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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)DescriptionActionsGraphical viewLength
Metal bindingi29Zinc 11
Metal bindingi39Zinc 11
Metal bindingi84Zinc 31
Metal bindingi96Zinc 31
Metal bindingi154Zinc 31
Metal bindingi158Zinc 11
Metal bindingi158Zinc 31
Metal bindingi164Zinc 21
Metal bindingi176Zinc 21
Metal bindingi180Zinc 21
Metal bindingi297Calcium 1Curated1
Metal bindingi299Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi300Calcium 3Curated1
Metal bindingi301Calcium 3By similarity1
Metal bindingi321Calcium 2By similarity1
Metal bindingi322Calcium 2By similarity1
Metal bindingi324Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi325Calcium 3By similarity1
Metal bindingi326Calcium 2By similarity1
Metal bindingi326Calcium 3By similarity1
Metal bindingi364Calcium 1Curated1
Metal bindingi365Calcium 1; via carbonyl oxygenBy similarity1

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

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)DescriptionActionsGraphical viewLength
Mutagenesisi29W → S: Loss of all enzyme activities. 1 Publication1
Mutagenesisi39H → G or L: No enzyme accumulates. 1 Publication1
Mutagenesisi39H → S: Loss of all enzyme activities. 1 Publication1
Mutagenesisi84D → N: Loss of all enzyme activities. 1 Publication1
Mutagenesisi96H → G or S: Loss of all enzyme activities. 1 Publication1
Mutagenesisi97F → C: Loss of all enzyme activities. 1 Publication1
Mutagenesisi154H → G or S: Loss of all enzyme activities. 1 Publication1
Mutagenesisi158D → N: Loss of all enzyme activities. 1 Publication1
Mutagenesisi164H → A, G or S: Loss of all enzyme activities. 1 Publication1
Mutagenesisi176H → G, L or S: Loss of all enzyme activities. 1 Publication1
Mutagenesisi180E → Q: Loss of all enzyme activities. 1 Publication1
Mutagenesisi297D → N: Increased dependence of PLC on Ca(2+). Dramatically decreases hemolytic, cytotoxic and myotoxic activities. 1 Publication1
Mutagenesisi300T → P: Significant loss of activities; protein conformation has changed. 1 Publication1
Mutagenesisi303Y → F or N: Increased dependence of PLC on Ca(2+). Dramatically decreases hemolytic, cytotoxic and myotoxic activities. 1 Publication1
Mutagenesisi364D → N: Increased dependence of PLC on Ca(2+). Dramatically decreases hemolytic, cytotoxic and myotoxic activities. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 28By similarityAdd BLAST28
ChainiPRO_000002393129 – 398Phospholipase CAdd BLAST370

Structurei

Secondary structure

1398
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni33 – 35Combined sources3
Helixi38 – 53Combined sources16
Helixi60 – 71Combined sources12
Helixi73 – 81Combined sources9
Helixi82 – 84Combined sources3
Helixi94 – 96Combined sources3
Turni100 – 102Combined sources3
Turni106 – 108Combined sources3
Helixi122 – 138Combined sources17
Helixi142 – 159Combined sources18
Turni163 – 167Combined sources5
Turni170 – 172Combined sources3
Helixi175 – 186Combined sources12
Helixi187 – 190Combined sources4
Helixi202 – 209Combined sources8
Helixi213 – 234Combined sources22
Helixi242 – 273Combined sources32
Turni277 – 280Combined sources4
Beta strandi285 – 292Combined sources8
Beta strandi302 – 310Combined sources9
Beta strandi315 – 319Combined sources5
Beta strandi323 – 325Combined sources3
Beta strandi332 – 338Combined sources7
Helixi346 – 348Combined sources3
Beta strandi349 – 357Combined sources9
Beta strandi359 – 362Combined sources4
Beta strandi368 – 375Combined sources8
Beta strandi378 – 384Combined sources7
Beta strandi394 – 396Combined sources3

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP0C216.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini29 – 278Zn-dependent PLCPROSITE-ProRule annotationAdd BLAST250
Domaini284 – 398PLATPROSITE-ProRule annotationAdd BLAST115

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni275 – 283Linker9

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)DescriptionActionsGraphical viewLength
Natural varianti2K → E in strain: CER 89L1216. 1
Natural varianti10I → V in strain: 8-6. 1
Natural varianti13 – 15TLA → ALR in strain: CER 89L1105 and CER 89L1216. 3
Natural varianti13T → A in strain: 8-6, KZ211, L9, NCIB 10691, BP6K and KZ1340. 1
Natural varianti15A → V in strain: 8-6. 1
Natural varianti22A → T in strain: L9 and BP6K. 1
Natural varianti22A → V in strain: 8-6. 1
Natural varianti43V → A in strain: NCIB 10691. 1
Natural varianti47V → I in strain: L9 and KZ1340. 1
Natural varianti54L → M in strain: 8-6. 1
Natural varianti71E → D in strain: 8-6. 1
Natural varianti91D → N in strain: KZ1340. 1
Natural varianti103D → N in strain: 8-6. 1
Natural varianti176H → Y in strain: KZ1340; probably inactive. 1
Natural varianti195A → V in strain: 8-6, NCIB 10663 and NCIB 10748. 1
Natural varianti202D → A in strain: NCIB 10691 and CER 89L1105. 1
Natural varianti205A → T in strain: NCIB 10691 and CER 89L1105. 1
Natural varianti281K → N in strain: 8-6. 1
Natural varianti329T → A in strain: 8-6. 1
Natural varianti363P → S in strain: NCIB 10691 and CER 89L1105. 1
Natural varianti373I → L in strain: PB6K. 1
Natural varianti373I → V in strain: 8-6, NCIB 10662, L9, NCIB 10663, NCIB 10748, CER 89L43 and KZ1340. 1

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.
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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Phylogenomic databases

KOiK16619.
OMAiDHFWDPD.
OrthoDBiPOG091H10JI.

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: November 30, 2016
This is version 73 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.