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Phospholipase C (PLC) (EC 3.1.4.3) (Alpha-toxin) (Hemolysin) (Lecithinase) (Phosphatidylcholine cholinephosphohydrolase)

 PHLC1_CLOPE             Reviewed;         398 AA.
P0C216; P15310; P94658; Q46246; Q46279; Q46280; Q46281; Q46282;
Q57317; Q59303; Q59304; Q59305; Q59313; Q60121;
31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
31-OCT-2006, sequence version 1.
28-MAR-2018, entry version 79.
RecName: Full=Phospholipase C;
Short=PLC;
EC=3.1.4.3;
AltName: Full=Alpha-toxin;
AltName: Full=Hemolysin;
AltName: Full=Lecithinase;
AltName: Full=Phosphatidylcholine cholinephosphohydrolase;
Flags: Precursor;
Name=plc; Synonyms=cpa; OrderedLocusNames=CPE0036;
Clostridium perfringens (strain 13 / Type A).
Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
Clostridium.
NCBI_TaxID=195102;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
STRAIN=8-6 / Type A;
PubMed=2560137; DOI=10.1007/BF00259619;
Saint-Joanis B., Garnier T., Cole S.T.;
"Gene cloning shows the alpha-toxin of Clostridium perfringens to
contain both sphingomyelinase and lecithinase activities.";
Mol. Gen. Genet. 219:453-460(1989).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 3628 / NCIMB 10662 / Type C;
PubMed=8423073;
Katayama S., Matsushita O., Minami J., Mizobuchi S., Okabe A.;
"Comparison of the alpha-toxin genes of Clostridium perfringens type A
and C strains: evidence for extragenic regulation of transcription.";
Infect. Immun. 61:457-463(1993).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=13 / Type A, ATCC 10543 / DSM 798 / NCIB 8875 / BP6K / Type A,
ATCC 27324 / NCIMB 10748 / NCTC 13111 / Type E,
ATCC 3626 / NCIMB 10691 / Type B, KZ211 / Type A, L9 / Type D, and
NCIMB 10663 / NCTC 13109 / Type D;
PubMed=8522524; DOI=10.1128/jb.177.24.7164-7170.1995;
Tsutsui K., Minami J., Matsushita O., Katayama S., Taniguchi Y.,
Nakamura S., Nishioka M., Okabe A.;
"Phylogenetic analysis of phospholipase C genes from Clostridium
perfringens types A to E and Clostridium novyi.";
J. Bacteriol. 177:7164-7170(1995).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND USE AS A VACCINE.
STRAIN=13 / Type A, CER 89L1105 / Type A, CER 89L1216 / Type A, and
CER 89L43 / Type A;
PubMed=8581165; DOI=10.1099/13500872-142-1-191;
Ginter A., Williamson E.D., Dessy F., Coppe P., Bullifent H.,
Howells A.M., Titball R.W.;
"Molecular variation between the alpha-toxins from the type strain
(NCTC 8237) and clinical isolates of Clostridium perfringens
associated with disease in man and animals.";
Microbiology 142:191-198(1996).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=KZ1340 / Type A;
PubMed=8709860; DOI=10.1111/j.1348-0421.1996.tb03344.x;
Kameyama K., Matsushita O., Katayama S., Minami J., Maeda M.,
Nakamura S., Okabe A.;
"Analysis of the phospholipase C gene of Clostridium perfringens
KZ1340 isolated from Antarctic soil.";
Microbiol. Immunol. 40:255-263(1996).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=13 / Type A;
PubMed=11792842; DOI=10.1073/pnas.022493799;
Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A.,
Shiba T., Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
"Complete genome sequence of Clostridium perfringens, an anaerobic
flesh-eater.";
Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002).
[7]
MUTAGENESIS OF ZINC AND SUBSTRATE BINDING RESIDUES.
STRAIN=8-6 / Type A;
PubMed=8698464;
Guillouard I., Garnier T., Cole S.T.;
"Use of site-directed mutagenesis to probe structure-function
relationships of alpha-toxin from Clostridium perfringens.";
Infect. Immun. 64:2440-2444(1996).
[8]
MUTAGENESIS OF ASP-297; THR-300; TYR-303 AND ASP-364, AND OTHER
CONSERVED ASPARTATE AND TYROSINE RESIDUES.
