ID A0A1J0GKK7_9CLOT Unreviewed; 233 AA.
AC A0A1J0GKK7;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
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=A7L45_15730 {ECO:0000313|EMBL:APC41422.1};
OS Clostridium estertheticum subsp. estertheticum.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1552 {ECO:0000313|EMBL:APC41422.1, ECO:0000313|Proteomes:UP000182569};
RN [1] {ECO:0000313|Proteomes:UP000182569}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 8809 {ECO:0000313|Proteomes:UP000182569};
RX PubMed=27891116;
RA Yu Z., Gunn L., Brennan E., Reid R., Wall P.G., Gaora O.P., Hurley D.,
RA Bolton D., Fanning S.;
RT "Complete Genome Sequence of Clostridium estertheticum DSM 8809, a Microbe
RT Identified in Spoiled Vacuum Packed Beef.";
RL Front. Microbiol. 7:1764-1764(2016).
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 ---------------------------------------------------------------------------
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; CP015756; APC41422.1; -; Genomic_DNA.
DR RefSeq; WP_071613716.1; NZ_CP015756.1.
DR AlphaFoldDB; A0A1J0GKK7; -.
DR STRING; 1552.A7L45_15730; -.
DR KEGG; ceu:A7L45_15730; -.
DR OrthoDB; 1677163at2; -.
DR Proteomes; UP000182569; Chromosome.
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:UP000182569};
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; 27361 MW; 4894BE371CD1B4CB CRC64;
MKKKFEATYG KTLKGLMVTI NPIKKRIMKT HCIVHKFINI QAIEILKNKG YREVHTFYKS
YVKELNNGVT WADQDFKSSN HFYHHITGTG LYGFSNALTE FNKYYKCALR FVEAGDIRQA
LFYFGAACHL IQDATVPQHV NNKLLKNHRN FELWIIGRLM SDYSFPIFNE IIKQDNIEDY
IKNNATFASD IYISHVHIKN KEERYRKVST LIVQRAQKTT AGLMINFYNE INK
//