PHLC_LISMO
ID PHLC_LISMO Reviewed; 289 AA.
AC P33378;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Phospholipase C;
DE Short=PLC;
DE EC=3.1.4.3;
DE AltName: Full=Lecithinase;
DE AltName: Full=Phosphatidylcholine cholinephosphohydrolase;
DE Flags: Precursor;
GN Name=plcB; Synonyms=prtC; OrderedLocusNames=lmo0205;
OS Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=169963;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LO28 / Serovar 1/2c;
RX PubMed=1309513; DOI=10.1128/iai.60.1.219-230.1992;
RA Vazquez-Boland J.-A., Kocks C., Dramsi S., Ohayon H., Geoffroy C.,
RA Mengaud J., Cossart P.;
RT "Nucleotide sequence of the lecithinase operon of Listeria monocytogenes
RT and possible role of lecithinase in cell-to-cell spread.";
RL Infect. Immun. 60:219-230(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=EGD / Serovar 1/2a;
RX PubMed=1582425; DOI=10.1002/j.1460-2075.1992.tb05252.x;
RA Domann E., Wehland J., Rohde M., Pistor S., Hartl M., Goebel W.,
RA Leimeister-Waechter M., Wuensher M., Chakraborty T.;
RT "A novel bacterial virulence gene in Listeria monocytogenes required for
RT host cell microfilament interaction with homology to the proline-rich
RT region of vinculin.";
RL EMBO J. 11:1981-1990(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=11679669; DOI=10.1126/science.1063447;
RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT "Comparative genomics of Listeria species.";
RL Science 294:849-852(2001).
RN [4]
RP PROTEIN SEQUENCE OF 144-152.
RX PubMed=1904842; DOI=10.1128/iai.59.7.2382-2388.1991;
RA Geoffroy C., Raveneau J., Beretti J.-L., Lecroisey A.,
RA Vazquez-Boland J.-A., Alouf J.E., Berche P.;
RT "Purification and characterization of an extracellular 29-kilodalton
RT phospholipase C from Listeria monocytogenes.";
RL Infect. Immun. 59:2382-2388(1991).
CC -!- FUNCTION: Important role in the infectious process. May contribute to
CC efficient lysis of the two-membrane vacuoles that surround the bacteria
CC after direct cell-to-cell spread.
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00678};
CC Note=Binds 3 Zn(2+) ions per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00678};
CC -!- SIMILARITY: Belongs to the bacterial zinc-metallophospholipase C
CC family. {ECO:0000255|PROSITE-ProRule:PRU00678}.
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DR EMBL; M82881; AAA25270.1; -; Genomic_DNA.
DR EMBL; X59723; CAA42408.1; -; Genomic_DNA.
DR EMBL; AL591974; CAD00732.1; -; Genomic_DNA.
DR PIR; AF1100; AF1100.
DR PIR; C43868; C43868.
DR PIR; S20888; S20888.
DR RefSeq; NP_463736.1; NC_003210.1.
DR RefSeq; WP_010989375.1; NZ_CP023861.1.
DR AlphaFoldDB; P33378; -.
DR SMR; P33378; -.
DR STRING; 169963.lmo0205; -.
DR PaxDb; P33378; -.
DR EnsemblBacteria; CAD00732; CAD00732; CAD00732.
DR GeneID; 987036; -.
DR KEGG; lmo:lmo0205; -.
DR PATRIC; fig|169963.11.peg.210; -.
DR eggNOG; ENOG5030A2K; Bacteria.
DR HOGENOM; CLU_841040_0_0_9; -.
DR OMA; IKANACC; -.
DR BioCyc; LMON169963:LMO0205-MON; -.
DR Proteomes; UP000000817; Chromosome.
DR GO; GO:0034480; F:phosphatidylcholine phospholipase C activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd11009; Zn_dep_PLPC; 1.
DR Gene3D; 1.10.575.10; -; 1.
DR InterPro; IPR008947; PLipase_C/P1_nuclease_dom_sf.
DR InterPro; IPR029002; PLPC/GPLD1.
DR InterPro; IPR001531; Zn_PLipaseC.
DR Pfam; PF00882; Zn_dep_PLPC; 1.
DR PRINTS; PR00479; PRPHPHLPASEC.
DR SMART; SM00770; Zn_dep_PLPC; 1.
DR SUPFAM; SSF48537; SSF48537; 1.
DR PROSITE; PS00384; PROKAR_ZN_DEPEND_PLPC_1; 1.
DR PROSITE; PS51346; PROKAR_ZN_DEPEND_PLPC_2; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Hydrolase; Metal-binding; Reference proteome;
KW Signal; Zinc; Zymogen.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT PROPEP 26..51
FT /evidence="ECO:0000250"
FT /id="PRO_0000023937"
FT CHAIN 52..289
FT /note="Phospholipase C"
FT /id="PRO_0000023938"
FT DOMAIN 52..289
FT /note="Zn-dependent PLC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00678"
FT BINDING 52
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00678"
FT BINDING 65
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00678"
FT BINDING 106
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00678"
FT BINDING 120
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00678"
FT BINDING 169
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00678"
FT BINDING 173
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00678"
FT BINDING 173
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00678"
FT BINDING 179
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00678"
FT BINDING 193
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00678"
FT BINDING 197
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00678"
FT CONFLICT 5
FT /note="K -> N (in Ref. 2; CAA42408)"
FT /evidence="ECO:0000305"
FT CONFLICT 13
FT /note="I -> T (in Ref. 2; CAA42408)"
FT /evidence="ECO:0000305"
FT CONFLICT 222
FT /note="D -> G (in Ref. 2; CAA42408)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 289 AA; 33278 MW; 0F35A2A3EDA6E372 CRC64;
MKFKKVVLGM CLIASVLVFP VTIKANACCD EYLQTPAAPH DIDSKLPHKL SWSADNPTNT
DVNTHYWLFK QAEKILAKDV NHMRANLMNE LKKFDKQIAQ GIYDADHKNP YYDTSTFLSH
FYNPDRDNTY LPGFANAKIT GAKYFNQSVT DYREGKFDTA FYKLGLAIHY YTDISQPMHA
NNFTAISYPP GYHCAYENYV DTIKHNYQAT EDMVAKRFCS DDVKDWLYEN AKRAKADYPK
IVNAKTKKSY LVGNSEWKKD TVEPTGARLR DSQQTLAGFL EFWSKKTNE
