphatidylinositol phosphodiesterase

EC=4.6.1.13
Alternative name(s):
Phosphatidylinositol diacylglycerol-lyase
Phosphatidylinositol-specific phospholipase C
Short name=PI-PLC
OrganismBacillus cereus
Taxonomic identifier1396 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length329 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Cleaves glycosylphosphatidylinositol (GPI) and phosphatidylinositol (PI) anchors but not PI phosphates.

Catalytic activity

1-phosphatidyl-1D-myo-inositol = 1D-myo-inositol 1,2-cyclic phosphate + 1,2-diacyl-sn-glycerol.

Subcellular location

Secreted.

Sequence similarities

Contains 1 PI-PLC X-box domain.

Ontologies

Keywords
   Biological processLipid degradation
Lipid metabolism
   Cellular componentSecreted
   DomainSignal
   Molecular functionLyase
   Technical term3D-structure
Gene Ontology (GO)
   Biological_processlipid catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionphosphatidylinositol diacylglycerol-lyase activity

Inferred from electronic annotation. Source: UniProtKB-EC

phosphoric diester hydrolase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3131
Chain32 – 3292981-phosphatidylinositol phosphodiesterase
PRO_0000024294

Regions

Domain53 – 194142PI-PLC X-box

Sites

Active site631Proton acceptor
Active site1131Proton donor

Secondary structure

....................................................... 329
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P14262 [UniParc].

Last modified January 1, 1990. Version 1.
Checksum: 0D731F5604135CB4

FASTA32938,109
        10         20         30         40         50         60 
MSNKKLILKL FICSTIFITF VFALHDKRVV AASSVNELEN WSKWMQPIPD SIPLARISIP 

        70         80         90        100        110        120 
GTHDSGTFKL QNPIKQVWGM TQEYDFRYQM DHGARIFDIR GRLTDDNTIV LHHGPLYLYV 

       130        140        150        160        170        180 
TLHEFINEAK QFLKDNPSET IIMSLKKEYE DMKGAEDSFS STFEKKYFVD PIFLKTEGNI 

       190        200        210        220        230        240 
KLGDARGKIV LLKRYSGSNE PGGYNNFYWP DNETFTTTVN QNANVTVQDK YKVSYDEKVK 

       250        260        270        280        290        300 
SIKDTMDETM NNSEDLNHLY INFTSLSSGG TAWNSPYYYA SYINPEIANY IKQKNPARVG 

       310        320 
WVIQDYINEK WSPLLYQEVI RANKSLIKE 

« Hide

References

[1]"Phosphatidylinositol-specific phospholipase C of Bacillus cereus: cloning, sequencing, and relationship to other phospholipases."
Kuppe A., Evans L.M., McMillen D.A., Griffith O.H.
J. Bacteriol. 171:6077-6083(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Crystal structure of the phosphatidylinositol-specific phospholipase C from Bacillus cereus in complex with myo-inositol."
Heinz D.W., Ryan M., Bullock T.L., Griffith O.H.
EMBO J. 14:3855-3863(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
[3]"Crystal structure of phosphatidylinositol-specific phospholipase C from Bacillus cereus in complex with glucosaminyl(alpha 1-->6)-D-myo-inositol, an essential fragment of GPI anchors."
Heinz D.W., Ryan M., Smith M.P., Weaver L.H., Keana J.F., Griffith O.H.
Biochemistry 35:9496-9504(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
[4]"Probing the roles of active site residues in phosphatidylinositol-specific phospholipase C from Bacillus cereus by site-directed mutagenesis."
Gassler C.S., Ryan M., Liu T., Griffith O.H., Heinz D.W.
Biochemistry 36:12802-12813(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M30809 Genomic DNA. Translation: AAA22665.1.
PIRA33493.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1GYMX-ray2.20A32-329[»]
1PTDX-ray2.60A32-329[»]
1PTGX-ray2.60A32-329[»]
2PTDX-ray2.00A32-329[»]
3PTDX-ray2.20A32-329[»]
4PTDX-ray2.30A32-329[»]
5PTDX-ray2.70A32-329[»]
6PTDX-ray2.60A32-329[»]
7PTDX-ray2.60A32-329[»]
ProteinModelPortalP14262.
SMRP14262. Positions 32-327.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-15192.

Family and domain databases

Gene3D3.20.20.190. 1 hit.
InterProIPR017946. PLC-like_Pdiesterase_TIM-brl.
IPR000909. PLipase_C_PInositol-sp_X_dom.
[Graphical view]
PfamPF00388. PI-PLC-X. 1 hit.
[Graphical view]
SMARTSM00148. PLCXc. 1 hit.
[Graphical view]
SUPFAMSSF51695. SSF51695. 1 hit.
PROSITEPS50007. PIPLC_X_DOMAIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP14262.

Entry information

Entry namePLC_BACCE
AccessionPrimary (citable) accession number: P14262
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: October 16, 2013
This is version 83 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