GenomeNet

Database: UniProt
Entry: Q1HXP9_CLOPF
LinkDB: Q1HXP9_CLOPF
Original site: Q1HXP9_CLOPF 
ID   Q1HXP9_CLOPF            Unreviewed;       398 AA.
AC   Q1HXP9;
DT   13-JUN-2006, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2006, sequence version 1.
DT   28-JUN-2023, entry version 63.
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   Name=plc {ECO:0000313|EMBL:ABA64012.1};
OS   Clostridium perfringens.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1502 {ECO:0000313|EMBL:ABA64012.1};
RN   [1] {ECO:0000313|EMBL:ABA64012.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NRRL B-23819 {ECO:0000313|EMBL:ABA63941.1}, NRRL B-23821
RC   {ECO:0000313|EMBL:ABA63942.1}, NRRL B-23824
RC   {ECO:0000313|EMBL:ABA63944.1}, and NRRL B-23825
RC   {ECO:0000313|EMBL:ABA64012.1};
RX   PubMed=16489222; DOI=10.1534/genetics.105.054601;
RA   Rooney A.P., Swezey J.L., Friedman R., Hecht D.W., Maddox C.W.;
RT   "Analysis of core housekeeping and virulence genes reveals cryptic lineages
RT   of Clostridium perfringens that are associated with distinct disease
RT   presentations.";
RL   Genetics 172:2081-2092(2006).
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};
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; DQ183948; ABA63941.1; -; Genomic_DNA.
DR   EMBL; DQ183949; ABA63942.1; -; Genomic_DNA.
DR   EMBL; DQ183951; ABA63944.1; -; Genomic_DNA.
DR   EMBL; DQ184019; ABA64012.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q1HXP9; -.
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; PS50095; PLAT; 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, ECO:0000256|SAM:SignalP};
KW   Toxin {ECO:0000256|ARBA:ARBA00022656};
KW   Virulence {ECO:0000256|ARBA:ARBA00023026};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..398
FT                   /note="Phospholipase C"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5038288191"
FT   DOMAIN          26..278
FT                   /note="Zn-dependent PLC"
FT                   /evidence="ECO:0000259|PROSITE:PS51346"
FT   DOMAIN          284..398
FT                   /note="PLAT"
FT                   /evidence="ECO:0000259|PROSITE:PS50095"
SQ   SEQUENCE   398 AA;  45476 MW;  2E774A7469175972 CRC64;
     MKRKICKALI CAALATSLWA GASTKVYAWD GKIDGTGTHA MIVTQGVSIL ENDLSKNEPE
     SVRKNLEILK ENMHELQLGS TYPDYDKNAY DLYQDHFWDP DTDNNFSKDN SWYLAYSIPD
     TGESQIRKFS ALARYEWQRG NYKQATFYLG EAMHYFGDID TPYHPANVTA VDSAGHVKFE
     TFAEERKEQY KINTAGCKTN EDFYADILKN KDFNAWSKEY ARGFAKTGKS IYYSHASMSH
     SWDDWDYAAK VTLANSQKGT AGYIYRFLHD VSEGNDSSVG KNVKELVAYI STSGEKDAGT
     DDYMYFGIKT KDGKTQEWEM DNPGNDFMTG SKDTYTFKLK DENLKIDDIQ NMWIRKRKYT
     AFPDAYKPEN IKVIANGKVV VDKDINEWIS GNSTYNIK
//
DBGET integrated database retrieval system