PHLC_PARBF
ID PHLC_PARBF Reviewed; 398 AA.
AC P20419; Q8VUZ4; Q9S532;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Phospholipase C;
DE Short=PLC;
DE EC=3.1.4.3;
DE AltName: Full=Cbp;
DE AltName: Full=Phosphatidylcholine cholinephosphohydrolase;
DE Flags: Precursor;
GN Name=plc; Synonyms=cbp;
OS Paraclostridium bifermentans (Clostridium bifermentans).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Paraclostridium.
OX NCBI_TaxID=1490;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RC STRAIN=ATCC 638 / DSM 14991 / JCM 1386 / NCIMB 10716 / NCTC 13019;
RX PubMed=2536356; DOI=10.1128/iai.57.2.468-476.1989;
RA Tso J.Y., Siebel C.;
RT "Cloning and expression of the phospholipase C gene from Clostridium
RT perfringens and Clostridium bifermentans.";
RL Infect. Immun. 57:468-476(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CONSTRUCTION OF A HYBRID ENZYME.
RC STRAIN=ATCC 638 / DSM 14991 / JCM 1386 / NCIMB 10716 / NCTC 13019;
RX PubMed=10377104; DOI=10.1128/iai.67.7.3297-3301.1999;
RA Jepson M., Howells A.M., Bullifent H.L., Bolgiano B., Crane D.T.,
RA Miller J., Holley J., Jayasekera P., Titball R.W.;
RT "Differences in the carboxy-terminal (putative phospholipid binding)
RT domains of Clostridium perfringens and Clostridium bifermentans
RT phospholipases C influence the hemolytic and lethal properties of these
RT enzymes.";
RL Infect. Immun. 67:3297-3301(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=KZ 1012;
RX PubMed=12540540; DOI=10.1128/iai.71.2.641-646.2003;
RA Karasawa T., Wang X., Maegawa T., Michiwa Y., Kita H., Miwa K.,
RA Nakamura S.;
RT "Clostridium sordellii phospholipase C: gene cloning and comparison of
RT enzymatic and biological activities with those of Clostridium perfringens
RT and Clostridium bifermentans phospholipase C.";
RL Infect. Immun. 71:641-646(2003).
RN [4]
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. This enzyme has 10-fold less
CC activity towards sphingomyelin than its C.perfringens counterpart, is
CC approximately 100-fold less hemolytic against mouse erythrocytes and at
CC least 100-fold less toxic in mice.
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 is conferred by this C-terminal domain (By
CC similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: A hybrid protein between the N-terminus of
CC C.bifermentans and the C-terminus of C.perfringens has an activity
CC intermediate between the two.
CC -!- SIMILARITY: Belongs to the bacterial zinc-metallophospholipase C
CC family. {ECO:0000255|PROSITE-ProRule:PRU00678}.
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DR EMBL; AF072123; AAD41623.1; -; Genomic_DNA.
DR EMBL; AB061869; BAB83265.1; -; Genomic_DNA.
DR PIR; B30565; B30565.
DR RefSeq; WP_021434260.1; NZ_NOLL01000007.1.
DR AlphaFoldDB; P20419; -.
DR SMR; P20419; -.
DR STRING; 1490.B2H97_13000; -.
DR PRIDE; P20419; -.
DR GeneID; 67474144; -.
DR eggNOG; ENOG5033QPJ; Bacteria.
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..26
FT /evidence="ECO:0000250"
FT CHAIN 27..398
FT /note="Phospholipase C"
FT /id="PRO_0000023933"
FT DOMAIN 27..276
FT /note="Zn-dependent PLC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00678"
FT DOMAIN 282..398
FT /note="PLAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT REGION 273..281
FT /note="Linker"
FT BINDING 27
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00678"
FT BINDING 37
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00678"
FT BINDING 82
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00678"
FT BINDING 94
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00678"
FT BINDING 152
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00678"
FT BINDING 156
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00678"
FT BINDING 156
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00678"
FT BINDING 162
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00678"
FT BINDING 174
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00678"
FT BINDING 178
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00678"
FT BINDING 297
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 298
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 299
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 319
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 320
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 323
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
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 324
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 363
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT CONFLICT 120..123
FT /note="SRNS -> AETQ (in Ref. 2 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 272..274
FT /note="GNT -> ENI (in Ref. 3; BAB83265)"
FT /evidence="ECO:0000305"
FT CONFLICT 280
FT /note="L -> S (in Ref. 3; BAB83265)"
FT /evidence="ECO:0000305"
FT CONFLICT 311
FT /note="G -> D (in Ref. 3; BAB83265)"
FT /evidence="ECO:0000305"
FT CONFLICT 357
FT /note="R -> K (in Ref. 3; BAB83265)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 398 AA; 45366 MW; 0B628AFE7146BC56 CRC64;
MKALKKVSNI LCVLGLCTLM GGTSYAWDGK KDGTGTHSLI AEHGLSMLNN DLSGNESQQV
KDNIKILNEY LGDLKLGSTY PDYDPNAYDL YQDHFYDPDT GNNFTIDNSW YASYPIYDTS
RNSVRKFATL AKNEWEKGNF KEATFLLGQG LHYLGDLNTP YHASNVTAVD SPGHVKYETF
VEERKDNYAL NTSGNDTTSG VYKEAMENPS FNKWMTQNSI KYAKIAKDLY YSHSTMSHSW
DDWDYSGREA IKNSQVCTAG FLYRFMNEVS NGNTGDNDSL TNEFNIVLKT ADNKYAGTDD
NVYFGFETNE GKKFEWKLDN AGNDFERNQV DNYILKTKDG EEVDINNISN YWIRKERLTS
ISDDWELSNF KLIANGKVIQ QQDVNKVFTG NETYYINK
