P09598 (PHLC_BACCE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Phospholipase C
Short name=PLC
EC=3.1.4.3

Alternative name(s):
Cereolysin A
Phosphatidylcholine cholinephosphohydrolase

Gene names

Name:

plc

Organism

Bacillus cereus

Taxonomic identifier

1396 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

Protein attributes

Sequence length	283 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Required, with sphingomyelinase, to effect target cell lysis (hemolysis).
Catalytic activity	A phosphatidylcholine + H2O = 1,2-diacyl-sn-glycerol + phosphocholine.
Cofactor	Binds 3 zinc ions per subunit.
Subunit structure	Monomer.
Sequence similarities	Belongs to the bacterial zinc-metallophospholipase C family. Contains 1 Zn-dependent PLC domain.

Ontologies

Keywords
Biological process	Cytolysis Hemolysis
Domain	Signal
Ligand	Metal-binding Zinc
Molecular function	Hydrolase
PTM	Zymogen
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological_process	cytolysis Inferred from electronic annotation. Source: UniProtKB-KW hemolysis in other organism Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	phosphatidylcholine phospholipase C activity Inferred from electronic annotation. Source: EC zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 24

24

Potential

Propeptide

25 – 38

14

PRO_0000023927

Chain

39 – 283

245

Phospholipase C

PRO_0000023928

Regions

Domain

39 – 283

245

Zn-dependent PLC

Sites

Metal binding

39

1

Zinc 3

Metal binding

52

1

Zinc 3

Metal binding

93

1

Zinc 1

Metal binding

107

1

Zinc 1

Metal binding

156

1

Zinc 1

Metal binding

160

1

Zinc 1

Metal binding

160

1

Zinc 3

Metal binding

166

1

Zinc 2

Metal binding

180

1

Zinc 2

Metal binding

184

1

Zinc 2

Natural variations

Natural variant

212

1

E → D in strain: IAM 1208.

Natural variant

226

1

S → A in strain: IAM 1208.

Natural variant

239

1

K → R in strain: IAM 1208.

Natural variant

282

1

D → N in strain: IAM 1208.

Secondary structure

1

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283

Helix Strand Turn

Details...

Beta strand

43 – 45

3

Helix

47 – 49

3

Helix

51 – 65

15

Helix

72 – 80

9

Helix

82 – 91

10

Turn

92 – 94

3

Turn

96 – 103

8

Helix

105 – 107

3

Turn

111 – 113

3

Helix

124 – 140

17

Helix

144 – 161

18

Turn

164 – 169

6

Beta strand

174 – 176

3

Helix

179 – 190

12

Helix

191 – 194

4

Helix

210 – 223

14

Helix

225 – 227

3

Helix

231 – 240

10

Helix

244 – 280

37

Sequences

	Sequence		Length	Mass (Da)
	P09598 [UniParc]. Last modified July 1, 1989. Version 1. Checksum: AC5452EFF2E22B19	FASTA	283	32,383
	10 20 30 40 50 60 MKKKVLALAA AITVVAPLQS VAFAHENDGG SKIKIVHRWS AEDKHKEGVN SHLWIVNRAI 70 80 90 100 110 120 DIMSRNTTLV KQDRVAQLNE WRTELENGIY AADYENPYYD NSTFASHFYD PDNGKTYIPF 130 140 150 160 170 180 AKQAKETGAK YFKLAGESYK NKDMKQAFFY LGLSLHYLGD VNQPMHAANF TNLSYPQGFH 190 200 210 220 230 240 SKYENFVDTI KDNYKVTDGN GYWNWKGTNP EEWIHGAAVV AKQDYSGIVN DNTKDWFVKA 250 260 270 280 AVSQEYADKW RAEVTPMTGK RLMDAQRVTA GYIQLWFDTY GDR

References

[1]	"Cloning and sequencing of the gene encoding the phosphatidylcholine-preferring phospholipase C of Bacillus cereus." Johansen T., Holm T., Guddal P.H., Sletten K., Haugli F.B., Little C. Gene 65:293-304(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: SE-1.
[2]	"Nucleotide sequence of phospholipase C and sphingomyelinase genes from Bacillus cereus BKM-B164." Kuzmin N.P., Gavrilenko I.V., Krukov V.M., Karpov A.V. Bioorg. Khim. 19:133-138(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: VKM B-164.
[3]	"Nucleotide sequence and expression in Escherichia coli of the gene coding for sphingomyelinase of Bacillus cereus." Yamada A., Tsukagoshi N., Udaka S., Sasaki T., Makino S., Nakamura S., Little C., Tomita M., Ikezawa H. Eur. J. Biochem. 175:213-220(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 166-283. Strain: IAM 1208.
[4]	"Some characteristics of phospholipase C from Bacillus cereus." Otnaess A.-B., Little C., Sletten K., Wallin R., Johnsen S., Flengsrud R., Prydz H. Eur. J. Biochem. 79:459-468(1977) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 39-65.
[5]	"Kinetics of the hydrolysis of monodispersed and micellar phosphatidylcholines catalyzed by a phospholipase C from Bacillus cereus." Ikeda K., Inoue S., Amasaki C., Teshima K., Ikezawa H. J. Biochem. 110:88-95(1991) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 39-49. Strain: IAM 1208.
[6]	"High-resolution (1.5 A) crystal structure of phospholipase C from Bacillus cereus." Hough E., Hansen L.K., Birknes B., Jynge K., Hansen S., Hordvik A., Little C., Dodson E., Derewenda Z. Nature 338:357-360(1989) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X64141 Genomic DNA. Translation: CAA45502.1.
X12854 Genomic DNA. Translation: CAA31332.1.
X12711 Genomic DNA. Translation: CAA31213.1.
X64140 Genomic DNA. Translation: CAA45501.1. Different termination.

PIR

PS0197. S18978.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AH7	X-ray	1.50	A	39-283	[»]
1P5X	X-ray	2.00	A	39-283	[»]
1P6D	X-ray	2.00	A	39-283	[»]
1P6E	X-ray	2.30	A	39-283	[»]
2FFZ	X-ray	2.05	A	39-283	[»]
2FGN	X-ray	2.04	A	39-283	[»]
2HUC	X-ray	1.90	A	39-283	[»]

ProteinModelPortal

P09598.

SMR

P09598. Positions 39-283.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Enzyme and pathway databases

SABIO-RK

P09598.

Family and domain databases

Gene3D

1.10.575.10. 1 hit.

InterPro

IPR008947. PLipase_C/P1_nuclease.
IPR001531. PLipaseC_domain.
[Graphical view]

PRINTS

PR00479. PRPHPHLPASEC.

ProDom

PD003946. PLipaseC_Zn-bd_prok. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00770. Zn_dep_PLPC. 1 hit.
[Graphical view]

SUPFAM

SSF48537. PLC_Nuclease. 1 hit.

PROSITE

PS00384. PROKAR_ZN_DEPEND_PLPC_1. 1 hit.
PS51346. PROKAR_ZN_DEPEND_PLPC_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P09598.

ChEMBL

CHEMBL1293202.

EvolutionaryTrace

P09598.

Entry information

Entry name

PHLC_BACCE

Accession

Primary (citable) accession number: P09598

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	July 1, 1989
Last modified:	April 3, 2013
This is version 97 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program