PLC_BACTU
ID PLC_BACTU Reviewed; 329 AA.
AC P08954;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1988, sequence version 1.
DT 25-MAY-2022, entry version 116.
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 thuringiensis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1428;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=ATCC 10792 / DSM 2046 / LMG 7138 / NCIMB 9134 / NRRL HD-735;
RX PubMed=3194218; DOI=10.1093/nar/16.21.10383;
RA Henner D.J., Yang M., Chen E., Helmiss R., Rodriguez H., Low M.G.;
RT "Sequence of the Bacillus thuringiensis phosphatidylinositol specific
RT phospholipase C.";
RL Nucleic Acids Res. 16:10383-10383(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 10792 / DSM 2046 / LMG 7138 / NCIMB 9134 / NRRL HD-735;
RX PubMed=2548063; DOI=10.1111/j.1365-2958.1989.tb00209.x;
RA Lechner M., Kupke T., Kaim G., Stefanovic S., Goetz F.;
RT "Molecular characterization and sequence of phosphatidylinositol-specific
RT phospholipase C of Bacillus thuringiensis.";
RL Mol. Microbiol. 3:621-626(1989).
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; X12952; CAA31410.1; -; Genomic_DNA.
DR EMBL; X14178; CAA32378.1; -; Genomic_DNA.
DR PIR; A30760; A30760.
DR RefSeq; WP_000066296.1; NZ_WJDT01000031.1.
DR PDB; 1T6M; X-ray; 2.11 A; A/B=32-329.
DR PDB; 2OR2; X-ray; 1.84 A; A/B=32-327.
DR PDB; 3EA1; X-ray; 1.75 A; A/B=32-329.
DR PDB; 3EA2; X-ray; 1.95 A; A/B=32-329.
DR PDB; 3EA3; X-ray; 1.78 A; A/B=32-329.
DR PDBsum; 1T6M; -.
DR PDBsum; 2OR2; -.
DR PDBsum; 3EA1; -.
DR PDBsum; 3EA2; -.
DR PDBsum; 3EA3; -.
DR AlphaFoldDB; P08954; -.
DR SMR; P08954; -.
DR GeneID; 67467973; -.
DR BRENDA; 4.6.1.13; 711.
DR SABIO-RK; P08954; -.
DR EvolutionaryTrace; P08954; -.
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; Direct protein sequencing; Lipid degradation;
KW Lipid metabolism; Lyase; Secreted; Signal.
FT SIGNAL 1..31
FT CHAIN 32..329
FT /note="1-phosphatidylinositol phosphodiesterase"
FT /id="PRO_0000024295"
FT DOMAIN 51..194
FT /note="PI-PLC X-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT ACT_SITE 63
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT ACT_SITE 113
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT HELIX 35..39
FT /evidence="ECO:0007829|PDB:3EA1"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:1T6M"
FT TURN 44..47
FT /evidence="ECO:0007829|PDB:3EA1"
FT TURN 54..56
FT /evidence="ECO:0007829|PDB:3EA1"
FT STRAND 59..62
FT /evidence="ECO:0007829|PDB:3EA1"
FT TURN 63..66
FT /evidence="ECO:0007829|PDB:3EA1"
FT HELIX 68..71
FT /evidence="ECO:0007829|PDB:2OR2"
FT HELIX 73..79
FT /evidence="ECO:0007829|PDB:3EA1"
FT HELIX 86..91
FT /evidence="ECO:0007829|PDB:3EA1"
FT STRAND 96..103
FT /evidence="ECO:0007829|PDB:3EA1"
FT STRAND 109..113
FT /evidence="ECO:0007829|PDB:3EA1"
FT STRAND 116..121
FT /evidence="ECO:0007829|PDB:3EA1"
FT HELIX 122..135
FT /evidence="ECO:0007829|PDB:3EA1"
FT STRAND 141..147
FT /evidence="ECO:0007829|PDB:3EA1"
FT HELIX 159..166
FT /evidence="ECO:0007829|PDB:3EA1"
FT TURN 167..169
FT /evidence="ECO:0007829|PDB:3EA1"
FT HELIX 182..185
FT /evidence="ECO:0007829|PDB:3EA1"
FT STRAND 188..196
FT /evidence="ECO:0007829|PDB:3EA1"
FT STRAND 213..218
FT /evidence="ECO:0007829|PDB:3EA1"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:3EA1"
FT STRAND 224..228
FT /evidence="ECO:0007829|PDB:3EA1"
FT HELIX 235..250
FT /evidence="ECO:0007829|PDB:3EA1"
FT TURN 251..254
FT /evidence="ECO:0007829|PDB:3EA1"
FT STRAND 258..263
FT /evidence="ECO:0007829|PDB:3EA1"
FT HELIX 272..274
FT /evidence="ECO:0007829|PDB:3EA1"
FT HELIX 276..294
FT /evidence="ECO:0007829|PDB:3EA1"
FT STRAND 301..305
FT /evidence="ECO:0007829|PDB:3EA1"
FT STRAND 308..313
FT /evidence="ECO:0007829|PDB:3EA1"
FT HELIX 315..321
FT /evidence="ECO:0007829|PDB:3EA1"
FT HELIX 322..326
FT /evidence="ECO:0007829|PDB:3EA1"
SQ SEQUENCE 329 AA; 38091 MW; CB89586F3195267C CRC64;
MSNKKLILKL FICSTIFITF VFALHDKRVV AASSVNELEN WSKWMQPIPD NIPLARISIP
GTHDSGTFKL QNPIKQVWGM TQEYDFRYQM DHGARIFDIR GRLTDDNTIV LHHGPLYLYV
TLHEFINEAK QFLKDNPSET IIMSLKKEYE DMKGAEGSFS STFEKNYFVD PIFLKTEGNI
KLGDARGKIV LLKRYSGSNE SGGYNNFYWP DNETFTTTVN QNVNVTVQDK YKVNYDEKVK
SIKDTMDETM NNSEDLNHLY INFTSLSSGG TAWNSPYYYA SYINPEIAND IKQKNPTRVG
WVIQDYINEK WSPLLYQEVI RANKSLIKE
