ID   C0L3J2_CLOPF            Unreviewed;       212 AA.
AC   C0L3J2;
DT   05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   05-MAY-2009, sequence version 1.
DT   03-MAY-2023, entry version 41.
DE   SubName: Full=Phospholipase C {ECO:0000313|EMBL:ACN38385.1};
DE   Flags: Fragment;
GN   Name=plc {ECO:0000313|EMBL:ACN38385.1};
OS   Clostridium perfringens.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1502 {ECO:0000313|EMBL:ACN38385.1};
RN   [1] {ECO:0000313|EMBL:ACN38385.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ELA14 {ECO:0000313|EMBL:ACN38385.1};
RA   Karpowicz E., Novinscak A., Barlocher F., Filion M.;
RT   "qPCR quantification and genetic characterization of Clostridium
RT   perfringens populations in biosolids composted for 2 years.";
RL   J. Appl. Microbiol. 108:571-581(2010).
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; FJ655580; ACN38385.1; -; Genomic_DNA.
DR   AlphaFoldDB; C0L3J2; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0004629; F:phospholipase C activity; IEA:InterPro.
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   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; IPR001531; Zn_PLipaseC.
DR   Pfam; PF01477; PLAT; 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; 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   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Toxin {ECO:0000256|ARBA:ARBA00022656};
KW   Virulence {ECO:0000256|ARBA:ARBA00023026}.
FT   DOMAIN          1..122
FT                   /note="Zn-dependent PLC"
FT                   /evidence="ECO:0000259|PROSITE:PS51346"
FT   DOMAIN          128..212
FT                   /note="PLAT"
FT                   /evidence="ECO:0000259|PROSITE:PS50095"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ACN38385.1"
FT   NON_TER         212
FT                   /evidence="ECO:0000313|EMBL:ACN38385.1"
SQ   SEQUENCE   212 AA;  24233 MW;  2971ABCA44C0871D CRC64;
     GDIDTPYHPV NVTAVDSAGH VKFETFAEER KEQYKINTAG CKTNEDFYAD ILKNKDFNAW
     SKEYARGFAK TGKSIYYSHA SMSHSWDDWD YAAKVTLANS QKGTAGYIYR FLHDVSEGND
     PSVGKNVKEL VAYISTSGEK DAGTDDYMYF GIKTKDGKTQ EWEMDNPGND FMTGSKDTYT
     FKLKDENLKI DDIQNMWIRK RKYTAFPDAY KP
//