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Protein

Phospholipase C

Gene

plc

Organism
Clostridium perfringens (strain 13 / Type A)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Bacterial hemolysins are exotoxins that attack blood cell membranes and cause cell rupture. Constitutes an essential virulence factor in gas gangrene. Binds to eukaryotic membranes where it hydrolyzes both phosphatidylcholine and sphingomyelin. The diacylglycerol produced can activate both the arachidonic acid pathway, leading to modulation of the inflammatory response cascade and thrombosis, and protein kinase C, leading to activation of eukaryotic phospholipases and further membrane damage. Acts on human and mouse erythrocytes, but not on rabbit or horse erythrocytes.

Catalytic activityi

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

Cofactori

Protein has several cofactor binding sites:
  • Ca2+CuratedNote: Binds 3 Ca2+ ions per subunit.Curated
  • Zn2+Note: Binds 3 Zn2+ ions per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi29 – 291Zinc 1
Metal bindingi39 – 391Zinc 1
Metal bindingi84 – 841Zinc 3
Metal bindingi96 – 961Zinc 3
Metal bindingi154 – 1541Zinc 3
Metal bindingi158 – 1581Zinc 1
Metal bindingi158 – 1581Zinc 3
Metal bindingi164 – 1641Zinc 2
Metal bindingi176 – 1761Zinc 2
Metal bindingi180 – 1801Zinc 2
Metal bindingi297 – 2971Calcium 1Curated
Metal bindingi299 – 2991Calcium 1; via carbonyl oxygenBy similarity
Metal bindingi300 – 3001Calcium 3Curated
Metal bindingi301 – 3011Calcium 3By similarity
Metal bindingi321 – 3211Calcium 2By similarity
Metal bindingi322 – 3221Calcium 2By similarity
Metal bindingi324 – 3241Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi325 – 3251Calcium 3By similarity
Metal bindingi326 – 3261Calcium 2By similarity
Metal bindingi326 – 3261Calcium 3By similarity
Metal bindingi364 – 3641Calcium 1Curated
Metal bindingi365 – 3651Calcium 1; via carbonyl oxygenBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Toxin

Keywords - Biological processi

Cytolysis, Hemolysis, Virulence

Keywords - Ligandi

Calcium, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciCPER195102:GJFM-47-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Phospholipase C (EC:3.1.4.3)
Short name:
PLC
Alternative name(s):
Alpha-toxin
Hemolysin
Lecithinase
Phosphatidylcholine cholinephosphohydrolase
Gene namesi
Name:plc
Synonyms:cpa
Ordered Locus Names:CPE0036
OrganismiClostridium perfringens (strain 13 / Type A)
Taxonomic identifieri195102 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium
Proteomesi
  • UP000000818 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Biotechnological usei

Vaccination of mice with a fragment (residues 275-398) protects them against a subsequent challenge with purified alpha-toxin.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi29 – 291W → S: Loss of all enzyme activities. 1 Publication
Mutagenesisi39 – 391H → G or L: No enzyme accumulates. 1 Publication
Mutagenesisi39 – 391H → S: Loss of all enzyme activities. 1 Publication
Mutagenesisi84 – 841D → N: Loss of all enzyme activities. 1 Publication
Mutagenesisi96 – 961H → G or S: Loss of all enzyme activities. 1 Publication
Mutagenesisi97 – 971F → C: Loss of all enzyme activities. 1 Publication
Mutagenesisi154 – 1541H → G or S: Loss of all enzyme activities. 1 Publication
Mutagenesisi158 – 1581D → N: Loss of all enzyme activities. 1 Publication
Mutagenesisi164 – 1641H → A, G or S: Loss of all enzyme activities. 1 Publication
Mutagenesisi176 – 1761H → G, L or S: Loss of all enzyme activities. 1 Publication
Mutagenesisi180 – 1801E → Q: Loss of all enzyme activities. 1 Publication
Mutagenesisi297 – 2971D → N: Increased dependence of PLC on Ca(2+). Dramatically decreases hemolytic, cytotoxic and myotoxic activities. 1 Publication
Mutagenesisi300 – 3001T → P: Significant loss of activities; protein conformation has changed. 1 Publication
Mutagenesisi303 – 3031Y → F or N: Increased dependence of PLC on Ca(2+). Dramatically decreases hemolytic, cytotoxic and myotoxic activities. 1 Publication
Mutagenesisi364 – 3641D → N: Increased dependence of PLC on Ca(2+). Dramatically decreases hemolytic, cytotoxic and myotoxic activities. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2828By similarityAdd
BLAST
Chaini29 – 398370Phospholipase CPRO_0000023931Add
BLAST

