PHLC1_CLOPE
ID PHLC1_CLOPE Reviewed; 398 AA.
AC P0C216; P15310; P94658; Q46246; Q46279; Q46280; Q46281; Q46282; Q57317;
AC Q59303; Q59304; Q59305; Q59313; Q60121;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Phospholipase C;
DE Short=PLC;
DE EC=3.1.4.3;
DE AltName: Full=Alpha-toxin;
DE AltName: Full=Hemolysin;
DE AltName: Full=Lecithinase;
DE AltName: Full=Phosphatidylcholine cholinephosphohydrolase;
DE Flags: Precursor;
GN Name=plc; Synonyms=cpa; OrderedLocusNames=CPE0036;
OS Clostridium perfringens (strain 13 / Type A).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=195102;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RC STRAIN=8-6 / Type A;
RX PubMed=2560137; DOI=10.1007/bf00259619;
RA Saint-Joanis B., Garnier T., Cole S.T.;
RT "Gene cloning shows the alpha-toxin of Clostridium perfringens to contain
RT both sphingomyelinase and lecithinase activities.";
RL Mol. Gen. Genet. 219:453-460(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 3628 / NCIMB 10662 / Type C;
RX PubMed=8423073; DOI=10.1128/iai.61.2.457-463.1993;
RA Katayama S., Matsushita O., Minami J., Mizobuchi S., Okabe A.;
RT "Comparison of the alpha-toxin genes of Clostridium perfringens type A and
RT C strains: evidence for extragenic regulation of transcription.";
RL Infect. Immun. 61:457-463(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=13 / Type A, ATCC 10543 / DSM 798 / NCIB 8875 / BP6K / Type A,
RC ATCC 27324 / NCIMB 10748 / NCTC 13111 / Type E,
RC ATCC 3626 / NCIMB 10691 / Type B, KZ211 / Type A, L9 / Type D, and
RC NCIMB 10663 / NCTC 13109 / Type D;
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND USE AS A VACCINE.
RC STRAIN=13 / Type A, CER 89L1105 / Type A, CER 89L1216 / Type A, and
RC CER 89L43 / Type A;
RX PubMed=8581165; DOI=10.1099/13500872-142-1-191;
RA Ginter A., Williamson E.D., Dessy F., Coppe P., Bullifent H., Howells A.M.,
RA Titball R.W.;
RT "Molecular variation between the alpha-toxins from the type strain (NCTC
RT 8237) and clinical isolates of Clostridium perfringens associated with
RT disease in man and animals.";
RL Microbiology 142:191-198(1996).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=KZ1340 / Type A;
RX PubMed=8709860; DOI=10.1111/j.1348-0421.1996.tb03344.x;
RA Kameyama K., Matsushita O., Katayama S., Minami J., Maeda M., Nakamura S.,
RA Okabe A.;
RT "Analysis of the phospholipase C gene of Clostridium perfringens KZ1340
RT isolated from Antarctic soil.";
RL Microbiol. Immunol. 40:255-263(1996).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=13 / Type A;
RX PubMed=11792842; DOI=10.1073/pnas.022493799;
RA Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T.,
RA Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
RT "Complete genome sequence of Clostridium perfringens, an anaerobic flesh-
RT eater.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002).
RN [7]
RP MUTAGENESIS OF TRP-29; HIS-39; ASP-84; HIS-94; PHE-97; HIS-154; ASP-158;
RP HIS-164; HIS-176 AND GLU-180.
RC STRAIN=8-6 / Type A;
RX PubMed=8698464; DOI=10.1128/iai.64.7.2440-2444.1996;
RA Guillouard I., Garnier T., Cole S.T.;
RT "Use of site-directed mutagenesis to probe structure-function relationships
RT of alpha-toxin from Clostridium perfringens.";
RL Infect. Immun. 64:2440-2444(1996).
RN [8]
RP MUTAGENESIS OF ASP-297; THR-300; TYR-303 AND ASP-364, AND OTHER CONSERVED
RP ASPARTATE AND TYROSINE RESIDUES.
