PLC_STAAE
ID PLC_STAAE Reviewed; 312 AA.
AC P45723; A6QD81;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 25-MAY-2022, entry version 113.
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=plc; OrderedLocusNames=NWMN_0041;
OS Staphylococcus aureus (strain Newman).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=426430;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8225585; DOI=10.1128/iai.61.12.5078-5089.1993;
RA Daugherty S., Low M.G.;
RT "Cloning, expression, and mutagenesis of phosphatidylinositol-specific
RT phospholipase C from Staphylococcus aureus: a potential staphylococcal
RT virulence factor.";
RL Infect. Immun. 61:5078-5089(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Newman;
RX PubMed=17951380; DOI=10.1128/jb.01000-07;
RA Baba T., Bae T., Schneewind O., Takeuchi F., Hiramatsu K.;
RT "Genome sequence of Staphylococcus aureus strain Newman and comparative
RT analysis of staphylococcal genomes: polymorphism and evolution of two major
RT pathogenicity islands.";
RL J. Bacteriol. 190:300-310(2008).
CC -!- FUNCTION: Cleaves glycosylphosphatidylinositol (GPI) and
CC phosphatidylinositol (PI) anchors but not PI phosphates. Potential
CC virulence factor.
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.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAF66313.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; L19298; AAA16442.1; -; Unassigned_DNA.
DR EMBL; AP009351; BAF66313.1; ALT_INIT; Genomic_DNA.
DR PDB; 3V16; X-ray; 2.05 A; A=11-312.
DR PDB; 3V18; X-ray; 2.34 A; A=12-312.
DR PDB; 3V1H; X-ray; 1.90 A; A=13-312.
DR PDB; 4F2B; X-ray; 2.16 A; A/B=11-312.
DR PDB; 4F2T; X-ray; 2.30 A; A=11-312.
DR PDB; 4F2U; X-ray; 2.19 A; A=11-312.
DR PDB; 4I8Y; X-ray; 2.10 A; A=11-312.
DR PDB; 4I90; X-ray; 1.65 A; A=11-312.
DR PDB; 4I9J; X-ray; 1.85 A; A=11-312.
DR PDB; 4I9M; X-ray; 2.20 A; A=11-312.
DR PDB; 4I9T; X-ray; 2.00 A; A=11-312.
DR PDB; 4RV3; X-ray; 2.00 A; A=12-312.
DR PDB; 4S3G; X-ray; 2.50 A; A=11-312.
DR PDBsum; 3V16; -.
DR PDBsum; 3V18; -.
DR PDBsum; 3V1H; -.
DR PDBsum; 4F2B; -.
DR PDBsum; 4F2T; -.
DR PDBsum; 4F2U; -.
DR PDBsum; 4I8Y; -.
DR PDBsum; 4I90; -.
DR PDBsum; 4I9J; -.
DR PDBsum; 4I9M; -.
DR PDBsum; 4I9T; -.
DR PDBsum; 4RV3; -.
DR PDBsum; 4S3G; -.
DR AlphaFoldDB; P45723; -.
DR SMR; P45723; -.
DR EnsemblBacteria; BAF66313; BAF66313; NWMN_0041.
DR KEGG; sae:NWMN_0041; -.
DR HOGENOM; CLU_024117_3_1_9; -.
DR OMA; ITMPGTH; -.
DR BRENDA; 4.6.1.13; 3352.
DR Proteomes; UP000006386; Chromosome.
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;
KW Virulence.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..312
FT /note="1-phosphatidylinositol phosphodiesterase"
FT /id="PRO_0000024297"
FT DOMAIN 27..176
FT /note="PI-PLC X-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT ACT_SITE 40
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT ACT_SITE 90
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT CONFLICT 234..236
FT /note="AKA -> LKL (in Ref. 1; AAA16442)"
FT /evidence="ECO:0000305"
FT CONFLICT 258..260
FT /note="AFN -> DL (in Ref. 1; AAA16442)"
FT /evidence="ECO:0000305"
FT HELIX 14..16
FT /evidence="ECO:0007829|PDB:4I90"
FT HELIX 18..24
FT /evidence="ECO:0007829|PDB:4I90"
FT HELIX 31..33
FT /evidence="ECO:0007829|PDB:4I90"
FT STRAND 36..39
FT /evidence="ECO:0007829|PDB:4I90"
FT HELIX 42..46
FT /evidence="ECO:0007829|PDB:4I90"
FT HELIX 50..56
FT /evidence="ECO:0007829|PDB:4I90"
FT HELIX 63..68
FT /evidence="ECO:0007829|PDB:4I90"
FT STRAND 73..82
FT /evidence="ECO:0007829|PDB:4I90"
FT STRAND 85..90
FT /evidence="ECO:0007829|PDB:4I90"
FT STRAND 93..98
FT /evidence="ECO:0007829|PDB:4I90"
FT HELIX 99..112
FT /evidence="ECO:0007829|PDB:4I90"
FT STRAND 118..124
FT /evidence="ECO:0007829|PDB:4I90"
FT HELIX 136..143
FT /evidence="ECO:0007829|PDB:4I90"
FT TURN 144..146
FT /evidence="ECO:0007829|PDB:4I90"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:4I90"
FT TURN 151..153
FT /evidence="ECO:0007829|PDB:4I90"
FT HELIX 164..167
FT /evidence="ECO:0007829|PDB:4I90"
FT STRAND 170..175
FT /evidence="ECO:0007829|PDB:4I90"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:4I90"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:4I90"
FT STRAND 189..191
FT /evidence="ECO:0007829|PDB:4RV3"
FT STRAND 199..205
FT /evidence="ECO:0007829|PDB:4I90"
FT TURN 206..209
FT /evidence="ECO:0007829|PDB:4I90"
FT STRAND 210..216
FT /evidence="ECO:0007829|PDB:4I90"
FT HELIX 222..237
FT /evidence="ECO:0007829|PDB:4I90"
FT STRAND 244..249
FT /evidence="ECO:0007829|PDB:4I90"
FT STRAND 256..258
FT /evidence="ECO:0007829|PDB:3V1H"
FT STRAND 259..261
FT /evidence="ECO:0007829|PDB:3V16"
FT HELIX 262..279
FT /evidence="ECO:0007829|PDB:4I90"
FT STRAND 287..292
FT /evidence="ECO:0007829|PDB:4I90"
FT HELIX 303..309
FT /evidence="ECO:0007829|PDB:4I90"
SQ SEQUENCE 312 AA; 35255 MW; 6E2F1ADB3EE5382D CRC64;
MSGWYHSAHA SDSLSKSPEN WMSKLDDGKH LTEINIPGSH DSGSFTLKDP VKSVWAKTQD
KDYLTQMKSG VRFFDIRGRA SADNMISVHH GMVYLHHELG KFLDDAKYYL SAYPNETIVM
SMKKDYDSDS KVTKTFEEIF REYYYNNPQY QNLFYTGSNA NPTLKETKGK IVLFNRMGGT
YIKSGYGADT SGIQWADNAT FETKINNGSL NLKVQDEYKD YYDKKVEAVK NLLAKAKTDS
NKDNVYVNFL SVASGGSAFN STYNYASHIN PEIAKTIKAN GKARTGWLIV DYAGYTWPGY
DDIVSEIIDS NK
