UniProtKB - Q0TV31 (PHLC_CLOP1)
Phospholipase C
plc
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.
Miscellaneous
Catalytic activityi
- EC:3.1.4.3
Cofactori
Protein has several cofactor binding sites:Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 29 | Zinc 1 | 1 | |
Metal bindingi | 39 | Zinc 1 | 1 | |
Metal bindingi | 84 | Zinc 3 | 1 | |
Metal bindingi | 96 | Zinc 3 | 1 | |
Metal bindingi | 154 | Zinc 3 | 1 | |
Metal bindingi | 158 | Zinc 1 | 1 | |
Metal bindingi | 158 | Zinc 3 | 1 | |
Metal bindingi | 164 | Zinc 2Curated | 1 | |
Metal bindingi | 176 | Zinc 2Curated | 1 | |
Metal bindingi | 180 | Zinc 2Curated | 1 | |
Metal bindingi | 297 | Calcium 1 | 1 | |
Metal bindingi | 299 | Calcium 1; via carbonyl oxygen | 1 | |
Metal bindingi | 300 | Calcium 3 | 1 | |
Metal bindingi | 301 | Calcium 3 | 1 | |
Metal bindingi | 321 | Calcium 2 | 1 | |
Metal bindingi | 322 | Calcium 2 | 1 | |
Metal bindingi | 324 | Calcium 2; via carbonyl oxygen | 1 | |
Metal bindingi | 325 | Calcium 3 | 1 | |
Metal bindingi | 326 | Calcium 2 | 1 | |
Metal bindingi | 326 | Calcium 3 | 1 | |
Metal bindingi | 364 | Calcium 1 | 1 | |
Metal bindingi | 365 | Calcium 1; via carbonyl oxygen | 1 |
GO - Molecular functioni
- hydrolase activity Source: CACAO
- phosphatidylcholine phospholipase C activity Source: UniProtKB-EC
- toxin activity Source: UniProtKB-KW
- zinc ion binding Source: InterPro
GO - Biological processi
- hemolysis in another organism Source: CACAO
Keywordsi
Molecular function | Hydrolase, Toxin |
Biological process | Cytolysis, Hemolysis, Virulence |
Ligand | 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:CPF_0042 |
Organismi | Clostridium perfringens (strain ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 / Type A) |
Taxonomic identifieri | 195103 [NCBI] |
Taxonomic lineagei | Bacteria › Firmicutes › Clostridia › Eubacteriales › Clostridiaceae › Clostridium › |
Proteomesi |
|
Subcellular locationi
Extracellular region or secreted
Extracellular region or secreted
- extracellular region Source: UniProtKB-SubCell
Keywords - Cellular componenti
SecretedPathology & Biotechi
Biotechnological usei
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 278 – 398 | Missing : Loss of sphingomyelinase, hemolytic activity and lethality. 1 PublicationAdd BLAST | 121 | |
Mutagenesisi | 297 | D → Y: Binds less Ca(2+), small decrease in PLC, sphingomyelinase and myotoxicity, increased hemolytic and cytotoxic activities. 2 Publications | 1 | |
Mutagenesisi | 303 | Y → F or N: Increased dependence of PLC on Ca(2+). Dramatically decreases hemolytic, cytotoxic and myotoxic activities. 1 Publication | 1 | |
Mutagenesisi | 321 | D → S: Reduces affinity for Ca(2+), decreases toxin activity. 1 Publication | 1 | |
Mutagenesisi | 333 | D → G: Decreases toxin activity in vivo and against aggregated substrates in vitro. May destabilize interactions between the N and C-terminal domains. 1 Publication | 1 | |
Mutagenesisi | 335 | Y → F: Dramatically decreases hemolytic and cytotoxic activities. 1 Publication | 1 | |
Mutagenesisi | 358 | K → E: Decreases toxin activity in vivo and against aggregated substrates in vitro. 1 Publication | 1 | |
Mutagenesisi | 359 | Y → F or L: Dramatically decreases hemolytic and cytotoxic activities. 2 Publications | 1 | |
Mutagenesisi | 362 | F → I: Dramatically decreases sphingomyelinase, cytotoxicity and hemolytic and myotoxic activities. 1 Publication | 1 | |
Mutagenesisi | 364 | D → N: Increased dependence of PLC on Ca(2+). Dramatically decreases hemolytic, cytotoxic and myotoxic activities. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 28 | 2 PublicationsAdd BLAST | 28 | |
ChainiPRO_0000259456 | 29 – 398 | Phospholipase CAdd BLAST | 370 |
Proteomic databases
PRIDEi | Q0TV31 |
Structurei
Secondary structure
3D structure databases
AlphaFoldDBi | Q0TV31 |