RC STRAIN=8-6 / Type A;
RX PubMed=9426125; DOI=10.1046/j.1365-2958.1997.6161993.x;
RA Guillouard I., Alzari P.M., Saliou B., Cole S.T.;
RT "The carboxy-terminal C2-like domain of the alpha-toxin from Clostridium
RT perfringens mediates calcium-dependent membrane recognition.";
RL Mol. Microbiol. 26:867-876(1997).
RN [9]
RP IDENTIFICATION OF ALPHA-TOXIN AS AN ENZYME.
RX PubMed=16747456; DOI=10.1042/bj0350884;
RA Macfarlane M.G., Knight B.C.J.G.;
RT "The biochemistry of bacterial toxins. I. The lecithinase activity of
RT Cl.welchii toxins.";
RL Biochem. J. 35:884-902(1941).
RN [10]
RP IMPORTANCE IN VIRULENCE OF GAS GANGRENE.
RC STRAIN=13 / Type A;
RX PubMed=10456947; DOI=10.1128/iai.67.9.4902-4907.1999;
RA Ellemor D.M., Baird R.N., Awad M.M., Boyd R.L., Rood J.I., Emmins J.J.;
RT "Use of genetically manipulated strains of Clostridium perfringens reveals
RT that both alpha-toxin and theta-toxin are required for vascular leukostasis
RT to occur in experimental gas gangrene.";
RL Infect. Immun. 67:4902-4907(1999).
RN [11]
RP EFFECT ON LEUKOCYTE AGGREGATION AND THROMBOSIS.
RC STRAIN=JIR325;
RX PubMed=9207366; DOI=10.1086/514022;
RA Stevens D.L., Tweten R.K., Awad M.M., Rood J.I., Bryant A.E.;
RT "Clostridial gas gangrene: evidence that alpha and theta toxins
RT differentially modulate the immune response and induce acute tissue
RT necrosis.";
RL J. Infect. Dis. 176:189-195(1997).
RN [12]
RP REVIEW.
RX PubMed=16887662; DOI=10.1006/anae.1999.0191;
RA Titball R.W., Naylor C.E., Basak A.K.;
RT "The Clostridium perfringens alpha-toxin.";
RL Anaerobe 5:51-64(1999).
RN [13]
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).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 29-398 OF THE OPEN FORM, AND
RP DISCUSSION OF CATALYSIS.
RC STRAIN=CER 89L43 / Type A;
RX PubMed=9699639; DOI=10.1038/1447;
RA Naylor C.E., Eaton J.T., Howells A.M., Justin N., Moss D.S., Titball R.W.,
RA Basak A.K.;
RT "Structure of the key toxin in gas gangrene.";
RL Nat. Struct. Biol. 5:738-746(1998).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 29-398 OF THE CLOSED FORM.
RC STRAIN=CER 89L43 / Type A;
RX PubMed=12051905; DOI=10.1016/s0022-2836(02)00290-5;
RA Eaton J.T., Naylor C.E., Howells A.M., Moss D.S., Titball R.W., Basak A.K.;
RT "Crystal structure of the C. perfringens alpha-toxin with the active site
RT closed by a flexible loop region.";
RL J. Mol. Biol. 319:275-281(2002).
CC -!- FUNCTION: Bacterial hemolysins are exotoxins that attack blood cell
CC membranes and cause cell rupture. Constitutes an essential virulence
CC factor in gas gangrene. Binds to eukaryotic membranes where it
CC hydrolyzes both phosphatidylcholine and sphingomyelin. The
CC diacylglycerol produced can activate both the arachidonic acid pathway,
CC leading to modulation of the inflammatory response cascade and
CC thrombosis, and protein kinase C, leading to activation of eukaryotic
CC phospholipases and further membrane damage. Acts on human and mouse
CC erythrocytes, but not on rabbit or horse erythrocytes.
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:0000305};
CC Note=Binds 3 Ca(2+) ions per subunit. {ECO:0000305};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Note=Binds 3 Zn(2+) ions per subunit.;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
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 -!- BIOTECHNOLOGY: Vaccination of mice with a fragment (residues 275-398)
CC protects them against a subsequent challenge with purified alpha-toxin.
