PLC_BACCE
ID PLC_BACCE Reviewed; 329 AA.
AC P14262;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 110.
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;
OS Bacillus cereus.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1396;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2509427; DOI=10.1128/jb.171.11.6077-6083.1989;
RA Kuppe A., Evans L.M., McMillen D.A., Griffith O.H.;
RT "Phosphatidylinositol-specific phospholipase C of Bacillus cereus: cloning,
RT sequencing, and relationship to other phospholipases.";
RL J. Bacteriol. 171:6077-6083(1989).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
RX PubMed=7664726; DOI=10.1002/j.1460-2075.1995.tb00057.x;
RA Heinz D.W., Ryan M., Bullock T.L., Griffith O.H.;
RT "Crystal structure of the phosphatidylinositol-specific phospholipase C
RT from Bacillus cereus in complex with myo-inositol.";
RL EMBO J. 14:3855-3863(1995).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
RX PubMed=8755729; DOI=10.1021/bi9606105;
RA Heinz D.W., Ryan M., Smith M.P., Weaver L.H., Keana J.F., Griffith O.H.;
RT "Crystal structure of phosphatidylinositol-specific phospholipase C from
RT Bacillus cereus in complex with glucosaminyl(alpha 1-->6)-D-myo-inositol,
RT an essential fragment of GPI anchors.";
RL Biochemistry 35:9496-9504(1996).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=9335537; DOI=10.1021/bi971102d;
RA Gassler C.S., Ryan M., Liu T., Griffith O.H., Heinz D.W.;
RT "Probing the roles of active site residues in phosphatidylinositol-specific
RT phospholipase C from Bacillus cereus by site-directed mutagenesis.";
RL Biochemistry 36:12802-12813(1997).
CC -!- FUNCTION: Cleaves glycosylphosphatidylinositol (GPI) and
CC phosphatidylinositol (PI) anchors but not PI phosphates.
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 -!- SUBCELLULAR LOCATION: Secreted.
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DR EMBL; M30809; AAA22665.1; -; Genomic_DNA.
DR PIR; A33493; A33493.
DR PDB; 1GYM; X-ray; 2.20 A; A=32-329.
DR PDB; 1PTD; X-ray; 2.60 A; A=32-329.
DR PDB; 1PTG; X-ray; 2.60 A; A=32-329.
DR PDB; 2PTD; X-ray; 2.00 A; A=32-329.
DR PDB; 3PTD; X-ray; 2.20 A; A=32-329.
DR PDB; 4PTD; X-ray; 2.30 A; A=32-329.
DR PDB; 5PTD; X-ray; 2.70 A; A=32-329.
DR PDB; 6PTD; X-ray; 2.60 A; A=32-329.
DR PDB; 6S2A; X-ray; 2.70 A; A/B/C=33-329.
DR PDB; 7PTD; X-ray; 2.60 A; A=32-329.
DR PDBsum; 1GYM; -.
DR PDBsum; 1PTD; -.
DR PDBsum; 1PTG; -.
DR PDBsum; 2PTD; -.
DR PDBsum; 3PTD; -.
DR PDBsum; 4PTD; -.
DR PDBsum; 5PTD; -.
DR PDBsum; 6PTD; -.
DR PDBsum; 6S2A; -.
DR PDBsum; 7PTD; -.
DR AlphaFoldDB; P14262; -.
DR SMR; P14262; -.
DR STRING; 1396.DJ87_1179; -.
DR BindingDB; P14262; -.
DR ChEMBL; CHEMBL4739677; -.
DR DrugBank; DB03779; Glucosaminyl-(Alpha-6)-D-Myo-Inositol.
DR DrugBank; DB03106; scyllo-inositol.
DR eggNOG; COG0823; Bacteria.
DR BioCyc; MetaCyc:MON-15192; -.
DR EvolutionaryTrace; P14262; -.
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; IEA:InterPro.
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; Lipid degradation; Lipid metabolism; Lyase; Secreted; Signal.
