ID   PLC_LISMO               Reviewed;         317 AA.
AC   P34024;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   27-MAR-2024, entry version 151.
DE   RecName: Full=1-phosphatidylinositol phosphodiesterase;
DE            EC=4.6.1.13;
DE   AltName: Full=Phosphatidylinositol diacylglycerol-lyase;
DE   AltName: Full=Phosphatidylinositol-specific phospholipase C;
DE            Short=PI-PLC;
DE   Flags: Precursor;
GN   Name=plcA; Synonyms=pic; OrderedLocusNames=lmo0201;
OS   Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=169963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=LO28 / Serovar 1/2c;
RX   PubMed=1645839; DOI=10.1111/j.1365-2958.1991.tb02118.x;
RA   Mengaud J., Braun-Breton C., Cossart P.;
RT   "Identification of phosphatidylinositol-specific phospholipase C activity
RT   in Listeria monocytogenes: a novel type of virulence factor?";
RL   Mol. Microbiol. 5:367-372(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=EGD / Serovar 1/2a;
RX   PubMed=1645838; DOI=10.1111/j.1365-2958.1991.tb02117.x;
RA   Leimeister-Waechter M., Domann E., Chakraborty T.;
RT   "Detection of a gene encoding a phosphatidylinositol-specific phospholipase
RT   C that is co-ordinately expressed with listeriolysin in Listeria
RT   monocytogenes.";
RL   Mol. Microbiol. 5:361-366(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-679 / EGD-e;
RX   PubMed=11679669; DOI=10.1126/science.1063447;
RA   Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA   Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA   Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA   Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA   Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA   Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA   Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA   Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA   Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA   Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT   "Comparative genomics of Listeria species.";
RL   Science 294:849-852(2001).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 70-317.
RX   PubMed=2509367; DOI=10.1128/iai.57.12.3695-3701.1989;
RA   Mengaud J., Vicente M.-F., Cossart P.;
RT   "Transcriptional mapping and nucleotide sequence of the Listeria
RT   monocytogenes hlyA region reveal structural features that may be involved
RT   in regulation.";
RL   Infect. Immun. 57:3695-3701(1989).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 43-317.
RC   STRAIN=EGD / Serovar 1/2a;
RX   PubMed=9367761; DOI=10.1006/jmbi.1997.1290;
RA   Moser J., Gerstel B., Meyer J.E., Chakraborty T., Wehland J., Heinz D.W.;
RT   "Crystal structure of the phosphatidylinositol-specific phospholipase C
RT   from the human pathogen Listeria monocytogenes.";
RL   J. Mol. Biol. 273:269-282(1997).
CC   -!- FUNCTION: Cleaves glycosylphosphatidylinositol (GPI) and
CC       phosphatidylinositol (PI) anchors but not PI phosphates. Important
CC       factor in pathogenesis, PI-PLC activity is present only in virulent
CC       listeria species. It may participate in the lysis of the phagolysosomal
CC       membrane.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) = 1D-myo-
CC         inositol 1,2-cyclic phosphate + a 1,2-diacyl-sn-glycerol;
CC         Xref=Rhea:RHEA:17093, ChEBI:CHEBI:17815, ChEBI:CHEBI:57880,
CC         ChEBI:CHEBI:58484; EC=4.6.1.13;
CC   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Secreted. Cytoplasm. Note=Secreted and, to a
CC       lesser extent, cytoplasmic.
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; X54618; CAA38438.1; -; Genomic_DNA.
DR   EMBL; AL591974; CAD00728.1; -; Genomic_DNA.
DR   PIR; AB1100; AB1100.
DR   PIR; S15336; A37204.
DR   RefSeq; NP_463732.1; NC_003210.1.
DR   RefSeq; WP_003733144.1; NZ_CP023861.1.
DR   PDB; 1AOD; X-ray; 2.60 A; A=29-317.
DR   PDB; 2PLC; X-ray; 2.00 A; A=43-316.
DR   PDBsum; 1AOD; -.
DR   PDBsum; 2PLC; -.
DR   AlphaFoldDB; P34024; -.
DR   SMR; P34024; -.
DR   STRING; 169963.gene:17592837; -.
DR   DrugBank; DB03106; scyllo-inositol.
DR   PaxDb; 169963-lmo0201; -.
DR   EnsemblBacteria; CAD00728; CAD00728; CAD00728.
DR   GeneID; 987032; -.
DR   KEGG; lmo:lmo0201; -.
DR   PATRIC; fig|169963.11.peg.206; -.
DR   eggNOG; COG0823; Bacteria.
DR   HOGENOM; CLU_024117_3_0_9; -.
DR   OrthoDB; 7191982at2; -.
DR   BioCyc; LMON169963:LMO0201-MONOMER; -.
DR   EvolutionaryTrace; P34024; -.