CC -!- MISCELLANEOUS: Variations seen in PLC activity between different
CC strains seem to be due to transcriptional regulation.
CC -!- MISCELLANEOUS: Mutating residues 303 or 359 of the C.perfringens toxin
CC to match those found in C.bifermentans (301 and 358 respectively)
CC reduces toxicity considerably.
CC -!- SIMILARITY: Belongs to the bacterial zinc-metallophospholipase C
CC family. {ECO:0000255|PROSITE-ProRule:PRU00678}.
CC -!- WEB RESOURCE: Name=Worthington enzyme manual;
CC URL="https://www.worthington-biochem.com/PLC/";
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DR EMBL; X17300; CAA35186.1; -; Genomic_DNA.
DR EMBL; D10248; BAA01093.1; -; Genomic_DNA.
DR EMBL; D32123; BAA06849.1; -; Genomic_DNA.
DR EMBL; D32124; BAA06850.1; -; Genomic_DNA.
DR EMBL; D32126; BAA06852.1; -; Genomic_DNA.
DR EMBL; D32127; BAA06853.1; -; Genomic_DNA.
DR EMBL; D32128; BAA06854.1; -; Genomic_DNA.
DR EMBL; D49968; BAA08720.1; -; Genomic_DNA.
DR EMBL; D49969; BAA08721.1; -; Genomic_DNA.
DR EMBL; L43545; AAA99192.1; -; Genomic_DNA.
DR EMBL; L43546; AAA99193.1; -; Genomic_DNA.
DR EMBL; L43547; AAA99194.1; -; Genomic_DNA.
DR EMBL; L43548; AAA99195.1; -; Genomic_DNA.
DR EMBL; D63911; BAA09944.1; -; Genomic_DNA.
DR EMBL; BA000016; BAB79742.1; -; Genomic_DNA.
DR PIR; B49231; B49231.
DR PIR; JQ0366; JQ0366.
DR RefSeq; WP_011009584.1; NC_003366.1.
DR PDB; 1CA1; X-ray; 1.90 A; A=29-398.
DR PDB; 1GYG; X-ray; 1.90 A; A/B=29-398.
DR PDB; 1QM6; X-ray; 2.50 A; A/B=29-398.
DR PDB; 1QMD; X-ray; 2.20 A; A/B=29-398.
DR PDBsum; 1CA1; -.
DR PDBsum; 1GYG; -.
DR PDBsum; 1QM6; -.
DR PDBsum; 1QMD; -.
DR AlphaFoldDB; P0C216; -.
DR SMR; P0C216; -.
DR STRING; 195102.gene:10489266; -.
DR EnsemblBacteria; BAB79742; BAB79742; BAB79742.
DR KEGG; cpe:CPE0036; -.
DR HOGENOM; CLU_690198_0_0_9; -.
DR OMA; DHFWDPD; -.
DR EvolutionaryTrace; P0C216; -.
DR Proteomes; UP000000818; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0050429; F:calcium-dependent phospholipase C activity; IDA:CACAO.
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 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 3D-structure; Calcium; Cytolysis; Hemolysis; Hydrolase; Metal-binding;
KW Reference proteome; Secreted; Signal; Toxin; Virulence; Zinc.
