ID A0A151B529_9CLOT Unreviewed; 233 AA.
AC A0A151B529;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 19.
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=CLTEP_10080 {ECO:0000313|EMBL:KYH35015.1};
OS Clostridium tepidiprofundi DSM 19306.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1121338 {ECO:0000313|EMBL:KYH35015.1, ECO:0000313|Proteomes:UP000075531};
RN [1] {ECO:0000313|EMBL:KYH35015.1, ECO:0000313|Proteomes:UP000075531}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19306 {ECO:0000313|EMBL:KYH35015.1,
RC ECO:0000313|Proteomes:UP000075531};
RA Poehlein A., Daniel R.;
RT "Genome sequence of Clostridium tepidiprofundi DSM 19306.";
RL Submitted (FEB-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};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KYH35015.1}.
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DR EMBL; LTBA01000007; KYH35015.1; -; Genomic_DNA.
DR RefSeq; WP_066823477.1; NZ_LTBA01000007.1.
DR AlphaFoldDB; A0A151B529; -.
DR STRING; 1121338.CLTEP_10080; -.
DR PATRIC; fig|1121338.3.peg.1041; -.
DR OrthoDB; 1677163at2; -.
DR Proteomes; UP000075531; 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:UP000075531};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 22..233
FT /note="Zn-dependent PLC"
FT /evidence="ECO:0000259|PROSITE:PS51346"
SQ SEQUENCE 233 AA; 27568 MW; 21CBCA2A64504912 CRC64;
MIRKIEKTYG ITLKGALKII NPIKKRLIKT YCLVHKFLNR QALRILHKEN YLDEYKFYSK
YIIFLNEGAV WADQDFKSIN HFFHYNKRSG LFGFSNALSE CCDYYNKAVD YYNQNNIEKS
MFYIGAACHL VQDSTVPQHV NNKLLSEHRQ FELWIIDEVI NKNSFGELSN IVEYDDIKDY
IIINSRKAYN IYRKNSHITD KYNRYNSVAS EIIKLAQGST AGFLIKFYNE NVK
//