Structurei

Secondary structure

1
398
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni33 – 353Combined sources
Helixi38 – 5316Combined sources
Helixi60 – 7112Combined sources
Helixi73 – 819Combined sources
Helixi82 – 843Combined sources
Helixi94 – 963Combined sources
Turni100 – 1023Combined sources
Turni106 – 1083Combined sources
Helixi122 – 13817Combined sources
Helixi142 – 15918Combined sources
Turni163 – 1675Combined sources
Turni170 – 1723Combined sources
Helixi175 – 18612Combined sources
Helixi187 – 1904Combined sources
Helixi202 – 2098Combined sources
Helixi213 – 23422Combined sources
Helixi242 – 27332Combined sources
Turni277 – 2804Combined sources
Beta strandi285 – 2928Combined sources
Beta strandi302 – 3109Combined sources
Beta strandi315 – 3195Combined sources
Beta strandi323 – 3253Combined sources
Beta strandi332 – 3387Combined sources
Helixi346 – 3483Combined sources
Beta strandi349 – 3579Combined sources
Beta strandi359 – 3624Combined sources
Beta strandi368 – 3758Combined sources
Beta strandi378 – 3847Combined sources
Beta strandi394 – 3963Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CA1X-ray1.90A29-398[»]
1GYGX-ray1.90A/B29-398[»]
1QM6X-ray2.50A/B29-398[»]
1QMDX-ray2.20A/B29-398[»]
1SB4model-A29-398[»]
ProteinModelPortaliP0C216.
SMRiP0C216. Positions 29-398.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0C216.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini29 – 278250Zn-dependent PLCPROSITE-ProRule annotationAdd
BLAST
Domaini284 – 398115PLATPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni275 – 2839Linker

Domaini

The protein is composed of 2 domains; the N-terminal domain contains the phospholipase C active site (PLC), in a cleft which is also occupied by the 3 zinc ions. The C-terminal domain is a putative phospholipid-recognition domain, which shows structural homology with phospholipid-binding C2-like domains from a range of eukaryotic proteins. The ability to bind membrane phospholipids in a Ca2+ dependent manner and toxicity is conferred by this C-terminal domain, which also contributes to the sphingomyelinase activity.

Sequence similaritiesi

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

Keywords - Domaini

Signal

Phylogenomic databases

KOiK16619.
OMAiDHFWDPD.
OrthoDBiPOG091H10JI.

Family and domain databases

Gene3Di1.10.575.10. 1 hit.
2.60.60.20. 1 hit.
InterProiIPR001024. PLAT/LH2_dom.
IPR008947. PLipase_C/P1_nuclease.
IPR029002. PLPC/GPLD1.
IPR001531. Zn_PLipaseC.
[Graphical view]
PfamiPF01477. PLAT. 1 hit.
PF00882. 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.
SSF49723. SSF49723. 1 hit.
PROSITEiPS50095. PLAT. 1 hit.
PS00384. 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.

P0C216-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKRKICKALI CATLATSLWA GASTKVYAWD GKIDGTGTHA MIVTQGVSIL
60 70 80 90 100
ENDLSKNEPE SVRKNLEILK ENMHELQLGS TYPDYDKNAY DLYQDHFWDP
110 120 130 140 150
DTDNNFSKDN SWYLAYSIPD TGESQIRKFS ALARYEWQRG NYKQATFYLG
160 170 180 190 200
EAMHYFGDID TPYHPANVTA VDSAGHVKFE TFAEERKEQY KINTAGCKTN
210 220 230 240 250
EDFYADILKN KDFNAWSKEY ARGFAKTGKS IYYSHASMSH SWDDWDYAAK
260 270 280 290 300
VTLANSQKGT AGYIYRFLHD VSEGNDPSVG KNVKELVAYI STSGEKDAGT
310 320 330 340 350
DDYMYFGIKT KDGKTQEWEM DNPGNDFMTG SKDTYTFKLK DENLKIDDIQ
360 370 380 390
NMWIRKRKYT AFPDAYKPEN IKIIANGKVV VDKDINEWIS GNSTYNIK
Length:398
Mass (Da):45,530
Last modified:October 31, 2006 - v1
Checksum:i2E9E4A61181028CA
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti2 – 21K → E in strain: CER 89L1216.
Natural varianti10 – 101I → V in strain: 8-6.
Natural varianti13 – 153TLA → ALR in strain: CER 89L1105 and CER 89L1216.
Natural varianti13 – 131T → A in strain: 8-6, KZ211, L9, NCIB 10691, BP6K and KZ1340.
Natural varianti15 – 151A → V in strain: 8-6.
Natural varianti22 – 221A → T in strain: L9 and BP6K.
Natural varianti22 – 221A → V in strain: 8-6.
Natural varianti43 – 431V → A in strain: NCIB 10691.
Natural varianti47 – 471V → I in strain: L9 and KZ1340.
Natural varianti54 – 541L → M in strain: 8-6.
Natural varianti71 – 711E → D in strain: 8-6.
Natural varianti91 – 911D → N in strain: KZ1340.
Natural varianti103 – 1031D → N in strain: 8-6.
Natural varianti176 – 1761H → Y in strain: KZ1340; probably inactive.
Natural varianti195 – 1951A → V in strain: 8-6, NCIB 10663 and NCIB 10748.
Natural varianti202 – 2021D → A in strain: NCIB 10691 and CER 89L1105.
Natural varianti205 – 2051A → T in strain: NCIB 10691 and CER 89L1105.
Natural varianti281 – 2811K → N in strain: 8-6.
Natural varianti329 – 3291T → A in strain: 8-6.
Natural varianti363 – 3631P → S in strain: NCIB 10691 and CER 89L1105.
Natural varianti373 – 3731I → L in strain: PB6K.
Natural varianti373 – 3731I → V in strain: 8-6, NCIB 10662, L9, NCIB 10663, NCIB 10748, CER 89L43 and KZ1340.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X17300 Genomic DNA. Translation: CAA35186.1.
D10248 Genomic DNA. Translation: BAA01093.1.
D32123 Genomic DNA. Translation: BAA06849.1.
D32124 Genomic DNA. Translation: BAA06850.1.
D32126 Genomic DNA. Translation: BAA06852.1.
D32127 Genomic DNA. Translation: BAA06853.1.
D32128 Genomic DNA. Translation: BAA06854.1.
D49968 Genomic DNA. Translation: BAA08720.1.
D49969 Genomic DNA. Translation: BAA08721.1.
L43545 Genomic DNA. Translation: AAA99192.1.
L43546 Genomic DNA. Translation: AAA99193.1.
L43547 Genomic DNA. Translation: AAA99194.1.
L43548 Genomic DNA. Translation: AAA99195.1.
D63911 Genomic DNA. Translation: BAA09944.1.
BA000016 Genomic DNA. Translation: BAB79742.1.
PIRiB49231.
JQ0366.
RefSeqiWP_011009584.1. NC_003366.1.

