plc

Functionⁱ

Bacterial hemolysins are exotoxins that attack blood cell membranes and cause cell rupture. Binds to eukaryotic membranes where it hydrolyzes phosphatidylcholine. This enzyme has 10-fold less activity towards sphingomyelin than its C.perfringens counterpart, is approximately 100-fold less hemolytic against mouse erythrocytes and at least 100-fold less toxic in mice.

Miscellaneous

A hybrid protein between the N-terminus of C.bifermentans and the C-terminus of C.perfringens has an activity intermediate between the two.

Catalytic activityⁱ

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

Cofactorⁱ

Protein has several cofactor binding sites:

Ca²⁺By similarityNote: Binds 3 Ca²⁺ ions per subunit.By similarity
Zn²⁺
PROSITE-ProRule annotation
Manual assertion according to rulesⁱ
- PROSITE-ProRule:PRU00678
Note: Binds 3 Zn²⁺ ions per subunit.
PROSITE-ProRule annotation
Manual assertion according to rulesⁱ
- PROSITE-ProRule:PRU00678

Sites

Feature key	Position(s)	DescriptionActions	Length
Metal bindingⁱ	27	Zinc 1PROSITE-ProRule annotation	1
Metal bindingⁱ	37	Zinc 1PROSITE-ProRule annotation	1
Metal bindingⁱ	82	Zinc 3PROSITE-ProRule annotation	1
Metal bindingⁱ	94	Zinc 3PROSITE-ProRule annotation	1
Metal bindingⁱ	152	Zinc 3PROSITE-ProRule annotation	1
Metal bindingⁱ	156	Zinc 1PROSITE-ProRule annotation	1
Metal bindingⁱ	156	Zinc 3PROSITE-ProRule annotation	1
Metal bindingⁱ	162	Zinc 2PROSITE-ProRule annotation	1
Metal bindingⁱ	174	Zinc 2PROSITE-ProRule annotation	1
Metal bindingⁱ	178	Zinc 2PROSITE-ProRule annotation	1
Metal bindingⁱ	297	Calcium 1; via carbonyl oxygenBy similarity	1
Metal bindingⁱ	298	Calcium 3By similarity	1
Metal bindingⁱ	299	Calcium 3By similarity	1
Metal bindingⁱ	319	Calcium 2By similarity	1
Metal bindingⁱ	320	Calcium 2By similarity	1
Metal bindingⁱ	322	Calcium 2; via carbonyl oxygenBy similarity	1
Metal bindingⁱ	323	Calcium 3By similarity	1
Metal bindingⁱ	324	Calcium 2By similarity	1
Metal bindingⁱ	324	Calcium 3By similarity	1
Metal bindingⁱ	363	Calcium 1By similarity	1

GO - Molecular functionⁱ

phosphatidylcholine phospholipase C activity Source: UniProtKB-EC
toxin activity Source: UniProtKB-KW
zinc ion binding Source: InterPro

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

hemolysis in other organism Source: UniProtKB-KW

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Hydrolase, Toxin
Biological process	Cytolysis, Hemolysis
Ligand	Calcium, Metal-binding, Zinc

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Phospholipase C (EC:3.1.4.3) Short name: PLC Alternative name(s): Cbp Phosphatidylcholine cholinephosphohydrolase
Gene namesⁱ	Name:plc Synonyms:cbp
Organismⁱ	Paraclostridium bifermentans (Clostridium bifermentans)
Taxonomic identifierⁱ	1490 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Bacteria › Terrabacteria group › Firmicutes › Clostridia › Clostridiales › Peptostreptococcaceae › Paraclostridium

Subcellular locationⁱ

Secreted
PROSITE-ProRule annotation
Manual assertion according to rulesⁱ
- PROSITE-ProRule:PRU00678

GO - Cellular componentⁱ

extracellular region Source: UniProtKB-SubCell

View the complete GO annotation on QuickGO ...

Keywords - Cellular componentⁱ

Secreted

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Signal peptideⁱ	1 – 26	By similarityAdd BLAST		26
ChainⁱPRO_0000023933	27 – 398	Phospholipase CAdd BLAST		372

Structureⁱ

3D structure databases

ProteinModelPortalⁱ	P20419.
SMRⁱ	P20419.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	27 – 276	Zn-dependent PLCPROSITE-ProRule annotationAdd BLAST		250
Domainⁱ	282 – 398	PLATPROSITE-ProRule annotationAdd BLAST		117

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	273 – 281	Linker		9

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 is conferred by this C-terminal domain (By similarity).By similarity

Sequence similaritiesⁱ

Belongs to the bacterial zinc-metallophospholipase C family.PROSITE-ProRule annotation

Keywords - Domainⁱ

Signal

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd11009. Zn_dep_PLPC. 1 hit.
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.
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF01477. PLAT. 1 hit. PF00882. Zn_dep_PLPC. 1 hit.
PRINTSⁱ	PR00479. PRPHPHLPASEC.
ProDomⁱ	View protein in ProDom or Entries sharing at least one domain PD003946. PLipaseC_Zn-bd_prok. 1 hit.
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.

Sequenceⁱ

Sequence statusⁱ: Complete.