FT SIGNAL 1..31
FT CHAIN 32..329
FT /note="1-phosphatidylinositol phosphodiesterase"
FT /id="PRO_0000024294"
FT DOMAIN 53..194
FT /note="PI-PLC X-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT ACT_SITE 63
FT /note="Proton acceptor"
FT ACT_SITE 113
FT /note="Proton donor"
FT HELIX 35..39
FT /evidence="ECO:0007829|PDB:2PTD"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:1PTD"
FT TURN 44..47
FT /evidence="ECO:0007829|PDB:2PTD"
FT TURN 54..56
FT /evidence="ECO:0007829|PDB:2PTD"
FT STRAND 59..62
FT /evidence="ECO:0007829|PDB:2PTD"
FT HELIX 65..67
FT /evidence="ECO:0007829|PDB:2PTD"
FT HELIX 73..79
FT /evidence="ECO:0007829|PDB:2PTD"
FT HELIX 86..90
FT /evidence="ECO:0007829|PDB:2PTD"
FT TURN 91..93
FT /evidence="ECO:0007829|PDB:2PTD"
FT STRAND 96..103
FT /evidence="ECO:0007829|PDB:2PTD"
FT STRAND 109..113
FT /evidence="ECO:0007829|PDB:2PTD"
FT STRAND 116..121
FT /evidence="ECO:0007829|PDB:2PTD"
FT HELIX 122..135
FT /evidence="ECO:0007829|PDB:2PTD"
FT STRAND 141..147
FT /evidence="ECO:0007829|PDB:2PTD"
FT HELIX 159..166
FT /evidence="ECO:0007829|PDB:2PTD"
FT TURN 167..169
FT /evidence="ECO:0007829|PDB:2PTD"
FT STRAND 170..173
FT /evidence="ECO:0007829|PDB:1PTD"
FT HELIX 182..185
FT /evidence="ECO:0007829|PDB:2PTD"
FT STRAND 188..194
FT /evidence="ECO:0007829|PDB:2PTD"
FT STRAND 211..218
FT /evidence="ECO:0007829|PDB:2PTD"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:2PTD"
FT STRAND 224..228
FT /evidence="ECO:0007829|PDB:2PTD"
FT HELIX 235..250
FT /evidence="ECO:0007829|PDB:2PTD"
FT TURN 251..254
FT /evidence="ECO:0007829|PDB:2PTD"
FT STRAND 258..263
FT /evidence="ECO:0007829|PDB:2PTD"
FT STRAND 271..275
FT /evidence="ECO:0007829|PDB:2PTD"
FT HELIX 276..294
FT /evidence="ECO:0007829|PDB:2PTD"
FT STRAND 301..305
FT /evidence="ECO:0007829|PDB:2PTD"
FT STRAND 311..313
FT /evidence="ECO:0007829|PDB:2PTD"
FT HELIX 315..321
FT /evidence="ECO:0007829|PDB:2PTD"
FT HELIX 322..326
FT /evidence="ECO:0007829|PDB:2PTD"
SQ SEQUENCE 329 AA; 38109 MW; 0D731F5604135CB4 CRC64;
MSNKKLILKL FICSTIFITF VFALHDKRVV AASSVNELEN WSKWMQPIPD SIPLARISIP
GTHDSGTFKL QNPIKQVWGM TQEYDFRYQM DHGARIFDIR GRLTDDNTIV LHHGPLYLYV
TLHEFINEAK QFLKDNPSET IIMSLKKEYE DMKGAEDSFS STFEKKYFVD PIFLKTEGNI
KLGDARGKIV LLKRYSGSNE PGGYNNFYWP DNETFTTTVN QNANVTVQDK YKVSYDEKVK
SIKDTMDETM NNSEDLNHLY INFTSLSSGG TAWNSPYYYA SYINPEIANY IKQKNPARVG
WVIQDYINEK WSPLLYQEVI RANKSLIKE
