PHLN_BURPS
ID PHLN_BURPS Reviewed; 700 AA.
AC Q9RGS8; Q63SC1;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 2.
DT 03-AUG-2022, entry version 99.
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=BPSL2403;
OS Burkholderia pseudomallei (strain K96243).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=272560;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RC STRAIN=SPT1;
RX PubMed=10523590; DOI=10.1128/jcm.37.11.3742-3745.1999;
RA Korbsrisate S., Suwanasai N., Leelaporn A., Ezaki T., Kawamura Y.,
RA Sarasombath S.;
RT "Cloning and characterization of a nonhemolytic phospholipase C gene from
RT Burkholderia pseudomallei.";
RL J. Clin. Microbiol. 37:3742-3745(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K96243;
RX PubMed=15377794; DOI=10.1073/pnas.0403302101;
RA Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.-M.,
RA Atkins T., Crossman L.C., Pitt T., Churcher C., Mungall K.L., Bentley S.D.,
RA Sebaihia M., Thomson N.R., Bason N., Beacham I.R., Brooks K., Brown K.A.,
RA Brown N.F., Challis G.L., Cherevach I., Chillingworth T., Cronin A.,
RA Crossett B., Davis P., DeShazer D., Feltwell T., Fraser A., Hance Z.,
RA Hauser H., Holroyd S., Jagels K., Keith K.E., Maddison M., Moule S.,
RA Price C., Quail M.A., Rabbinowitsch E., Rutherford K., Sanders M.,
RA Simmonds M., Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M.,
RA Whitehead S., Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J.;
RT "Genomic plasticity of the causative agent of melioidosis, Burkholderia
RT pseudomallei.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF107252; AAF17299.1; -; Genomic_DNA.
DR EMBL; BX571965; CAH36406.1; -; Genomic_DNA.
DR RefSeq; WP_004527449.1; NZ_CP009538.1.
DR RefSeq; YP_108995.1; NC_006350.1.
DR AlphaFoldDB; Q9RGS8; -.
DR SMR; Q9RGS8; -.
DR STRING; 272560.BPSL2403; -.
DR EnsemblBacteria; CAH36406; CAH36406; BPSL2403.
DR GeneID; 56528784; -.
DR KEGG; bps:BPSL2403; -.
DR PATRIC; fig|272560.51.peg.2993; -.
DR eggNOG; COG3511; Bacteria.
DR OMA; YHCSFIG; -.
DR BRENDA; 3.1.4.3; 1031.
DR Proteomes; UP000000605; Chromosome 1.
DR GO; GO:0034480; F:phosphatidylcholine phospholipase C activity; IEA:UniProtKB-EC.
DR GO; GO:0016042; P:lipid catabolic process; IEA:InterPro.
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 InterPro; IPR019546; TAT_signal_bac_arc.
DR PANTHER; PTHR31956; PTHR31956; 1.
DR Pfam; PF05506; DUF756; 2.
DR Pfam; PF04185; Phosphoesterase; 1.
DR TIGRFAMs; TIGR03396; PC_PLC; 1.
DR TIGRFAMs; TIGR01409; TAT_signal_seq; 1.
DR PROSITE; PS51318; TAT; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Reference proteome; Signal.
FT SIGNAL 1..34
FT /note="Tat-type signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT CHAIN 35..700
FT /note="Non-hemolytic phospholipase C"
FT /id="PRO_0000023940"
FT CONFLICT 80
FT /note="A -> T (in Ref. 1; AAF17299)"
FT /evidence="ECO:0000305"
FT CONFLICT 86
FT /note="S -> P (in Ref. 1; AAF17299)"
FT /evidence="ECO:0000305"
FT CONFLICT 124
FT /note="M -> T (in Ref. 1; AAF17299)"
FT /evidence="ECO:0000305"
FT CONFLICT 151
FT /note="D -> G (in Ref. 1; AAF17299)"
FT /evidence="ECO:0000305"
FT CONFLICT 254
FT /note="S -> A (in Ref. 1; AAF17299)"
FT /evidence="ECO:0000305"
FT CONFLICT 369
FT /note="E -> D (in Ref. 1; AAF17299)"
FT /evidence="ECO:0000305"
FT CONFLICT 383
FT /note="A -> P (in Ref. 1; AAF17299)"
FT /evidence="ECO:0000305"
FT CONFLICT 387
FT /note="T -> A (in Ref. 1; AAF17299)"
FT /evidence="ECO:0000305"
FT CONFLICT 436
FT /note="S -> P (in Ref. 1; AAF17299)"
FT /evidence="ECO:0000305"
FT CONFLICT 492
FT /note="A -> V (in Ref. 1; AAF17299)"
FT /evidence="ECO:0000305"
FT CONFLICT 532
FT /note="N -> K (in Ref. 1; AAF17299)"
FT /evidence="ECO:0000305"
FT CONFLICT 548
FT /note="L -> V (in Ref. 1; AAF17299)"
FT /evidence="ECO:0000305"
FT CONFLICT 574
FT /note="I -> L (in Ref. 1; AAF17299)"
FT /evidence="ECO:0000305"
FT CONFLICT 600
FT /note="S -> N (in Ref. 1; AAF17299)"
FT /evidence="ECO:0000305"
FT CONFLICT 627
FT /note="A -> T (in Ref. 1; AAF17299)"
FT /evidence="ECO:0000305"
FT CONFLICT 633
FT /note="T -> A (in Ref. 1; AAF17299)"
FT /evidence="ECO:0000305"
FT CONFLICT 638..640
FT /note="NAA -> KES (in Ref. 1; AAF17299)"
FT /evidence="ECO:0000305"
FT CONFLICT 668
FT /note="S -> T (in Ref. 1; AAF17299)"
FT /evidence="ECO:0000305"
FT CONFLICT 700
FT /note="A -> V (in Ref. 1; AAF17299)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 700 AA; 77077 MW; 9F7F4FB478ACFFD2 CRC64;
MTNQNRRDFL RLAAGTAGAA ALQLFPPVIR EALAIPANRR TGTIRDVEHI VILMQENRSF
DHYFGKLRGV RGFGDPRPLA LQNGKSVFHQ PVLLGPAELL PFHPDASNLG MQFLQDLPHG
WQDMHGAWNK GRYDRWIANK GTTTMAYLER DDIPFHYQLA DAFTICDAYH CSIPSSTDPN
RYYMWTGYVG NDGAGGGPVL GNEEAGYGWS TYPETLEQAG VSWKIYQDIG TGLDAAGSWG
WTQNPYIGNY GDNSLLYFNQ YRNAQPGSPL YDKARTGTNV SAGGTLFDVL QQDVKNGTLP
QVSWICAPEA YSEHPNWPAN YGAWYVEQVL KALTSNPDVW SKTALFITYD ENDGFFDHVA
PPFAPQSREN GLSTVSTAGE IFAGDATHMA GPYGLGPRVP MLVVSPWTKG GWVCSQTFDH
TSLLQFIEAR FNDRYSVRAP NVTPWRRAVC GDLTSAFNFS SPDGSWPQLP DTSGYAPPDR
NRHPSYVPVP PAAQSMPKQE AGLRAARALP YELFVLGRID QSTGKFKLTF ANTGRAGAAF
QVTAGNRLDG PWAYTVEARK RLSDEWSTAL TLSIYDLTVY GPNGFLCQFR GSTAAALGLS
ANPEVIYGYD VANGNITLRL SNRGRAAVRL TVTNAYGNAA PRVYELKPGQ RINDYWDLRD
SHSWYDLSVS DGAPNGFLRR FAGHVETGRP STSDPLIATA
