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Q46150 (PHLC_CLONO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Phospholipase C
Short name=PLC
EC=3.1.4.3
Alternative name(s):
Gamma-toxin
Phosphatidylcholine cholinephosphohydrolase
Gene names
Name:plc
OrganismClostridium novyi
Taxonomic identifier1542 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium

Protein attributes

Sequence length398 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Bacterial hemolysins are exotoxins that attack blood cell membranes and cause cell rupture. Binds to eukaryotic membranes where it hydrolyzes phosphatidylcholine, sphingomyelin and phosphatidylethanolamine. 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 By similarity. This enzyme is hemolytic against horse erythrocytes.

Catalytic activity

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

Cofactor

Binds 3 calcium ions per subunit By similarity.

Binds 3 zinc ions per subunit By similarity.

Subcellular location

Secreted By similarity.

Domain

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 similarities

Belongs to the bacterial zinc-metallophospholipase C family.

Contains 1 PLAT domain.

Contains 1 Zn-dependent PLC domain.

Ontologies

Keywords
   Biological processCytolysis
Hemolysis
   Cellular componentSecreted
   DomainSignal
   LigandCalcium
Metal-binding
Zinc
   Molecular functionHydrolase
Toxin
Gene Ontology (GO)
   Biological_processcytolysis

Inferred from electronic annotation. Source: UniProtKB-KW

hemolysis in other organism

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionphosphatidylcholine phospholipase C activity

Inferred from electronic annotation. Source: EC

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2828 By similarity
Chain29 – 398370Phospholipase C
PRO_0000023935

Regions

Domain29 – 278250Zn-dependent PLC
Domain284 – 398115PLAT
Region275 – 2839Linker

Sites

Metal binding291Zinc 1 By similarity
Metal binding391Zinc 1 By similarity
Metal binding841Zinc 3 By similarity
Metal binding961Zinc 3 By similarity
Metal binding1541Zinc 3 By similarity
Metal binding1581Zinc 1 By similarity
Metal binding1581Zinc 3 By similarity
Metal binding1641Zinc 2 By similarity
Metal binding1761Zinc 2 By similarity
Metal binding1801Zinc 2 By similarity
Metal binding2991Calcium 1; via carbonyl oxygen By similarity
Metal binding3001Calcium 3 By similarity
Metal binding3011Calcium 3 By similarity
Metal binding3211Calcium 2 By similarity
Metal binding3221Calcium 2 By similarity
Metal binding3241Calcium 2; via carbonyl oxygen By similarity
Metal binding3251Calcium 3 By similarity
Metal binding3261Calcium 2 By similarity
Metal binding3261Calcium 3 By similarity
Metal binding3641Calcium 1 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q46150 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 7EFBEDD516CC7E58

FASTA39845,952
        10         20         30         40         50         60 
MKKKFLKGLC CAFVISITCL GASSKAYGWD GKKDGTGTHS MIVTQAVKVL ENDMSKDEPE 

        70         80         90        100        110        120 
IVKQNFKILQ DNMHKFQLGS TYPDYDPNAY KLFQDHFWDP DTDHNFSKDN LWYLSYSIKD 

       130        140        150        160        170        180 
TAESQVRKFT ALARNEWEKG NYEKATWYFG QAMHYFGDLN TPYHAANVTA VDSIGHTKYE 

       190        200        210        220        230        240 
GFAEKRKDQY RINTTGIKTN EGFYADALKN SNFDSWSKEY CKGWAKQAKN LYYSHSTMKH 

       250        260        270        280        290        300 
TNEDWDYSAS HALKNAQMGT AGCIYRFLYD VSKDLLPTEN HKINGLMVVI KTANEIAAGT 

       310        320        330        340        350        360 
DDYVYFGIER KDGTVQEWTL DNPGNDFEAN QEDTYILKIK KPSIKFSDIN RMWIRKANFT 

       370        380        390 
PVSDDWKVKG IKVIADGSVQ YEKQINKWIH GNEKYYIN

« Hide

References

[1]"Phylogenetic analysis of phospholipase C genes from Clostridium perfringens types A to E and Clostridium novyi."
Tsutsui K., Minami J., Matsushita O., Katayama S., Taniguchi Y., Nakamura S., Nishioka M., Okabe A.
J. Bacteriol. 177:7164-7170(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: CL49 / Type A.
[2]"Phospholipase C from Clostridium novyi type A. I."
Taguchi R., Ikezawa H.
Biochim. Biophys. Acta 409:75-85(1975) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
Strain: IID 140 / Type A.
[3]"Structure and function of clostridial phospholipases C."
Jepson M., Titball R.W.
Microbes Infect. 2:1277-1284(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		D32125 Genomic DNA. Translation: BAA06851.1.

3D structure databases

ProteinModelPortalQ46150.
SMRQ46150. Positions 29-395.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D1.10.575.10. 1 hit.
2.60.60.20. 1 hit.
InterProIPR008976. Lipase_LipOase.
IPR001024. LipOase_LH2.
IPR008947. PLipase_C/P1_nuclease.
IPR001531. PLipaseC_domain.
[Graphical view]
PfamPF01477. PLAT. 1 hit.
[Graphical view]
PRINTSPR00479. PRPHPHLPASEC.
ProDomPD003946. PLipaseC_Zn-bd_prok. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00770. Zn_dep_PLPC. 1 hit.
[Graphical view]
SUPFAMSSF49723. Lipase_LipOase. 1 hit.
SSF48537. PLC_Nuclease. 1 hit.
PROSITEPS50095. PLAT. 1 hit.
PS00384. PROKAR_ZN_DEPEND_PLPC_1. 1 hit.
PS51346. PROKAR_ZN_DEPEND_PLPC_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePHLC_CLONO
AccessionPrimary (citable) accession number: Q46150
Entry history
Integrated into UniProtKB/Swiss-Prot: October 10, 2002
Last sequence update: November 1, 1996
Last modified: April 3, 2013
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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