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P09598 (PHLC_BACCE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 101. 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:
Phospholipase C

Short name=PLC
EC=3.1.4.3
Alternative name(s):
Cereolysin A
Phosphatidylcholine cholinephosphohydrolase
Gene names
Name:plc
OrganismBacillus cereus
Taxonomic identifier1396 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length283 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

A phosphatidylcholine + H2O = 1,2-diacyl-sn-glycerol + phosphocholine.

Cofactor

Binds 3 zinc ions per subunit.

Subunit structure

Monomer.

Sequence similarities

Belongs to the bacterial zinc-metallophospholipase C family.

Contains 1 Zn-dependent PLC domain.

Ontologies

Keywords
   Biological processCytolysis
Hemolysis
   DomainSignal
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
   PTMZymogen
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processhemolysis in other organism

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionphosphatidylcholine phospholipase C activity

Inferred from electronic annotation. Source: UniProtKB-EC

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential
Propeptide25 – 3814
PRO_0000023927
Chain39 – 283245Phospholipase C
PRO_0000023928

Regions

Domain39 – 283245Zn-dependent PLC

Sites

Metal binding391Zinc 3
Metal binding521Zinc 3
Metal binding931Zinc 1
Metal binding1071Zinc 1
Metal binding1561Zinc 1
Metal binding1601Zinc 1
Metal binding1601Zinc 3
Metal binding1661Zinc 2
Metal binding1801Zinc 2
Metal binding1841Zinc 2

Natural variations

Natural variant2121E → D in strain: IAM 1208.
Natural variant2261S → A in strain: IAM 1208.
Natural variant2391K → R in strain: IAM 1208.
Natural variant2821D → N in strain: IAM 1208.

Secondary structure

..................................... 283
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P09598 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: AC5452EFF2E22B19

FASTA28332,383
        10         20         30         40         50         60 
MKKKVLALAA AITVVAPLQS VAFAHENDGG SKIKIVHRWS AEDKHKEGVN SHLWIVNRAI 

        70         80         90        100        110        120 
DIMSRNTTLV KQDRVAQLNE WRTELENGIY AADYENPYYD NSTFASHFYD PDNGKTYIPF 

       130        140        150        160        170        180 
AKQAKETGAK YFKLAGESYK NKDMKQAFFY LGLSLHYLGD VNQPMHAANF TNLSYPQGFH 

       190        200        210        220        230        240 
SKYENFVDTI KDNYKVTDGN GYWNWKGTNP EEWIHGAAVV AKQDYSGIVN DNTKDWFVKA 

       250        260        270        280 
AVSQEYADKW RAEVTPMTGK RLMDAQRVTA GYIQLWFDTY GDR 

« Hide

References

[1]"Cloning and sequencing of the gene encoding the phosphatidylcholine-preferring phospholipase C of Bacillus cereus."
Johansen T., Holm T., Guddal P.H., Sletten K., Haugli F.B., Little C.
Gene 65:293-304(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: SE-1.
[2]"Nucleotide sequence of phospholipase C and sphingomyelinase genes from Bacillus cereus BKM-B164."
Kuzmin N.P., Gavrilenko I.V., Krukov V.M., Karpov A.V.
Bioorg. Khim. 19:133-138(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: VKM B-164.
[3]"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] OF 166-283.
Strain: IAM 1208.
[4]"Some characteristics of phospholipase C from Bacillus cereus."
Otnaess A.-B., Little C., Sletten K., Wallin R., Johnsen S., Flengsrud R., Prydz H.
Eur. J. Biochem. 79:459-468(1977) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 39-65.
[5]"Kinetics of the hydrolysis of monodispersed and micellar phosphatidylcholines catalyzed by a phospholipase C from Bacillus cereus."
Ikeda K., Inoue S., Amasaki C., Teshima K., Ikezawa H.
J. Biochem. 110:88-95(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 39-49.
Strain: IAM 1208.
[6]"High-resolution (1.5 A) crystal structure of phospholipase C from Bacillus cereus."
Hough E., Hansen L.K., Birknes B., Jynge K., Hansen S., Hordvik A., Little C., Dodson E., Derewenda Z.
Nature 338:357-360(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X64141 Genomic DNA. Translation: CAA45502.1.
X12854 Genomic DNA. Translation: CAA31332.1.
X12711 Genomic DNA. Translation: CAA31213.1.
X64140 Genomic DNA. Translation: CAA45501.1. Different termination.
PIRPS0197. S18978.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AH7X-ray1.50A39-283[»]
1P5XX-ray2.00A39-283[»]
1P6DX-ray2.00A39-283[»]
1P6EX-ray2.30A39-283[»]
2FFZX-ray2.05A39-283[»]
2FGNX-ray2.04A39-283[»]
2HUCX-ray1.90A39-283[»]
ProteinModelPortalP09598.
SMRP09598. Positions 39-283.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBP09598.
ChEMBLCHEMBL1293202.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKP09598.

Family and domain databases

Gene3D1.10.575.10. 1 hit.
InterProIPR008947. PLipase_C/P1_nuclease.
IPR001531. PLipaseC_domain.
[Graphical view]
PRINTSPR00479. PRPHPHLPASEC.
ProDomPD003946. PLipaseC_Zn-bd_prok. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00770. Zn_dep_PLPC. 1 hit.
[Graphical view]
SUPFAMSSF48537. SSF48537. 1 hit.
PROSITEPS00384. PROKAR_ZN_DEPEND_PLPC_1. 1 hit.
PS51346. PROKAR_ZN_DEPEND_PLPC_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP09598.

Entry information

Entry namePHLC_BACCE
AccessionPrimary (citable) accession number: P09598
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: April 16, 2014
This is version 101 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