Genome annotation databases

EnsemblBacteriaiBAB79742; BAB79742; BAB79742.
GeneIDi988262.
KEGGicpe:CPE0036.
PATRICi19493928. VBICloPer59675_0094.

Cross-referencesi

Web resourcesi

Worthington enzyme manual

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X17300 Genomic DNA. Translation: CAA35186.1.
D10248 Genomic DNA. Translation: BAA01093.1.
D32123 Genomic DNA. Translation: BAA06849.1.
D32124 Genomic DNA. Translation: BAA06850.1.
D32126 Genomic DNA. Translation: BAA06852.1.
D32127 Genomic DNA. Translation: BAA06853.1.
D32128 Genomic DNA. Translation: BAA06854.1.
D49968 Genomic DNA. Translation: BAA08720.1.
D49969 Genomic DNA. Translation: BAA08721.1.
L43545 Genomic DNA. Translation: AAA99192.1.
L43546 Genomic DNA. Translation: AAA99193.1.
L43547 Genomic DNA. Translation: AAA99194.1.
L43548 Genomic DNA. Translation: AAA99195.1.
D63911 Genomic DNA. Translation: BAA09944.1.
BA000016 Genomic DNA. Translation: BAB79742.1.
PIRiB49231.
JQ0366.
RefSeqiWP_011009584.1. NC_003366.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CA1X-ray1.90A29-398[»]
1GYGX-ray1.90A/B29-398[»]
1QM6X-ray2.50A/B29-398[»]
1QMDX-ray2.20A/B29-398[»]
1SB4model-A29-398[»]
ProteinModelPortaliP0C216.
SMRiP0C216. Positions 29-398.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAB79742; BAB79742; BAB79742.
GeneIDi988262.
KEGGicpe:CPE0036.
PATRICi19493928. VBICloPer59675_0094.

Phylogenomic databases

KOiK16619.
OMAiDHFWDPD.
OrthoDBiPOG091H10JI.

Enzyme and pathway databases

BioCyciCPER195102:GJFM-47-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0C216.

Family and domain databases

Gene3Di1.10.575.10. 1 hit.
2.60.60.20. 1 hit.
InterProiIPR001024. PLAT/LH2_dom.
IPR008947. PLipase_C/P1_nuclease.
IPR029002. PLPC/GPLD1.
IPR001531. Zn_PLipaseC.
[Graphical view]
PfamiPF01477. PLAT. 1 hit.
PF00882. 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.
SSF49723. SSF49723. 1 hit.
PROSITEiPS50095. PLAT. 1 hit.
PS00384. PROKAR_ZN_DEPEND_PLPC_1. 1 hit.
PS51346. PROKAR_ZN_DEPEND_PLPC_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPHLC1_CLOPE
AccessioniPrimary (citable) accession number: P0C216
Secondary accession number(s): P15310
, P94658, Q46246, Q46279, Q46280, Q46281, Q46282, Q57317, Q59303, Q59304, Q59305, Q59313, Q60121
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: October 31, 2006
Last modified: September 7, 2016
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Variations seen in PLC activity between different strains seem to be due to transcriptional regulation.
Mutating residues 303 or 359 of the C.perfringens toxin to match those found in C.bifermentans (301 and 358 respectively) reduces toxicity considerably.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

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.