STRAIN=8-6 / Type A;
PubMed=9426125; DOI=10.1046/j.1365-2958.1997.6161993.x;
Guillouard I., Alzari P.M., Saliou B., Cole S.T.;
"The carboxy-terminal C2-like domain of the alpha-toxin from
Clostridium perfringens mediates calcium-dependent membrane
recognition.";
Mol. Microbiol. 26:867-876(1997).
[9]
IDENTIFICATION OF ALPHA-TOXIN AS AN ENZYME.
PubMed=16747456; DOI=10.1042/bj0350884;
Macfarlane M.G., Knight B.C.J.G.;
"The biochemistry of bacterial toxins. I. The lecithinase activity of
Cl.welchii toxins.";
Biochem. J. 35:884-902(1941).
[10]
IMPORTANCE IN VIRULENCE OF GAS GANGRENE.
STRAIN=13 / Type A;
PubMed=10456947;
Ellemor D.M., Baird R.N., Awad M.M., Boyd R.L., Rood J.I.,
Emmins J.J.;
"Use of genetically manipulated strains of Clostridium perfringens
reveals that both alpha-toxin and theta-toxin are required for
vascular leukostasis to occur in experimental gas gangrene.";
Infect. Immun. 67:4902-4907(1999).
[11]
EFFECT ON LEUKOCYTE AGGREGATION AND THROMBOSIS.
STRAIN=JIR325;
PubMed=9207366; DOI=10.1086/514022;
Stevens D.L., Tweten R.K., Awad M.M., Rood J.I., Bryant A.E.;
"Clostridial gas gangrene: evidence that alpha and theta toxins
differentially modulate the immune response and induce acute tissue
necrosis.";
J. Infect. Dis. 176:189-195(1997).
[12]
REVIEW.
PubMed=16887662; DOI=10.1006/anae.1999.0191;
Titball R.W., Naylor C.E., Basak A.K.;
"The Clostridium perfringens alpha-toxin.";
Anaerobe 5:51-64(1999).
[13]
REVIEW.
PubMed=11008117; DOI=10.1016/S1286-4579(00)01281-8;
Jepson M., Titball R.W.;
"Structure and function of clostridial phospholipases C.";
Microbes Infect. 2:1277-1284(2000).
[14]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 29-398 OF THE OPEN FORM, AND
DISCUSSION OF CATALYSIS.
STRAIN=CER 89L43 / Type A;
PubMed=9699639; DOI=10.1038/1447;
Naylor C.E., Eaton J.T., Howells A.M., Justin N., Moss D.S.,
Titball R.W., Basak A.K.;
"Structure of the key toxin in gas gangrene.";
Nat. Struct. Biol. 5:738-746(1998).
[15]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 29-398 OF THE CLOSED FORM.
STRAIN=CER 89L43 / Type A;
PubMed=12051905; DOI=10.1016/S0022-2836(02)00290-5;
Eaton J.T., Naylor C.E., Howells A.M., Moss D.S., Titball R.W.,
Basak A.K.;
"Crystal structure of the C. perfringens alpha-toxin with the active
site closed by a flexible loop region.";
J. Mol. Biol. 319:275-281(2002).
-!- FUNCTION: Bacterial hemolysins are exotoxins that attack blood
cell membranes and cause cell rupture. Constitutes an essential
virulence factor in gas gangrene. Binds to eukaryotic membranes
where it hydrolyzes both phosphatidylcholine and sphingomyelin.
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. Acts on human and mouse erythrocytes, but not on rabbit or
horse erythrocytes.
-!- CATALYTIC ACTIVITY: A phosphatidylcholine + H(2)O = 1,2-diacyl-sn-
glycerol + phosphocholine.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000305};
Note=Binds 3 Ca(2+) ions per subunit. {ECO:0000305};
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Note=Binds 3 Zn(2+) ions per subunit.;
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
-!- DOMAIN: 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 Ca(2+) dependent manner and toxicity is
conferred by this C-terminal domain, which also contributes to the
sphingomyelinase activity.
-!- BIOTECHNOLOGY: Vaccination of mice with a fragment (residues 275-
398) protects them against a subsequent challenge with purified
alpha-toxin.
-!- MISCELLANEOUS: Variations seen in PLC activity between different
strains seem to be due to transcriptional regulation.
