ID E5AWQ0_CLOPF Unreviewed; 340 AA.
AC E5AWQ0;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 03-MAY-2023, entry version 37.
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};
DE Flags: Fragment;
GN Name=plc {ECO:0000313|EMBL:CBX19404.1};
OS Clostridium perfringens.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1502 {ECO:0000313|EMBL:CBX19404.1};
RN [1] {ECO:0000313|EMBL:CBX19404.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=AG03-4 {ECO:0000313|EMBL:CBX19404.1};
RA Alam S.I.;
RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CBX19404.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=AG03-4 {ECO:0000313|EMBL:CBX19404.1};
RA Sengupta N.;
RT "Genetic and proteomic characterization of Clostridium perfringens
RT environmental strains.";
RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
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};
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DR EMBL; FR687997; CBX19404.1; -; Genomic_DNA.
DR AlphaFoldDB; E5AWQ0; -.
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; 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};
KW Toxin {ECO:0000256|ARBA:ARBA00022656};
KW Virulence {ECO:0000256|ARBA:ARBA00023026};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 1..234
FT /note="Zn-dependent PLC"
FT /evidence="ECO:0000259|PROSITE:PS51346"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:CBX19404.1"
FT NON_TER 340
FT /evidence="ECO:0000313|EMBL:CBX19404.1"
SQ SEQUENCE 340 AA; 39229 MW; B0FBB72962B3923D CRC64;
QGVSILENDL SKNEPESVRK NLEILKENMH ELQLGSTYPD YDKNAYDLYQ DHFWDPDTDN
NFSKDNSWYL AYSIPDTGES QIRKFSALAR YEWQRGNYKQ ATFYLGEAMH YFGDIDTPYH
PANVTAVDSA GHVKFETFAE ERKEQYKINT AGCKTNEDFY ADILKNKDFN AWSKEYARGF
AKTGKSIYYS HASMSHSWDD WDYAAKVTLA NSQKGTAGYI YRFLHDVSEG NDPSVGKNVK
ELVAYISTSG EKDAGTDDYM YFGIKTKDGK TQEWEMDNPG NDFMTGSKDT YTFKLKDENL
KIDDIQNMWI RKRKYTAFPD AYKPENIKVI ANGKVVVDKD
//
