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Protein

Phospholipase C

Gene

plc

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

Functioni

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

Catalytic activityi

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

Cofactori

Zn2+Note: Binds 3 Zn2+ ions per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi39 – 391Zinc 3
Metal bindingi52 – 521Zinc 3
Metal bindingi93 – 931Zinc 1
Metal bindingi107 – 1071Zinc 1
Metal bindingi156 – 1561Zinc 1
Metal bindingi160 – 1601Zinc 1
Metal bindingi160 – 1601Zinc 3
Metal bindingi166 – 1661Zinc 2
Metal bindingi180 – 1801Zinc 2
Metal bindingi184 – 1841Zinc 2

GO - Molecular functioni

  1. phosphatidylcholine phospholipase C activity Source: UniProtKB-EC
  2. zinc ion binding Source: InterPro

GO - Biological processi

  1. hemolysis in other organism Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Cytolysis, Hemolysis

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.1.4.3. 648.
SABIO-RKP09598.

Names & Taxonomyi

Protein namesi
Recommended name:
Phospholipase C (EC:3.1.4.3)
Short name:
PLC
Alternative name(s):
Cereolysin A
Phosphatidylcholine cholinephosphohydrolase
Gene namesi
Name:plc
OrganismiBacillus cereus
Taxonomic identifieri1396 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424Sequence AnalysisAdd
BLAST
Propeptidei25 – 38142 PublicationsPRO_0000023927Add
BLAST
Chaini39 – 283245Phospholipase CPRO_0000023928Add
BLAST

Keywords - PTMi

Zymogen

Interactioni

Subunit structurei

Monomer.

Structurei

Secondary structure

1
283
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi43 – 453Combined sources
Helixi47 – 493Combined sources
Helixi51 – 6515Combined sources
Helixi72 – 809Combined sources
Helixi82 – 9110Combined sources
Turni92 – 943Combined sources
Turni96 – 1038Combined sources
Helixi105 – 1073Combined sources
Turni111 – 1133Combined sources
Helixi124 – 14017Combined sources
Helixi144 – 16118Combined sources
Turni164 – 1696Combined sources
Beta strandi174 – 1763Combined sources
Helixi179 – 19012Combined sources
Helixi191 – 1944Combined sources
Helixi210 – 22314Combined sources
Helixi225 – 2273Combined sources
Helixi231 – 24010Combined sources
Helixi244 – 28037Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
SMRiP09598. Positions 39-283.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP09598.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini39 – 283245Zn-dependent PLCPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the bacterial zinc-metallophospholipase C family.PROSITE-ProRule annotation
Contains 1 Zn-dependent PLC domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Family and domain databases

Gene3Di1.10.575.10. 1 hit.
InterProiIPR008947. PLipase_C/P1_nuclease.
IPR001531. PLipaseC_domain.
IPR029002. PLPC/GPLD1.
[Graphical view]
PfamiPF00882. Zn_dep_PLPC. 1 hit.
[Graphical view]
PRINTSiPR00479. PRPHPHLPASEC.
ProDomiPD003946. PLipaseC_Zn-bd_prok. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00770. Zn_dep_PLPC. 1 hit.
[Graphical view]
SUPFAMiSSF48537. SSF48537. 1 hit.
PROSITEiPS00384. PROKAR_ZN_DEPEND_PLPC_1. 1 hit.
PS51346. PROKAR_ZN_DEPEND_PLPC_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P09598-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKKVLALAA AITVVAPLQS VAFAHENDGG SKIKIVHRWS AEDKHKEGVN
60 70 80 90 100
SHLWIVNRAI DIMSRNTTLV KQDRVAQLNE WRTELENGIY AADYENPYYD
110 120 130 140 150
NSTFASHFYD PDNGKTYIPF AKQAKETGAK YFKLAGESYK NKDMKQAFFY
160 170 180 190 200
LGLSLHYLGD VNQPMHAANF TNLSYPQGFH SKYENFVDTI KDNYKVTDGN
210 220 230 240 250
GYWNWKGTNP EEWIHGAAVV AKQDYSGIVN DNTKDWFVKA AVSQEYADKW
260 270 280
RAEVTPMTGK RLMDAQRVTA GYIQLWFDTY GDR
Length:283
Mass (Da):32,383
Last modified:July 1, 1989 - v1
Checksum:iAC5452EFF2E22B19
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti212 – 2121E → D in strain: IAM 1208.
Natural varianti226 – 2261S → A in strain: IAM 1208.
Natural varianti239 – 2391K → R in strain: IAM 1208.
Natural varianti282 – 2821D → N in strain: IAM 1208.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiS18978. PS0197.
RefSeqiWP_000731014.1. NZ_KN050656.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiS18978. PS0197.
RefSeqiWP_000731014.1. NZ_KN050656.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
SMRiP09598. Positions 39-283.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

BindingDBiP09598.
ChEMBLiCHEMBL1293202.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.1.4.3. 648.
SABIO-RKP09598.

Miscellaneous databases

EvolutionaryTraceiP09598.

Family and domain databases

Gene3Di1.10.575.10. 1 hit.
InterProiIPR008947. PLipase_C/P1_nuclease.
IPR001531. PLipaseC_domain.
IPR029002. PLPC/GPLD1.
[Graphical view]
PfamiPF00882. Zn_dep_PLPC. 1 hit.
[Graphical view]
PRINTSiPR00479. PRPHPHLPASEC.
ProDomiPD003946. PLipaseC_Zn-bd_prok. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00770. Zn_dep_PLPC. 1 hit.
[Graphical view]
SUPFAMiSSF48537. SSF48537. 1 hit.
PROSITEiPS00384. PROKAR_ZN_DEPEND_PLPC_1. 1 hit.
PS51346. PROKAR_ZN_DEPEND_PLPC_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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. 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).

Entry informationi

Entry nameiPHLC_BACCE
AccessioniPrimary (citable) accession number: P09598
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: April 1, 2015
This is version 107 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

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 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.