-!- MISCELLANEOUS: Mutating residues 303 or 359 of the C.perfringens
toxin to match those found in C.bifermentans (301 and 358
respectively) reduces toxicity considerably.
-!- SIMILARITY: Belongs to the bacterial zinc-metallophospholipase C
family. {ECO:0000255|PROSITE-ProRule:PRU00678}.
-!- WEB RESOURCE: Name=Worthington enzyme manual;
URL="http://www.worthington-biochem.com/PLC/";
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EMBL; X17300; CAA35186.1; -; Genomic_DNA.
EMBL; D10248; BAA01093.1; -; Genomic_DNA.
EMBL; D32123; BAA06849.1; -; Genomic_DNA.
EMBL; D32124; BAA06850.1; -; Genomic_DNA.
EMBL; D32126; BAA06852.1; -; Genomic_DNA.
EMBL; D32127; BAA06853.1; -; Genomic_DNA.
EMBL; D32128; BAA06854.1; -; Genomic_DNA.
EMBL; D49968; BAA08720.1; -; Genomic_DNA.
EMBL; D49969; BAA08721.1; -; Genomic_DNA.
EMBL; L43545; AAA99192.1; -; Genomic_DNA.
EMBL; L43546; AAA99193.1; -; Genomic_DNA.
EMBL; L43547; AAA99194.1; -; Genomic_DNA.
EMBL; L43548; AAA99195.1; -; Genomic_DNA.
EMBL; D63911; BAA09944.1; -; Genomic_DNA.
EMBL; BA000016; BAB79742.1; -; Genomic_DNA.
PIR; B49231; B49231.
PIR; JQ0366; JQ0366.
RefSeq; WP_011009584.1; NC_003366.1.
PDB; 1CA1; X-ray; 1.90 A; A=29-398.
PDB; 1GYG; X-ray; 1.90 A; A/B=29-398.
PDB; 1QM6; X-ray; 2.50 A; A/B=29-398.
PDB; 1QMD; X-ray; 2.20 A; A/B=29-398.
PDB; 1SB4; Model; -; A=29-398.
PDBsum; 1CA1; -.
PDBsum; 1GYG; -.
PDBsum; 1QM6; -.
PDBsum; 1QMD; -.
PDBsum; 1SB4; -.
ProteinModelPortal; P0C216; -.
SMR; P0C216; -.
EnsemblBacteria; BAB79742; BAB79742; BAB79742.
KEGG; cpe:CPE0036; -.
KO; K16619; -.
OMA; DHFWDPD; -.
OrthoDB; POG091H10JI; -.
EvolutionaryTrace; P0C216; -.
Proteomes; UP000000818; Chromosome.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0034480; F:phosphatidylcholine phospholipase C activity; IEA:UniProtKB-EC.
GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0044179; P:hemolysis in other organism; IEA:UniProtKB-KW.
Gene3D; 1.10.575.10; -; 1.
InterPro; IPR001024; PLAT/LH2_dom.
InterPro; IPR036392; PLAT/LH2_dom_sf.
InterPro; IPR008947; PLipase_C/P1_nuclease_dom_sf.
InterPro; IPR029002; PLPC/GPLD1.
InterPro; IPR001531; Zn_PLipaseC.
Pfam; PF01477; PLAT; 1.
Pfam; PF00882; Zn_dep_PLPC; 1.
PRINTS; PR00479; PRPHPHLPASEC.
ProDom; PD003946; PLipaseC_Zn-bd_prok; 1.
SMART; SM00770; Zn_dep_PLPC; 1.
SUPFAM; SSF48537; SSF48537; 1.
SUPFAM; SSF49723; SSF49723; 1.
PROSITE; PS50095; PLAT; 1.
PROSITE; PS00384; PROKAR_ZN_DEPEND_PLPC_1; 1.
PROSITE; PS51346; PROKAR_ZN_DEPEND_PLPC_2; 1.
1: Evidence at protein level;
3D-structure; Calcium; Complete proteome; Cytolysis; Hemolysis;
Hydrolase; Metal-binding; Reference proteome; Secreted; Signal; Toxin;
Virulence; Zinc.
SIGNAL 1 28 {ECO:0000250}.
CHAIN 29 398 Phospholipase C.