FT SIGNAL 1..28
FT /evidence="ECO:0000250"
FT CHAIN 29..398
FT /note="Phospholipase C"
FT /id="PRO_0000023931"
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 BINDING 39
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT BINDING 84
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT BINDING 96
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT BINDING 154
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT BINDING 158
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT BINDING 158
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT BINDING 164
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 176
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 180
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 297
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
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:0000305"
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:0000305"
FT BINDING 365
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT VARIANT 2
FT /note="K -> E (in strain: CER 89L1216)"
FT VARIANT 10
FT /note="I -> V (in strain: 8-6)"
FT VARIANT 13..15
FT /note="TLA -> ALR (in strain: CER 89L1105 and CER 89L1216)"
FT VARIANT 13
FT /note="T -> A (in strain: 8-6, KZ211, L9, NCIB 10691, BP6K
FT and KZ1340)"
FT VARIANT 15
FT /note="A -> V (in strain: 8-6)"
FT VARIANT 22
FT /note="A -> T (in strain: L9 and BP6K)"
FT VARIANT 22
FT /note="A -> V (in strain: 8-6)"
FT VARIANT 43
FT /note="V -> A (in strain: NCIB 10691)"
FT VARIANT 47
FT /note="V -> I (in strain: L9 and KZ1340)"
FT VARIANT 54
FT /note="L -> M (in strain: 8-6)"
FT VARIANT 71
FT /note="E -> D (in strain: 8-6)"
FT VARIANT 91
FT /note="D -> N (in strain: KZ1340)"
FT VARIANT 103
FT /note="D -> N (in strain: 8-6)"
FT VARIANT 176
FT /note="H -> Y (in strain: KZ1340; probably inactive)"
FT VARIANT 195
FT /note="A -> V (in strain: 8-6, NCIB 10663 and NCIB 10748)"
FT VARIANT 202
FT /note="D -> A (in strain: NCIB 10691 and CER 89L1105)"
FT VARIANT 205
FT /note="A -> T (in strain: NCIB 10691 and CER 89L1105)"
FT VARIANT 281
FT /note="K -> N (in strain: 8-6)"
FT VARIANT 329
FT /note="T -> A (in strain: 8-6)"
FT VARIANT 363
FT /note="P -> S (in strain: NCIB 10691 and CER 89L1105)"
FT VARIANT 373
FT /note="I -> L (in strain: PB6K)"
FT VARIANT 373
FT /note="I -> V (in strain: 8-6, NCIB 10662, L9, NCIB 10663,
FT NCIB 10748, CER 89L43 and KZ1340)"
FT MUTAGEN 29
FT /note="W->S: Loss of all enzyme activities."
FT /evidence="ECO:0000269|PubMed:8698464"
FT MUTAGEN 39
FT /note="H->G,L: No enzyme accumulates."
FT /evidence="ECO:0000269|PubMed:8698464"
FT MUTAGEN 39
FT /note="H->S: Loss of all enzyme activities."
FT /evidence="ECO:0000269|PubMed:8698464"
FT MUTAGEN 84
FT /note="D->N: Loss of all enzyme activities."
FT /evidence="ECO:0000269|PubMed:8698464"
FT MUTAGEN 96
FT /note="H->G,S: Loss of all enzyme activities."
FT /evidence="ECO:0000269|PubMed:8698464"
FT MUTAGEN 97
FT /note="F->C: Loss of all enzyme activities."
FT /evidence="ECO:0000269|PubMed:8698464"
FT MUTAGEN 154
FT /note="H->G,S: Loss of all enzyme activities."
FT /evidence="ECO:0000269|PubMed:8698464"
FT MUTAGEN 158
FT /note="D->N: Loss of all enzyme activities."
FT /evidence="ECO:0000269|PubMed:8698464"
FT MUTAGEN 164
FT /note="H->A,G,S: Loss of all enzyme activities."
FT /evidence="ECO:0000269|PubMed:8698464"
FT MUTAGEN 176
FT /note="H->G,L,S: Loss of all enzyme activities."
FT /evidence="ECO:0000269|PubMed:8698464"
FT MUTAGEN 180
FT /note="E->Q: Loss of all enzyme activities."
FT /evidence="ECO:0000269|PubMed:8698464"
FT MUTAGEN 297
FT /note="D->N: Increased dependence of PLC on Ca(2+).
FT Dramatically decreases hemolytic, cytotoxic and myotoxic
FT activities."
FT /evidence="ECO:0000269|PubMed:9426125"
FT MUTAGEN 300
FT /note="T->P: Significant loss of activities; protein
FT conformation has changed."
FT /evidence="ECO:0000269|PubMed:9426125"
FT MUTAGEN 303
FT /note="Y->F,N: Increased dependence of PLC on Ca(2+).
