PLC_LISMO
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 03-AUG-2022, entry version 144.
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; Firmicutes; 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.
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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.lmo0201; -.
DR DrugBank; DB03106; scyllo-inositol.
DR PaxDb; P34024; -.
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 OMA; LYVMHGV; -.
DR BioCyc; LMON169963:LMO0201-MON; -.
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 Gene3D; 3.20.20.190; -; 1.
DR InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR InterPro; IPR000909; PLipase_C_PInositol-sp_X_dom.
DR Pfam; PF00388; PI-PLC-X; 1.
DR SMART; SM00148; PLCXc; 1.
DR SUPFAM; SSF51695; SSF51695; 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