SMRi | Q0TV31 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | Q0TV31 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 29 – 278 | Zn-dependent PLCPROSITE-ProRule annotationAdd BLAST | 250 | |
Domaini | 284 – 398 | PLATPROSITE-ProRule annotationAdd BLAST | 115 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 275 – 283 | Linker | 9 |
Domaini
Sequence similaritiesi
Keywords - Domaini
SignalPhylogenomic databases
eggNOGi | ENOG5033QPJ, Bacteria |
HOGENOMi | CLU_690198_0_0_9 |
OMAi | DHFWDPD |
OrthoDBi | 753730at2 |
Family and domain databases
Gene3Di | 1.10.575.10, 1 hit |
InterProi | View protein in InterPro IPR001024, PLAT/LH2_dom IPR036392, PLAT/LH2_dom_sf IPR008947, PLipase_C/P1_nuclease_dom_sf IPR029002, PLPC/GPLD1 IPR001531, Zn_PLipaseC |
Pfami | View protein in Pfam PF01477, PLAT, 1 hit PF00882, Zn_dep_PLPC, 1 hit |
PRINTSi | PR00479, PRPHPHLPASEC |
SMARTi | View protein in SMART SM00770, Zn_dep_PLPC, 1 hit |
SUPFAMi | SSF48537, SSF48537, 1 hit SSF49723, SSF49723, 1 hit |
PROSITEi | View protein in PROSITE PS50095, PLAT, 1 hit PS00384, PROKAR_ZN_DEPEND_PLPC_1, 1 hit PS51346, PROKAR_ZN_DEPEND_PLPC_2, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
10 20 30 40 50
MKRKICKALI CAALATSLWA 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
EAFYTDILKN 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 AFSDAYKPEN IKIIANGKVV VDKDINEWIS GNSTYNIK
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 17 | S → T no nucleotide entry (PubMed:2536356).Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M24904 Genomic DNA Translation: AAA23272.1 X13608 Genomic DNA Translation: CAA31943.1 CP000246 Genomic DNA Translation: ABG84486.1 |
PIRi | A30565 |
RefSeqi | WP_011590041.1, NC_008261.1 |
Genome annotation databases
EnsemblBacteriai | ABG84486; ABG84486; CPF_0042 |
GeneIDi | 29569865 |
KEGGi | cpf:CPF_0042 |
Similar proteinsi
Cross-referencesi
Web resourcesi
Worthington enzyme manual |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M24904 Genomic DNA Translation: AAA23272.1 X13608 Genomic DNA Translation: CAA31943.1 CP000246 Genomic DNA Translation: ABG84486.1 |
PIRi | A30565 |
RefSeqi | WP_011590041.1, NC_008261.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1QM6 | X-ray | 2.50 | A/B | 29-398 | [»] | |
1QMD | X-ray | 2.20 | A/B | 29-398 | [»] | |
2WXT | X-ray | 2.00 | A | 29-398 | [»] | |
2WXU | X-ray | 1.80 | A | 29-398 | [»] | |
2WY6 | X-ray | 3.20 | A/B/C | 29-398 | [»] | |
AlphaFoldDBi | Q0TV31 | |||||
SMRi | Q0TV31 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
STRINGi | 195103.CPF_0042 |
Proteomic databases
PRIDEi | Q0TV31 |
Genome annotation databases
EnsemblBacteriai | ABG84486; ABG84486; CPF_0042 |
GeneIDi | 29569865 |
KEGGi | cpf:CPF_0042 |
Phylogenomic databases
eggNOGi | ENOG5033QPJ, Bacteria |
HOGENOMi | CLU_690198_0_0_9 |
OMAi | DHFWDPD |
OrthoDBi | 753730at2 |
Miscellaneous databases
EvolutionaryTracei | Q0TV31 |
Family and domain databases
Gene3Di | 1.10.575.10, 1 hit |
InterProi | View protein in InterPro IPR001024, PLAT/LH2_dom IPR036392, PLAT/LH2_dom_sf IPR008947, PLipase_C/P1_nuclease_dom_sf IPR029002, PLPC/GPLD1 IPR001531, Zn_PLipaseC |
Pfami | View protein in Pfam PF01477, PLAT, 1 hit PF00882, Zn_dep_PLPC, 1 hit |
PRINTSi | PR00479, PRPHPHLPASEC |
SMARTi | View protein in SMART SM00770, Zn_dep_PLPC, 1 hit |
SUPFAMi | SSF48537, SSF48537, 1 hit SSF49723, SSF49723, 1 hit |
PROSITEi | View protein in PROSITE PS50095, PLAT, 1 hit PS00384, PROKAR_ZN_DEPEND_PLPC_1, 1 hit PS51346, PROKAR_ZN_DEPEND_PLPC_2, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | PHLC_CLOP1 | |
Accessioni | Q0TV31Primary (citable) accession number: Q0TV31 Secondary accession number(s): P15310 Q60121 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | October 31, 2006 |
Last sequence update: | September 5, 2006 | |
Last modified: | May 25, 2022 | |
This is version 98 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencingDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families