FT Dramatically decreases hemolytic, cytotoxic and myotoxic
FT activities."
FT /evidence="ECO:0000269|PubMed:9426125"
FT MUTAGEN 364
FT /note="D->N: Increased dependence of PLC on Ca(2+).
FT Dramatically decreases hemolytic, cytotoxic and myotoxic
FT activities."
FT /evidence="ECO:0000269|PubMed:9426125"
FT TURN 33..35
FT /evidence="ECO:0007829|PDB:1CA1"
FT HELIX 38..53
FT /evidence="ECO:0007829|PDB:1CA1"
FT HELIX 60..71
FT /evidence="ECO:0007829|PDB:1CA1"
FT HELIX 73..81
FT /evidence="ECO:0007829|PDB:1CA1"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:1CA1"
FT HELIX 94..96
FT /evidence="ECO:0007829|PDB:1CA1"
FT TURN 100..102
FT /evidence="ECO:0007829|PDB:1CA1"
FT TURN 106..108
FT /evidence="ECO:0007829|PDB:1CA1"
FT HELIX 122..138
FT /evidence="ECO:0007829|PDB:1CA1"
FT HELIX 142..159
FT /evidence="ECO:0007829|PDB:1CA1"
FT TURN 163..167
FT /evidence="ECO:0007829|PDB:1CA1"
FT TURN 170..172
FT /evidence="ECO:0007829|PDB:1CA1"
FT HELIX 175..186
FT /evidence="ECO:0007829|PDB:1CA1"
FT HELIX 187..190
FT /evidence="ECO:0007829|PDB:1CA1"
FT HELIX 202..209
FT /evidence="ECO:0007829|PDB:1CA1"
FT HELIX 213..234
FT /evidence="ECO:0007829|PDB:1CA1"
FT HELIX 242..273
FT /evidence="ECO:0007829|PDB:1CA1"
FT TURN 277..280
FT /evidence="ECO:0007829|PDB:1CA1"
FT STRAND 285..292
FT /evidence="ECO:0007829|PDB:1CA1"
FT STRAND 302..310
FT /evidence="ECO:0007829|PDB:1CA1"
FT STRAND 315..319
FT /evidence="ECO:0007829|PDB:1CA1"
FT STRAND 323..325
FT /evidence="ECO:0007829|PDB:1CA1"
FT STRAND 332..338
FT /evidence="ECO:0007829|PDB:1CA1"
FT HELIX 346..348
FT /evidence="ECO:0007829|PDB:1CA1"
FT STRAND 349..357
FT /evidence="ECO:0007829|PDB:1CA1"
FT STRAND 359..362
FT /evidence="ECO:0007829|PDB:1CA1"
FT STRAND 368..375
FT /evidence="ECO:0007829|PDB:1CA1"
FT STRAND 378..384
FT /evidence="ECO:0007829|PDB:1CA1"
FT STRAND 394..396
FT /evidence="ECO:0007829|PDB:1CA1"
SQ SEQUENCE 398 AA; 45530 MW; 2E9E4A61181028CA CRC64;
MKRKICKALI CATLATSLWA GASTKVYAWD GKIDGTGTHA MIVTQGVSIL ENDLSKNEPE
SVRKNLEILK ENMHELQLGS TYPDYDKNAY DLYQDHFWDP DTDNNFSKDN SWYLAYSIPD
TGESQIRKFS ALARYEWQRG NYKQATFYLG EAMHYFGDID TPYHPANVTA VDSAGHVKFE
TFAEERKEQY KINTAGCKTN EDFYADILKN KDFNAWSKEY ARGFAKTGKS IYYSHASMSH
SWDDWDYAAK VTLANSQKGT AGYIYRFLHD VSEGNDPSVG KNVKELVAYI STSGEKDAGT
DDYMYFGIKT KDGKTQEWEM DNPGNDFMTG SKDTYTFKLK DENLKIDDIQ NMWIRKRKYT
AFPDAYKPEN IKIIANGKVV VDKDINEWIS GNSTYNIK