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

P20419-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MKALKKVSNI LCVLGLCTLM GGTSYAWDGK KDGTGTHSLI AEHGLSMLNN 
        60         70         80         90        100
DLSGNESQQV KDNIKILNEY LGDLKLGSTY PDYDPNAYDL YQDHFYDPDT 
       110        120        130        140        150
GNNFTIDNSW YASYPIYDTS RNSVRKFATL AKNEWEKGNF KEATFLLGQG 
       160        170        180        190        200
LHYLGDLNTP YHASNVTAVD SPGHVKYETF VEERKDNYAL NTSGNDTTSG 
       210        220        230        240        250
VYKEAMENPS FNKWMTQNSI KYAKIAKDLY YSHSTMSHSW DDWDYSGREA 
       260        270        280        290        300
IKNSQVCTAG FLYRFMNEVS NGNTGDNDSL TNEFNIVLKT ADNKYAGTDD 
       310        320        330        340        350
NVYFGFETNE GKKFEWKLDN AGNDFERNQV DNYILKTKDG EEVDINNISN 
       360        370        380        390 
YWIRKERLTS ISDDWELSNF KLIANGKVIQ QQDVNKVFTG NETYYINK

Length:398

Mass (Da):45,366

Last modified:February 1, 1991 - v1

Checksum:ⁱ0B628AFE7146BC56

GO

Experimental Info

Feature key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	120 – 123	SRNS → AETQ (PubMed:10377104).Curated	4
Sequence conflictⁱ	120 – 123	SRNS → AETQ (PubMed:12540540).Curated	4
Sequence conflictⁱ	272 – 274	GNT → ENI in BAB83265 (PubMed:12540540).Curated	3
Sequence conflictⁱ	280	L → S in BAB83265 (PubMed:12540540).Curated	1
Sequence conflictⁱ	311	G → D in BAB83265 (PubMed:12540540).Curated	1
Sequence conflictⁱ	357	R → K in BAB83265 (PubMed:12540540).Curated	1

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AF072123 Genomic DNA. Translation: AAD41623.1. AB061869 Genomic DNA. Translation: BAB83265.1.
PIRⁱ	B30565.

Protein	Similar proteins	Organisms	Length	Cluster ID	Cluster name	Size
P20419	T4W0L1 A0A1X2JFE9 A0A099HS94 A0A0M3DHL3 T4VH92 UPI00040F8C3B UPI0009EC95E3	Paraclostridium bifermentans ATCC 19299 Paraclostridium bifermentans (Clostridium bifermentans) Clostridium sp. NCR Paraclostridium benzoelyticum Paraclostridium bifermentans ATCC 638 Candidatus Dorea massiliensis	398	UniRef90_P20419	Cluster: Phospholipase C	8

Protein	Similar proteins	Organisms	Length	Cluster ID	Cluster name	Size
P20419	A0A099HS94 A0A0M3DHL3 UPI00040F8C3B UPI0009EC95E3 T4VH92 A0A1X2JFE9 T4W0L1	Clostridium sp. NCR Paraclostridium benzoelyticum Paraclostridium bifermentans (Clostridium bifermentans) Candidatus Dorea massiliensis Paraclostridium bifermentans ATCC 638 Paraclostridium bifermentans ATCC 19299	398	UniRef50_P20419	Cluster: Phospholipase C	8

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AF072123 Genomic DNA. Translation: AAD41623.1. AB061869 Genomic DNA. Translation: BAB83265.1.
PIRⁱ	B30565.

3D structure databases

ProteinModelPortalⁱ	P20419.
SMRⁱ	P20419.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd11009. Zn_dep_PLPC. 1 hit.
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.
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF01477. PLAT. 1 hit. PF00882. Zn_dep_PLPC. 1 hit.
PRINTSⁱ	PR00479. PRPHPHLPASEC.
ProDomⁱ	View protein in ProDom or Entries sharing at least one domain PD003946. PLipaseC_Zn-bd_prok. 1 hit.
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.
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	PHLC_PARBF
Accessionⁱ	P20419Primary (citable) accession number: P20419 Secondary accession number(s): Q8VUZ4, Q9S532
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
	Last sequence update:	February 1, 1991
	Last modified:	March 28, 2018
	This is version 114 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Prokaryotic Protein Annotation Program

UniProtKB - P20419 (PHLC_PARBF)

Your basket is currently empty. ⁱ

Phospholipase C

Select a section on the left to see content.

Functionⁱ

Miscellaneous

Catalytic activityⁱ

Cofactorⁱ

Sites

GO - Molecular functionⁱ

GO - Biological processⁱ

Keywordsⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

Keywords - Cellular componentⁱ

PTM / Processingⁱ

Molecule processing

Structureⁱ

3D structure databases

Family & Domainsⁱ

Domains and Repeats

Region

Domainⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Family and domain databases

Sequenceⁱ

Experimental Info

Sequence databases

Similar proteinsⁱ

Cross-referencesⁱ

Sequence databases

3D structure databases

Protocols and materials databases

Family and domain databases

Entry informationⁱ

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P20419 (PHLC_PARBF)

Your basket is currently empty. i <p>When browsing through different UniProt proteins, you can use the ‘basket’ to save them, so that you can back to find or analyse them later.<p><a href='/help/basket' target='_top'>More...</a></p>

Phospholipase C

plc

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Miscellaneous

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Cellular componenti

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Region

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Family and domain databases

Experimental Info

Sequence databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protocols and materials databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

Your basket is currently empty. ⁱ

Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

PTM / Processingⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Cross-referencesⁱ

Entry informationⁱ