PHLC_CLONO
ID PHLC_CLONO Reviewed; 398 AA.
AC Q46150;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Phospholipase C;
DE Short=PLC;
DE EC=3.1.4.3;
DE AltName: Full=Gamma-toxin;
DE AltName: Full=Phosphatidylcholine cholinephosphohydrolase;
DE Flags: Precursor;
GN Name=plc;
OS Clostridium novyi.
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1542;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=CL49 / Type A;
RX PubMed=8522524; DOI=10.1128/jb.177.24.7164-7170.1995;
RA Tsutsui K., Minami J., Matsushita O., Katayama S., Taniguchi Y.,
RA Nakamura S., Nishioka M., Okabe A.;
RT "Phylogenetic analysis of phospholipase C genes from Clostridium
RT perfringens types A to E and Clostridium novyi.";
RL J. Bacteriol. 177:7164-7170(1995).
RN [2]
RP CHARACTERIZATION.
RC STRAIN=IID 140 / Type A;
RX PubMed=241423; DOI=10.1016/0005-2760(75)90082-x;
RA Taguchi R., Ikezawa H.;
RT "Phospholipase C from Clostridium novyi type A. I.";
RL Biochim. Biophys. Acta 409:75-85(1975).
RN [3]
RP REVIEW.
RX PubMed=11008117; DOI=10.1016/s1286-4579(00)01281-8;
RA Jepson M., Titball R.W.;
RT "Structure and function of clostridial phospholipases C.";
RL Microbes Infect. 2:1277-1284(2000).
CC -!- FUNCTION: Bacterial hemolysins are exotoxins that attack blood cell
CC membranes and cause cell rupture. Binds to eukaryotic membranes where
CC it hydrolyzes phosphatidylcholine, sphingomyelin and
CC phosphatidylethanolamine. The diacylglycerol produced can activate both
CC the arachidonic acid pathway, leading to modulation of the inflammatory
CC response cascade and thrombosis, and protein kinase C, leading to
CC activation of eukaryotic phospholipases and further membrane damage (By
CC similarity). This enzyme is hemolytic against horse erythrocytes.
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1,2-diacyl-
CC sn-glycerol + H(+) + phosphocholine; Xref=Rhea:RHEA:10604,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17815,
CC ChEBI:CHEBI:57643, ChEBI:CHEBI:295975; EC=3.1.4.3;
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Note=Binds 3 Ca(2+) ions per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00678};
CC Note=Binds 3 Zn(2+) ions per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00678};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000255|PROSITE-ProRule:PRU00678}.
CC -!- DOMAIN: The protein is composed of 2 domains; the N-terminal domain
CC contains the phospholipase C active site (PLC), in a cleft which is
CC also occupied by the 3 zinc ions. The C-terminal domain is a putative
CC phospholipid-recognition domain, which shows structural homology with
CC phospholipid-binding C2-like domains from a range of eukaryotic
CC proteins. The ability to bind membrane phospholipids in a Ca(2+)
CC dependent manner and toxicity is conferred by this C-terminal domain,
CC which also contributes to the sphingomyelinase activity.
CC -!- SIMILARITY: Belongs to the bacterial zinc-metallophospholipase C
CC family. {ECO:0000255|PROSITE-ProRule:PRU00678}.
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DR EMBL; D32125; BAA06851.1; -; Genomic_DNA.
DR AlphaFoldDB; Q46150; -.
DR SMR; Q46150; -.
DR OMA; DHFWDPD; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0034480; F:phosphatidylcholine phospholipase C activity; IEA:UniProtKB-EC.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR CDD; cd11009; Zn_dep_PLPC; 1.
DR Gene3D; 1.10.575.10; -; 1.
DR InterPro; IPR001024; PLAT/LH2_dom.
DR InterPro; IPR036392; PLAT/LH2_dom_sf.
DR InterPro; IPR008947; PLipase_C/P1_nuclease_dom_sf.
DR InterPro; IPR029002; PLPC/GPLD1.
DR InterPro; IPR001531; Zn_PLipaseC.
DR Pfam; PF01477; PLAT; 1.
DR Pfam; PF00882; Zn_dep_PLPC; 1.
DR PRINTS; PR00479; PRPHPHLPASEC.
DR SMART; SM00770; Zn_dep_PLPC; 1.
DR SUPFAM; SSF48537; SSF48537; 1.
DR SUPFAM; SSF49723; SSF49723; 1.
DR PROSITE; PS50095; PLAT; 1.
DR PROSITE; PS00384; PROKAR_ZN_DEPEND_PLPC_1; 1.
DR PROSITE; PS51346; PROKAR_ZN_DEPEND_PLPC_2; 1.
PE 1: Evidence at protein level;
KW Calcium; Cytolysis; Hemolysis; Hydrolase; Metal-binding; Secreted; Signal;
KW Toxin; Virulence; Zinc.
FT SIGNAL 1..28
FT /evidence="ECO:0000250"
FT CHAIN 29..398
FT /note="Phospholipase C"
FT /id="PRO_0000023935"
FT DOMAIN 29..278
FT /note="Zn-dependent PLC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00678"
FT DOMAIN 284..398
FT /note="PLAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT REGION 275..283
FT /note="Linker"
FT BINDING 29
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00678"
FT BINDING 39
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00678"
FT BINDING 84
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00678"
FT BINDING 96
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00678"
FT BINDING 154
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00678"
FT BINDING 158
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00678"
FT BINDING 158
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00678"
FT BINDING 164
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00678"
FT BINDING 176
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00678"
FT BINDING 180
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00678"
FT BINDING 299
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 300
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 301
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 321
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 322
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 324
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 325
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 326
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 326
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 364
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
SQ SEQUENCE 398 AA; 45952 MW; 7EFBEDD516CC7E58 CRC64;
MKKKFLKGLC CAFVISITCL GASSKAYGWD GKKDGTGTHS MIVTQAVKVL ENDMSKDEPE
IVKQNFKILQ DNMHKFQLGS TYPDYDPNAY KLFQDHFWDP DTDHNFSKDN LWYLSYSIKD
TAESQVRKFT ALARNEWEKG NYEKATWYFG QAMHYFGDLN TPYHAANVTA VDSIGHTKYE
GFAEKRKDQY RINTTGIKTN EGFYADALKN SNFDSWSKEY CKGWAKQAKN LYYSHSTMKH
TNEDWDYSAS HALKNAQMGT AGCIYRFLYD VSKDLLPTEN HKINGLMVVI KTANEIAAGT
DDYVYFGIER KDGTVQEWTL DNPGNDFEAN QEDTYILKIK KPSIKFSDIN RMWIRKANFT
PVSDDWKVKG IKVIADGSVQ YEKQINKWIH GNEKYYIN
