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Database: UniProt
Entry: PHLN_PSEAE
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Original site: PHLN_PSEAE 
ID   PHLN_PSEAE              Reviewed;         692 AA.
AC   P15713;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   08-DEC-2000, sequence version 2.
DT   27-MAR-2024, entry version 132.
DE   RecName: Full=Non-hemolytic phospholipase C;
DE            EC=3.1.4.3;
DE   AltName: Full=PLC-N;
DE   AltName: Full=Phosphatidylcholine cholinephosphohydrolase;
DE   AltName: Full=Phosphatidylcholine-hydrolyzing phospholipase C;
DE            Short=PC-PLC;
DE   Flags: Precursor;
GN   Name=plcN; OrderedLocusNames=PA3319;
OS   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS   14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2120196; DOI=10.1128/jb.172.10.5915-5923.1990;
RA   Ostroff R.M., Vasil A.I., Vasil M.L.;
RT   "Molecular comparison of a nonhemolytic and a hemolytic phospholipase C
RT   from Pseudomonas aeruginosa.";
RL   J. Bacteriol. 172:5915-5923(1990).
RN   [2]
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 phosphatidylserine as well as 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; M59304; AAA25968.1; -; Genomic_DNA.
DR   EMBL; M30223; AAA25969.1; -; Genomic_DNA.
DR   EMBL; AE004091; AAG06707.1; -; Genomic_DNA.
DR   PIR; A36143; A36143.
DR   PIR; E83230; E83230.
DR   RefSeq; NP_252009.1; NC_002516.2.
DR   RefSeq; WP_003113149.1; NZ_QZGE01000017.1.
DR   AlphaFoldDB; P15713; -.
DR   SMR; P15713; -.
DR   STRING; 208964.PA3319; -.
DR   PaxDb; 208964-PA3319; -.
DR   GeneID; 882484; -.
DR   KEGG; pae:PA3319; -.
DR   PATRIC; fig|208964.12.peg.3476; -.
DR   PseudoCAP; PA3319; -.
DR   HOGENOM; CLU_008770_1_0_6; -.
DR   InParanoid; P15713; -.
DR   OrthoDB; 9770871at2; -.
DR   PhylomeDB; P15713; -.
DR   BioCyc; PAER208964:G1FZ6-3383-MONOMER; -.
DR   Proteomes; UP000002438; Chromosome.
DR   GO; GO:0016298; F:lipase activity; IDA:PseudoCAP.
DR   GO; GO:0034480; F:phosphatidylcholine phospholipase C activity; IEA:UniProtKB-EC.
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   CDD; cd16014; PLC; 1.
DR   Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 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   NCBIfam; TIGR03396; PC_PLC; 1.
DR   PANTHER; PTHR31956:SF8; ACID PHOSPHATASE PHOA (AFU_ORTHOLOGUE AFUA_1G03570); 1.
DR   PANTHER; PTHR31956; NON-SPECIFIC PHOSPHOLIPASE C4-RELATED; 1.
DR   Pfam; PF04185; Phosphoesterase; 1.
DR   Pfam; PF05506; PLipase_C_C; 2.
DR   PROSITE; PS51318; TAT; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Reference proteome; Signal.
FT   SIGNAL          1..35
FT                   /note="Tat-type signal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT   CHAIN           36..692
FT                   /note="Non-hemolytic phospholipase C"
FT                   /id="PRO_0000023941"
FT   CONFLICT        18
FT                   /note="G -> A (in Ref. 1; AAA25968/AAA25969)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        385
FT                   /note="P -> A (in Ref. 1; AAA25968/AAA25969)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        584..585
FT                   /note="ER -> DG (in Ref. 1; AAA25968/AAA25969)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   692 AA;  77145 MW;  6B16C0BEEB25CAEF CRC64;
     MISKSRRSFI RLAAGTVGAT VATSMLPSSI QAALAIPAHR RHGNLKDVEH VVILMQENRS
     FDHYFGTLKG VRGFGDRMAI PLPDGQRVWH QKGSKGEILP YHFDTSTTSA QRVDGTPHTW
     PDAQQAWNEG RMDKWLPAKT ERSLGYYKEQ DIAFQFAMAN AFTICDAYHC SFQGGTNPNR
     LFLWTGTNDP LGQHGGPVTT NDHDSNGPVE QGYTWTTYPE RLQAAGITWR VYQDMADNFS
     DNPLIGFRQY RAAAPDSPLI VNGLSTWKLD ALKRDVLANS LPQVSWIVAP AKYSEHPGPS
     SPIWGAEYTS WVLDALTANP EVWSKTALLV MFDENDGFFD HVAPPAAPSL NKDGTLRGKT
     TADATLEWHT KGDIRYRNQP YGLGPRVPMY VISPWSKGGW VNSQVFDHTS VIRFLEQRFG
     VMEPNISPWR RAVCGDLTSA FNFANPNNEP FPELPDTSQA DAIVASQIKL PKPKPPAVAA
     MPKQEMGIRP ARALPYELGV HARYRSGGDA LSLTFANTGK AGAVFQVFDL LDSENPPKRY
     TVGARKRLHD SFQGDASGDY HLEVHGPNGF LRVFRGNLRR DLAERKAPLP EVRIDYEPLF
     GNLRVQLINR GRHPVKLTVK DNVYRQGERR TVNVPPGQRR EVRYSLRSSG NWYDFSVSAQ
     GADSFLRRFS GRMEDGRSGF SDPGMGLGTL TF
//
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