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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)DescriptionActionsGraphical viewLength
Metal bindingi29Zinc 1PROSITE-ProRule annotation1
Metal bindingi39Zinc 1PROSITE-ProRule annotation1
Metal bindingi84Zinc 3PROSITE-ProRule annotation1
Metal bindingi96Zinc 3PROSITE-ProRule annotation1
Metal bindingi154Zinc 3PROSITE-ProRule annotation1
Metal bindingi158Zinc 1PROSITE-ProRule annotation1
Metal bindingi158Zinc 3PROSITE-ProRule annotation1
Metal bindingi164Zinc 2PROSITE-ProRule annotation1
Metal bindingi176Zinc 2PROSITE-ProRule annotation1
Metal bindingi180Zinc 2PROSITE-ProRule annotation1
Metal bindingi299Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi300Calcium 3By similarity1
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 1By similarity1

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)DescriptionActionsGraphical viewLength
Signal peptidei1 – 28By similarityAdd BLAST28
ChainiPRO_000002393529 – 398Phospholipase CAdd BLAST370

Interactioni

Protein-protein interaction databases

STRINGi386415.NT01CX_0979.

Structurei

3D structure databases

ProteinModelPortaliQ46150.
ModBaseiSearch...
MobiDBiSearch...

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

eggNOGiENOG41064S2. Bacteria.
ENOG4112CMR. LUCA.

Family and domain databases

CDDicd11009. Zn_dep_PLPC. 1 hit.
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.

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.
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

CDDicd11009. Zn_dep_PLPC. 1 hit.
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 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: October 5, 2016
This is version 102 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.