/FTId=PRO_0000023931.
DOMAIN 29 278 Zn-dependent PLC. {ECO:0000255|PROSITE-
ProRule:PRU00678}.
DOMAIN 284 398 PLAT. {ECO:0000255|PROSITE-
ProRule:PRU00152}.
REGION 275 283 Linker.
METAL 29 29 Zinc 1.
METAL 39 39 Zinc 1.
METAL 84 84 Zinc 3.
METAL 96 96 Zinc 3.
METAL 154 154 Zinc 3.
METAL 158 158 Zinc 1.
METAL 158 158 Zinc 3.
METAL 164 164 Zinc 2.
METAL 176 176 Zinc 2.
METAL 180 180 Zinc 2.
METAL 297 297 Calcium 1. {ECO:0000305}.
METAL 299 299 Calcium 1; via carbonyl oxygen.
{ECO:0000250}.
METAL 300 300 Calcium 3. {ECO:0000305}.
METAL 301 301 Calcium 3. {ECO:0000250}.
METAL 321 321 Calcium 2. {ECO:0000250}.
METAL 322 322 Calcium 2. {ECO:0000250}.
METAL 324 324 Calcium 2; via carbonyl oxygen.
{ECO:0000250}.
METAL 325 325 Calcium 3. {ECO:0000250}.
METAL 326 326 Calcium 2. {ECO:0000250}.
METAL 326 326 Calcium 3. {ECO:0000250}.
METAL 364 364 Calcium 1. {ECO:0000305}.
METAL 365 365 Calcium 1; via carbonyl oxygen.
{ECO:0000250}.
VARIANT 2 2 K -> E (in strain: CER 89L1216).
VARIANT 10 10 I -> V (in strain: 8-6).
VARIANT 13 15 TLA -> ALR (in strain: CER 89L1105 and
CER 89L1216).
VARIANT 13 13 T -> A (in strain: 8-6, KZ211, L9, NCIB
10691, BP6K and KZ1340).
VARIANT 15 15 A -> V (in strain: 8-6).
VARIANT 22 22 A -> T (in strain: L9 and BP6K).
VARIANT 22 22 A -> V (in strain: 8-6).
VARIANT 43 43 V -> A (in strain: NCIB 10691).
VARIANT 47 47 V -> I (in strain: L9 and KZ1340).
VARIANT 54 54 L -> M (in strain: 8-6).
VARIANT 71 71 E -> D (in strain: 8-6).
VARIANT 91 91 D -> N (in strain: KZ1340).
VARIANT 103 103 D -> N (in strain: 8-6).
VARIANT 176 176 H -> Y (in strain: KZ1340; probably
inactive).
VARIANT 195 195 A -> V (in strain: 8-6, NCIB 10663 and
NCIB 10748).
VARIANT 202 202 D -> A (in strain: NCIB 10691 and CER
89L1105).
VARIANT 205 205 A -> T (in strain: NCIB 10691 and CER
89L1105).
VARIANT 281 281 K -> N (in strain: 8-6).
VARIANT 329 329 T -> A (in strain: 8-6).
VARIANT 363 363 P -> S (in strain: NCIB 10691 and CER
89L1105).
VARIANT 373 373 I -> L (in strain: PB6K).
VARIANT 373 373 I -> V (in strain: 8-6, NCIB 10662, L9,
NCIB 10663, NCIB 10748, CER 89L43 and
KZ1340).
MUTAGEN 29 29 W->S: Loss of all enzyme activities.
{ECO:0000269|PubMed:8698464}.
MUTAGEN 39 39 H->G,L: No enzyme accumulates.
{ECO:0000269|PubMed:8698464}.
MUTAGEN 39 39 H->S: Loss of all enzyme activities.
{ECO:0000269|PubMed:8698464}.
MUTAGEN 84 84 D->N: Loss of all enzyme activities.
{ECO:0000269|PubMed:8698464}.
MUTAGEN 96 96 H->G,S: Loss of all enzyme activities.
{ECO:0000269|PubMed:8698464}.
MUTAGEN 97 97 F->C: Loss of all enzyme activities.
{ECO:0000269|PubMed:8698464}.
MUTAGEN 154 154 H->G,S: Loss of all enzyme activities.
{ECO:0000269|PubMed:8698464}.
