PHLC_BACCE
ID PHLC_BACCE Reviewed; 283 AA.
AC P09598;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Phospholipase C;
DE Short=PLC;
DE EC=3.1.4.3;
DE AltName: Full=Cereolysin A;
DE AltName: Full=Phosphatidylcholine cholinephosphohydrolase;
DE Flags: Precursor;
GN Name=plc;
OS Bacillus cereus.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1396;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=SE-1;
RX PubMed=3137122; DOI=10.1016/0378-1119(88)90466-0;
RA Johansen T., Holm T., Guddal P.H., Sletten K., Haugli F.B., Little C.;
RT "Cloning and sequencing of the gene encoding the phosphatidylcholine-
RT preferring phospholipase C of Bacillus cereus.";
RL Gene 65:293-304(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=VKM B-164;
RX PubMed=8387306;
RA Kuzmin N.P., Gavrilenko I.V., Krukov V.M., Karpov A.V.;
RT "Nucleotide sequence of phospholipase C and sphingomyelinase genes from
RT Bacillus cereus BKM-B164.";
RL Bioorg. Khim. 19:133-138(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 166-283.
RC STRAIN=IAM 1208;
RX PubMed=2841128; DOI=10.1111/j.1432-1033.1988.tb14186.x;
RA Yamada A., Tsukagoshi N., Udaka S., Sasaki T., Makino S., Nakamura S.,
RA Little C., Tomita M., Ikezawa H.;
RT "Nucleotide sequence and expression in Escherichia coli of the gene coding
RT for sphingomyelinase of Bacillus cereus.";
RL Eur. J. Biochem. 175:213-220(1988).
RN [4]
RP PROTEIN SEQUENCE OF 39-65.
RX PubMed=72664; DOI=10.1111/j.1432-1033.1977.tb11828.x;
RA Otnaess A.-B., Little C., Sletten K., Wallin R., Johnsen S., Flengsrud R.,
RA Prydz H.;
RT "Some characteristics of phospholipase C from Bacillus cereus.";
RL Eur. J. Biochem. 79:459-468(1977).
RN [5]
RP PROTEIN SEQUENCE OF 39-49.
RC STRAIN=IAM 1208;
RX PubMed=1939031; DOI=10.1093/oxfordjournals.jbchem.a123547;
RA Ikeda K., Inoue S., Amasaki C., Teshima K., Ikezawa H.;
RT "Kinetics of the hydrolysis of monodispersed and micellar
RT phosphatidylcholines catalyzed by a phospholipase C from Bacillus cereus.";
RL J. Biochem. 110:88-95(1991).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
RX PubMed=2493587; DOI=10.1038/338357a0;
RA Hough E., Hansen L.K., Birknes B., Jynge K., Hansen S., Hordvik A.,
RA Little C., Dodson E., Derewenda Z.;
RT "High-resolution (1.5 A) crystal structure of phospholipase C from Bacillus
RT cereus.";
RL Nature 338:357-360(1989).
CC -!- FUNCTION: Required, with sphingomyelinase, to effect target cell lysis
CC (hemolysis).
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 Note=Binds 3 Zn(2+) ions per subunit.;
CC -!- SUBUNIT: Monomer.
CC -!- SIMILARITY: Belongs to the bacterial zinc-metallophospholipase C
CC family. {ECO:0000255|PROSITE-ProRule:PRU00678}.
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; X64141; CAA45502.1; -; Genomic_DNA.
DR EMBL; X12854; CAA31332.1; -; Genomic_DNA.
DR EMBL; X12711; CAA31213.1; -; Genomic_DNA.
DR EMBL; X64140; CAA45501.1; ALT_TERM; Genomic_DNA.
DR PIR; S18978; PS0197.
DR RefSeq; WP_000731014.1; NZ_QSVI01000005.1.
DR PDB; 1AH7; X-ray; 1.50 A; A=39-283.
DR PDB; 1P5X; X-ray; 2.00 A; A=39-283.
DR PDB; 1P6D; X-ray; 2.00 A; A=39-283.
DR PDB; 1P6E; X-ray; 2.30 A; A=39-283.
DR PDB; 2FFZ; X-ray; 2.05 A; A=39-283.
DR PDB; 2FGN; X-ray; 2.04 A; A=39-283.
DR PDB; 2HUC; X-ray; 1.90 A; A=39-283.
DR PDBsum; 1AH7; -.
