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Protein

Phospholipase C

Gene

plc

Organism
Clostridium novyi
Status
Reviewed-Annotation score: -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

Keywordsi

Molecular functionHydrolase, Toxin
Biological processCytolysis, Hemolysis
LigandCalcium, 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

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 28By similarityAdd BLAST28
ChainiPRO_000002393529 – 398Phospholipase CAdd BLAST370

Structurei

3D structure databases

ProteinModelPortaliQ46150
SMRiQ46150
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

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
InterProiView 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
PfamiView protein in Pfam
PF01477 PLAT, 1 hit
PF00882 Zn_dep_PLPC, 1 hit
PRINTSiPR00479 PRPHPHLPASEC
ProDomiView protein in ProDom or Entries sharing at least one domain
PD003946 PLipaseC_Zn-bd_prok, 1 hit
SMARTiView protein in SMART
SM00770 Zn_dep_PLPC, 1 hit
SUPFAMiSSF48537 SSF48537, 1 hit
SSF49723 SSF49723, 1 hit
PROSITEiView 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.

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

Genome annotation databases

GeneIDi4541971

Similar proteinsi

Entry informationi

Entry nameiPHLC_CLONO
AccessioniPrimary (citable) accession number: Q46150
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 10, 2002
Last sequence update: November 1, 1996
Last modified: March 28, 2018
This is version 109 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

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