DR   Proteomes; UP000000817; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004436; F:phosphatidylinositol diacylglycerol-lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008081; F:phosphoric diester hydrolase activity; IBA:GO_Central.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd00137; PI-PLCc; 1.
DR   Gene3D; 3.20.20.190; Phosphatidylinositol (PI) phosphodiesterase; 1.
DR   InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR   InterPro; IPR000909; PLipase_C_PInositol-sp_X_dom.
DR   PANTHER; PTHR13593:SF148; SI:DKEY-152B24.6-RELATED; 1.
DR   PANTHER; PTHR13593; UNCHARACTERIZED; 1.
DR   Pfam; PF00388; PI-PLC-X; 1.
DR   SMART; SM00148; PLCXc; 1.
DR   SUPFAM; SSF51695; PLC-like phosphodiesterases; 1.
DR   PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Lipid degradation; Lipid metabolism; Lyase;
KW   Reference proteome; Secreted; Signal; Virulence.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..317
FT                   /note="1-phosphatidylinositol phosphodiesterase"
FT                   /id="PRO_0000024296"
FT   DOMAIN          58..196
FT                   /note="PI-PLC X-box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT   ACT_SITE        67
FT                   /note="Proton acceptor"
FT   ACT_SITE        115
FT                   /note="Proton donor"
FT   HELIX           45..47
FT                   /evidence="ECO:0007829|PDB:2PLC"
FT   HELIX           49..51
FT                   /evidence="ECO:0007829|PDB:2PLC"
FT   HELIX           58..60
FT                   /evidence="ECO:0007829|PDB:2PLC"
FT   STRAND          61..66
FT                   /evidence="ECO:0007829|PDB:2PLC"
FT   TURN            67..72
FT                   /evidence="ECO:0007829|PDB:2PLC"
FT   HELIX           76..80
FT                   /evidence="ECO:0007829|PDB:2PLC"
FT   HELIX           82..85
FT                   /evidence="ECO:0007829|PDB:2PLC"
FT   HELIX           92..97
FT                   /evidence="ECO:0007829|PDB:2PLC"
FT   STRAND          102..107
FT                   /evidence="ECO:0007829|PDB:2PLC"
FT   STRAND          111..115
FT                   /evidence="ECO:0007829|PDB:2PLC"
FT   STRAND          118..123
FT                   /evidence="ECO:0007829|PDB:2PLC"
FT   HELIX           124..137
FT                   /evidence="ECO:0007829|PDB:2PLC"
FT   STRAND          143..149
FT                   /evidence="ECO:0007829|PDB:2PLC"
FT   HELIX           156..167
FT                   /evidence="ECO:0007829|PDB:2PLC"
FT   HELIX           168..171
FT                   /evidence="ECO:0007829|PDB:2PLC"
FT   STRAND          174..178
FT                   /evidence="ECO:0007829|PDB:2PLC"
FT   TURN            187..192
FT                   /evidence="ECO:0007829|PDB:2PLC"
FT   STRAND          194..200
FT                   /evidence="ECO:0007829|PDB:2PLC"
FT   STRAND          206..208
FT                   /evidence="ECO:0007829|PDB:2PLC"
FT   STRAND          211..216
FT                   /evidence="ECO:0007829|PDB:2PLC"
FT   STRAND          222..225
FT                   /evidence="ECO:0007829|PDB:2PLC"
FT   HELIX           233..249
FT                   /evidence="ECO:0007829|PDB:2PLC"
FT   STRAND          251..258
FT                   /evidence="ECO:0007829|PDB:2PLC"
FT   STRAND          264..266
FT                   /evidence="ECO:0007829|PDB:2PLC"
FT   HELIX           268..288
FT                   /evidence="ECO:0007829|PDB:2PLC"
FT   STRAND          295..301
FT                   /evidence="ECO:0007829|PDB:2PLC"
FT   HELIX           304..311
FT                   /evidence="ECO:0007829|PDB:2PLC"
SQ   SEQUENCE   317 AA;  36318 MW;  5D0E33649A983DA2 CRC64;
     MYKNYLQRTL VLLLCFILYF FTFPLGGKAY SLNNWNKPIK NSVTTKQWMS ALPDTTNLAA
     LSIPGTHDTM SYNGDITWTL TKPLAQTQTM SLYQQLEAGI RYIDIRAKDN LNIYHGPIFL
     NASLSGVLET ITQFLKKNPK ETIIMRLKDE QNSNDSFDYR IQPLINIYKD YFYTTPRTDT
     SNKIPTLKDV RGKILLLSEN HTKKPLVINS RKFGMQFGAP NQVIQDDYNG PSVKTKFKEI
     VQTAYQASKA DNKLFLNHIS ATSLTFTPRQ YAAALNNKVE QFVLNLTSEK VRGLGILIMD
     FPEKQTIKNI IKNNKFN
//