PHLC_PSEAE
ID PHLC_PSEAE Reviewed; 730 AA.
AC P06200; Q9I597;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2001, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Hemolytic phospholipase C;
DE EC=3.1.4.3;
DE AltName: Full=Heat-labile hemolysin;
DE AltName: Full=PLC-H;
DE AltName: Full=Phosphatidylcholine cholinephosphohydrolase;
DE Flags: Precursor;
GN Name=plcH; OrderedLocusNames=PA0844;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3087958; DOI=10.1128/jb.167.1.291-298.1986;
RA Pritchard A.E., Vasil M.L.;
RT "Nucleotide sequence and expression of a phosphate-regulated gene encoding
RT a secreted hemolysin of Pseudomonas aeruginosa.";
RL J. Bacteriol. 167:291-298(1986).
RN [2]
RP SEQUENCE REVISION.
RA Pritchard A.E.;
RL Submitted (AUG-1986) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
CC -!- FUNCTION: Hydrolyzes sphingomyelin in addition to phosphatidylcholine.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1,2-diacyl-
CC sn-glycerol + H(+) + phosphocholine; Xref=Rhea:RHEA:10604,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17815,
CC ChEBI:CHEBI:57643, ChEBI:CHEBI:295975; EC=3.1.4.3;
CC -!- PTM: Predicted to be exported by the Tat system. The position of the
CC signal peptide cleavage has not been experimentally proven.
CC -!- SIMILARITY: Belongs to the bacterial phospholipase C family.
CC {ECO:0000305}.
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DR EMBL; M13047; AAA25966.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG04233.1; -; Genomic_DNA.
DR PIR; A26391; A26391.
DR PIR; B83540; B83540.
DR RefSeq; NP_249535.1; NC_002516.2.
DR RefSeq; WP_003114225.1; NZ_QZGE01000007.1.
DR AlphaFoldDB; P06200; -.
DR SMR; P06200; -.
DR STRING; 287.DR97_1100; -.
DR PaxDb; P06200; -.
DR EnsemblBacteria; AAG04233; AAG04233; PA0844.
DR GeneID; 879296; -.
DR KEGG; pae:PA0844; -.
DR PATRIC; fig|208964.12.peg.876; -.
DR PseudoCAP; PA0844; -.
DR HOGENOM; CLU_008770_1_0_6; -.
DR InParanoid; P06200; -.
DR OMA; GYYCSLH; -.
DR PhylomeDB; P06200; -.
DR BioCyc; PAER208964:G1FZ6-859-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005615; C:extracellular space; IDA:PseudoCAP.
DR GO; GO:0016298; F:lipase activity; IDA:PseudoCAP.
DR GO; GO:0034480; F:phosphatidylcholine phospholipase C activity; IDA:PseudoCAP.
DR GO; GO:0033188; F:sphingomyelin synthase activity; IDA:PseudoCAP.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0044179; P:hemolysis in another organism; IDA:PseudoCAP.
DR GO; GO:0016042; P:lipid catabolic process; IEA:InterPro.
DR GO; GO:0015628; P:protein secretion by the type II secretion system; IDA:PseudoCAP.
DR Gene3D; 3.40.720.10; -; 2.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR017767; Bact_PC-PLC.
DR InterPro; IPR007312; Phosphoesterase.
DR InterPro; IPR008475; PLipase_C_C.
DR InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR31956; PTHR31956; 1.
DR Pfam; PF05506; DUF756; 2.
DR Pfam; PF04185; Phosphoesterase; 1.
DR TIGRFAMs; TIGR03396; PC_PLC; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Cytolysis; Hemolysis; Hydrolase; Reference proteome; Signal; Toxin;
KW Virulence.
FT SIGNAL 1..38
FT /note="Tat-type signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT CHAIN 39..730
FT /note="Hemolytic phospholipase C"
FT /id="PRO_0000023939"
FT CONFLICT 436
FT /note="V -> L (in Ref. 1; AAA25966)"
FT /evidence="ECO:0000305"
FT CONFLICT 550..552
FT /note="GHS -> DTA (in Ref. 1; AAA25966)"
FT /evidence="ECO:0000305"
FT CONFLICT 654..666
FT /note="SVTVTPNPAYTRE -> RRDGDAEPGLYPG (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 730 AA; 82667 MW; 7002A87ABD8DD5F5 CRC64;
MTENWKFRRR TFLKHGAQAA TLAGLSGLFP ETLRRALAVE PDIRTGTIQD VQHVVILMQE
NRSFDHYFGH LNGVRGFNDP RALKRQDGKP VWYQNYKYEF SPYHWDTKVT SAQWVSSQNH
EWSAFHAIWN QGRNDKWMAV QYPEAMGYFK RGDIPYYYAL ADAFTLCEAY HQSMMGPTNP
NRLYHMSGRA APSGDGKDVH IGNDMGDGTI GASGTVDWTT YPERLSAAGV DWRVYQEGGY
RSSSLWYLYV DAYWKYRLQE QNNYDCNALA WFRNFKNAPR DSDLWQRAML ARGVDQLRKD
VQENTLPQVS WIVAPYCYCE HPWWGPSFGE YYVTRVLEAL TSNPEVWART VFILNYDEGD
GFYDHASAPV PPWKDGVGLS TVSTAGEIEV SSGLPIGLGH RVPLIAISPW SKGGKVSAEV
FDHTSVLRFL ERRFGVVEEN ISPWRRAVCG DLTSLFDFQG AGDTQVAPDL TNVPQSDARK
EDAYWQQFYR PSPKYWSYEP KSLPGQEKGQ RPTLAVPYQL HATLALDIAA GKLRLTLGND
GMSLPGNPQG HSAAVFQVQP REVGNPRFYT VTSYPVVQES GEELGRTLND ELDDLLDANG
RYAFEVHGPN GFFREFHGNL HLAAQMARPE VSVTYQRNGN LQLNIRNLGR LPCSVTVTPN
PAYTREGSRR YELEPNQAIS EVWLLRSSQG WYDLSVTASN TEANYLRRLA GHVETGKPSR
SDPLLDIAAT
