ID Q1HXG6_CLOPF Unreviewed; 398 AA.
AC Q1HXG6;
DT 13-JUN-2006, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2006, sequence version 1.
DT 28-JUN-2023, entry version 61.
DE RecName: Full=Phospholipase C {ECO:0000256|ARBA:ARBA00018391};
DE EC=3.1.4.3 {ECO:0000256|ARBA:ARBA00012018};
DE AltName: Full=Phosphatidylcholine cholinephosphohydrolase {ECO:0000256|ARBA:ARBA00031285};
GN Name=plc {ECO:0000313|EMBL:ABA64095.1};
OS Clostridium perfringens.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1502 {ECO:0000313|EMBL:ABA64095.1};
RN [1] {ECO:0000313|EMBL:ABA64095.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NRRL B-23732 {ECO:0000313|EMBL:ABA64095.1};
RX PubMed=16489222; DOI=10.1534/genetics.105.054601;
RA Rooney A.P., Swezey J.L., Friedman R., Hecht D.W., Maddox C.W.;
RT "Analysis of core housekeeping and virulence genes reveals cryptic lineages
RT of Clostridium perfringens that are associated with distinct disease
RT presentations.";
RL Genetics 172:2081-2092(2006).
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 Evidence={ECO:0000256|ARBA:ARBA00000291};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00152}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DQ184102; ABA64095.1; -; Genomic_DNA.
DR AlphaFoldDB; Q1HXG6; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
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:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR CDD; cd00113; PLAT; 1.
DR CDD; cd10981; ZnPC_S1P1; 1.
DR Gene3D; 1.10.575.10; P1 Nuclease; 1.
DR Gene3D; 2.60.60.20; PLAT/LH2 domain; 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; SSF49723; Lipase/lipooxygenase domain (PLAT/LH2 domain); 1.
DR SUPFAM; SSF48537; Phospholipase C/P1 nuclease; 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 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Cytolysis {ECO:0000256|ARBA:ARBA00022852};
KW Hemolysis {ECO:0000256|ARBA:ARBA00022735};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Toxin {ECO:0000256|ARBA:ARBA00022656};
KW Virulence {ECO:0000256|ARBA:ARBA00023026};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..398
FT /note="Phospholipase C"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038695937"
FT DOMAIN 26..278
FT /note="Zn-dependent PLC"
FT /evidence="ECO:0000259|PROSITE:PS51346"
FT DOMAIN 284..398
FT /note="PLAT"
FT /evidence="ECO:0000259|PROSITE:PS50095"
SQ SEQUENCE 398 AA; 45504 MW; 4C809C7EFF888306 CRC64;
MKRKICKALI CATLATSLWA GASTKVYAWD GKIDGTGTHA MIVTQGISIL ENDLSKNEPE
SVRKNLEILK ENMHELQLGS TYPDYDKNAY DLYQDHFWDP DTDNNFSKDN SWYLAYSIPD
TGESQIRKFS ALARYEWQRG NYKQATFYLG EAMHYFGDID TPYHPANVTA VDSAGHVKFE
TFAEERKEQY KINTAGCKTN EDFYADILRN KDFNAWSKEY AKGFAKTGKS IYYSHASMSH
SWDDWDYAAK VTLANSQKGT AGYIYRFLHD VSEGNDPSVG KNVKELVAYI STSGEKDAGT
DDYMYFGIKT KDGKTQEWEM DNPGNDFMTG SKDTYTFKLK DENLKIDDIQ NMWIRKRKYT
AFPDAYKAEN IKVIANGKVV VDKDINEWIS GNSTYNIK
//