DR PDBsum; 1P5X; -.
DR PDBsum; 1P6D; -.
DR PDBsum; 1P6E; -.
DR PDBsum; 2FFZ; -.
DR PDBsum; 2FGN; -.
DR PDBsum; 2HUC; -.
DR AlphaFoldDB; P09598; -.
DR SMR; P09598; -.
DR STRING; 1396.DJ87_4438; -.
DR BindingDB; P09598; -.
DR ChEMBL; CHEMBL1293202; -.
DR DrugBank; DB03827; (3s)-3,4-Di-N-Hexanoyloxybutyl-1-Phosphocholine.
DR DrugBank; DB02225; 1,2-Di-N-Pentanoyl-Sn-Glycero-3-Dithiophosphocholine.
DR GeneID; 59156454; -.
DR GeneID; 64203811; -.
DR eggNOG; ENOG5030A2K; Bacteria.
DR OMA; IKANACC; -.
DR BRENDA; 3.1.4.3; 648.
DR SABIO-RK; P09598; -.
DR EvolutionaryTrace; P09598; -.
DR GO; GO:0034480; F:phosphatidylcholine phospholipase C activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
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 3D-structure; Cytolysis; Direct protein sequencing; Hemolysis; Hydrolase;
KW Metal-binding; Signal; Zinc; Zymogen.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT PROPEP 25..38
FT /evidence="ECO:0000269|PubMed:1939031,
FT ECO:0000269|PubMed:72664"
FT /id="PRO_0000023927"
FT CHAIN 39..283
FT /note="Phospholipase C"
FT /id="PRO_0000023928"
FT DOMAIN 39..283
FT /note="Zn-dependent PLC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00678"
FT BINDING 39
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT BINDING 52
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT BINDING 93
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT BINDING 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT BINDING 156
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT BINDING 160
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT BINDING 160
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT BINDING 166
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 180
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 184
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT VARIANT 212
FT /note="E -> D (in strain: IAM 1208)"
FT VARIANT 226
FT /note="S -> A (in strain: IAM 1208)"
FT VARIANT 239
FT /note="K -> R (in strain: IAM 1208)"
FT VARIANT 282
FT /note="D -> N (in strain: IAM 1208)"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:1AH7"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:1AH7"
FT HELIX 51..65
FT /evidence="ECO:0007829|PDB:1AH7"
FT HELIX 72..80
FT /evidence="ECO:0007829|PDB:1AH7"
FT HELIX 82..91
FT /evidence="ECO:0007829|PDB:1AH7"
FT TURN 92..94
FT /evidence="ECO:0007829|PDB:1AH7"
FT TURN 96..103
FT /evidence="ECO:0007829|PDB:1AH7"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:1AH7"
FT TURN 111..113
FT /evidence="ECO:0007829|PDB:1AH7"
FT HELIX 124..140
FT /evidence="ECO:0007829|PDB:1AH7"
FT HELIX 144..161
FT /evidence="ECO:0007829|PDB:1AH7"
FT TURN 164..169
FT /evidence="ECO:0007829|PDB:1AH7"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:1AH7"
FT HELIX 179..190
FT /evidence="ECO:0007829|PDB:1AH7"
FT HELIX 191..194
FT /evidence="ECO:0007829|PDB:1AH7"
FT HELIX 210..223
FT /evidence="ECO:0007829|PDB:1AH7"
FT HELIX 225..227
FT /evidence="ECO:0007829|PDB:1AH7"
FT HELIX 231..240
FT /evidence="ECO:0007829|PDB:1AH7"
FT HELIX 244..280
FT /evidence="ECO:0007829|PDB:1AH7"
SQ SEQUENCE 283 AA; 32383 MW; AC5452EFF2E22B19 CRC64;
MKKKVLALAA AITVVAPLQS VAFAHENDGG SKIKIVHRWS AEDKHKEGVN SHLWIVNRAI
DIMSRNTTLV KQDRVAQLNE WRTELENGIY AADYENPYYD NSTFASHFYD PDNGKTYIPF
AKQAKETGAK YFKLAGESYK NKDMKQAFFY LGLSLHYLGD VNQPMHAANF TNLSYPQGFH
SKYENFVDTI KDNYKVTDGN GYWNWKGTNP EEWIHGAAVV AKQDYSGIVN DNTKDWFVKA
AVSQEYADKW RAEVTPMTGK RLMDAQRVTA GYIQLWFDTY GDR