MUTAGEN 158 158 D->N: Loss of all enzyme activities.
{ECO:0000269|PubMed:8698464}.
MUTAGEN 164 164 H->A,G,S: Loss of all enzyme activities.
{ECO:0000269|PubMed:8698464}.
MUTAGEN 176 176 H->G,L,S: Loss of all enzyme activities.
{ECO:0000269|PubMed:8698464}.
MUTAGEN 180 180 E->Q: Loss of all enzyme activities.
{ECO:0000269|PubMed:8698464}.
MUTAGEN 297 297 D->N: Increased dependence of PLC on
Ca(2+). Dramatically decreases hemolytic,
cytotoxic and myotoxic activities.
{ECO:0000269|PubMed:9426125}.
MUTAGEN 300 300 T->P: Significant loss of activities;
protein conformation has changed.
{ECO:0000269|PubMed:9426125}.
MUTAGEN 303 303 Y->F,N: Increased dependence of PLC on
Ca(2+). Dramatically decreases hemolytic,
cytotoxic and myotoxic activities.
{ECO:0000269|PubMed:9426125}.
MUTAGEN 364 364 D->N: Increased dependence of PLC on
Ca(2+). Dramatically decreases hemolytic,
cytotoxic and myotoxic activities.
{ECO:0000269|PubMed:9426125}.
TURN 33 35 {ECO:0000244|PDB:1CA1}.
HELIX 38 53 {ECO:0000244|PDB:1CA1}.
HELIX 60 71 {ECO:0000244|PDB:1CA1}.
HELIX 73 81 {ECO:0000244|PDB:1CA1}.
HELIX 82 84 {ECO:0000244|PDB:1CA1}.
HELIX 94 96 {ECO:0000244|PDB:1CA1}.
TURN 100 102 {ECO:0000244|PDB:1CA1}.
TURN 106 108 {ECO:0000244|PDB:1CA1}.
HELIX 122 138 {ECO:0000244|PDB:1CA1}.
HELIX 142 159 {ECO:0000244|PDB:1CA1}.
TURN 163 167 {ECO:0000244|PDB:1CA1}.
TURN 170 172 {ECO:0000244|PDB:1CA1}.
HELIX 175 186 {ECO:0000244|PDB:1CA1}.
HELIX 187 190 {ECO:0000244|PDB:1CA1}.
HELIX 202 209 {ECO:0000244|PDB:1CA1}.
HELIX 213 234 {ECO:0000244|PDB:1CA1}.
HELIX 242 273 {ECO:0000244|PDB:1CA1}.
TURN 277 280 {ECO:0000244|PDB:1CA1}.
STRAND 285 292 {ECO:0000244|PDB:1CA1}.
STRAND 302 310 {ECO:0000244|PDB:1CA1}.
STRAND 315 319 {ECO:0000244|PDB:1CA1}.
STRAND 323 325 {ECO:0000244|PDB:1CA1}.
STRAND 332 338 {ECO:0000244|PDB:1CA1}.
HELIX 346 348 {ECO:0000244|PDB:1CA1}.
STRAND 349 357 {ECO:0000244|PDB:1CA1}.
STRAND 359 362 {ECO:0000244|PDB:1CA1}.
STRAND 368 375 {ECO:0000244|PDB:1CA1}.
STRAND 378 384 {ECO:0000244|PDB:1CA1}.
STRAND 394 396 {ECO:0000244|PDB:1CA1}.
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


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E0576r ELISA kit Group IB phospholipase A2,Phosphatidylcholine 2-acylhydrolase 1B,Phospholipase A2,Pla2g1b,Rat,Rattus norvegicus 96T
EIAAB31487 Choline phosphatase 3,Phosphatidylcholine-hydrolyzing phospholipase D3,Phospholipase D3,PLD 3,Pld3,Rat,Rattus norvegicus
EIAAB31489 Bos taurus,Bovine,Choline phosphatase 3,Phosphatidylcholine-hydrolyzing phospholipase D3,Phospholipase D3,PLD 3,PLD3
10-663-45346 Secreted Phospholipase A2-V (sPLA2-V) Human - EC 3.1.1.4; Phosphatidylcholine 2-acylhydrolase; PLA2-10; Group V phospholipase A2 N_A 0.002 mg


 

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