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Database: UniProt
Entry: A0A1I0WV33_9CLOT
LinkDB: A0A1I0WV33_9CLOT
Original site: A0A1I0WV33_9CLOT 
ID   A0A1I0WV33_9CLOT        Unreviewed;       240 AA.
AC   A0A1I0WV33;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
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   ORFNames=SAMN04488528_100683 {ECO:0000313|EMBL:SFA92511.1};
OS   Clostridium frigidicarnis.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=84698 {ECO:0000313|EMBL:SFA92511.1, ECO:0000313|Proteomes:UP000198619};
RN   [1] {ECO:0000313|EMBL:SFA92511.1, ECO:0000313|Proteomes:UP000198619}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12271 {ECO:0000313|EMBL:SFA92511.1,
RC   ECO:0000313|Proteomes:UP000198619};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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};
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DR   EMBL; FOKI01000006; SFA92511.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I0WV33; -.
DR   STRING; 84698.SAMN04488528_100683; -.
DR   OrthoDB; 1677163at2; -.
DR   Proteomes; UP000198619; Unassembled WGS sequence.
DR   GO; GO:0034480; F:phosphatidylcholine phospholipase C activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd11009; Zn_dep_PLPC; 1.
DR   Gene3D; 1.10.575.10; P1 Nuclease; 1.
DR   InterPro; IPR008947; PLipase_C/P1_nuclease_dom_sf.
DR   InterPro; IPR029002; PLPC/GPLD1.
DR   InterPro; IPR001531; Zn_PLipaseC.
DR   Pfam; PF00882; Zn_dep_PLPC; 1.
DR   SMART; SM00770; Zn_dep_PLPC; 1.
DR   SUPFAM; SSF48537; Phospholipase C/P1 nuclease; 1.
DR   PROSITE; PS51346; PROKAR_ZN_DEPEND_PLPC_2; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198619};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          22..239
FT                   /note="Zn-dependent PLC"
FT                   /evidence="ECO:0000259|PROSITE:PS51346"
SQ   SEQUENCE   240 AA;  28519 MW;  89C4B953DFC6553E CRC64;
     MKKTIEKTYG KAVTNVMKAV NPVKKKMLNT HCNVHKYINV EALNILNNEG YDKQYDFYRN
     YIDKLNQGAH WIDQDFKSTN HFYHITKERG LYGFSNALTE CIKYYNKSIE EYNEKNINES
     MFFLGACCHL IQDVTVPHHV DNRLLKKHRP FEIWIVKEIS QNSEKYSVHD GSKRYGNIDD
     YIKNNANTAR QIYYRYQDIE DEYKRYSKIS KEILGEAQKT TAGFLLDFYD EIINKKDNSK
//
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