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Protein

Phospholipase C

Gene

plc

Organism
Clostridium novyi
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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.By similarity

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 annotationNote: Binds 3 Zn2+ ions per subunit.PROSITE-ProRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi29 – 291Zinc 1PROSITE-ProRule annotation
Metal bindingi39 – 391Zinc 1PROSITE-ProRule annotation
Metal bindingi84 – 841Zinc 3PROSITE-ProRule annotation
Metal bindingi96 – 961Zinc 3PROSITE-ProRule annotation
Metal bindingi154 – 1541Zinc 3PROSITE-ProRule annotation
Metal bindingi158 – 1581Zinc 1PROSITE-ProRule annotation
Metal bindingi158 – 1581Zinc 3PROSITE-ProRule annotation
Metal bindingi164 – 1641Zinc 2PROSITE-ProRule annotation
Metal bindingi176 – 1761Zinc 2PROSITE-ProRule annotation
Metal bindingi180 – 1801Zinc 2PROSITE-ProRule annotation
Metal bindingi299 – 2991Calcium 1; via carbonyl oxygenBy similarity
Metal bindingi300 – 3001Calcium 3By similarity
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 1By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Toxin

Keywords - Biological processi

Cytolysis, Hemolysis

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):
Gamma-toxin
Phosphatidylcholine cholinephosphohydrolase
Gene namesi
Name:plc
OrganismiClostridium novyi
Taxonomic identifieri1542 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Subcellular locationi

  • Secreted PROSITE-ProRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2828By similarityAdd
BLAST
Chaini29 – 398370Phospholipase CPRO_0000023935Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi386415.NT01CX_0979.

Structurei

3D structure databases

ProteinModelPortaliQ46150.
SMRiQ46150. Positions 29-395.
ModBaseiSearch...
MobiDBiSearch...

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

eggNOGiENOG41064S2. Bacteria.
ENOG4112CMR. LUCA.

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.
IPR001531. PLipaseC_domain.
IPR029002. PLPC/GPLD1.
[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.

Q46150-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKKFLKGLC CAFVISITCL GASSKAYGWD GKKDGTGTHS MIVTQAVKVL
60 70 80 90 100
ENDMSKDEPE IVKQNFKILQ DNMHKFQLGS TYPDYDPNAY KLFQDHFWDP
110 120 130 140 150
DTDHNFSKDN LWYLSYSIKD TAESQVRKFT ALARNEWEKG NYEKATWYFG
160 170 180 190 200
QAMHYFGDLN TPYHAANVTA VDSIGHTKYE GFAEKRKDQY RINTTGIKTN
210 220 230 240 250
EGFYADALKN SNFDSWSKEY CKGWAKQAKN LYYSHSTMKH TNEDWDYSAS
260 270 280 290 300
HALKNAQMGT AGCIYRFLYD VSKDLLPTEN HKINGLMVVI KTANEIAAGT
310 320 330 340 350
DDYVYFGIER KDGTVQEWTL DNPGNDFEAN QEDTYILKIK KPSIKFSDIN
360 370 380 390
RMWIRKANFT PVSDDWKVKG IKVIADGSVQ YEKQINKWIH GNEKYYIN
Length:398
Mass (Da):45,952
Last modified:November 1, 1996 - v1
Checksum:i7EFBEDD516CC7E58
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D32125 Genomic DNA. Translation: BAA06851.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D32125 Genomic DNA. Translation: BAA06851.1.

3D structure databases

ProteinModelPortaliQ46150.
SMRiQ46150. Positions 29-395.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi386415.NT01CX_0979.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG41064S2. Bacteria.
ENOG4112CMR. LUCA.

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.
IPR001531. PLipaseC_domain.
IPR029002. PLPC/GPLD1.
[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...

Publicationsi

  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.

Entry informationi

Entry nameiPHLC_CLONO
AccessioniPrimary (citable) accession number: Q46150
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 10, 2002
Last sequence update: November 1, 1996
Last modified: November 11, 2015
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. 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.