P14262 (PLC_BACCE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: 1-phosphatidylinositol phosphodiesterase EC=4.6.1.13 Alternative name(s): Phosphatidylinositol diacylglycerol-lyase Phosphatidylinositol-specific phospholipase C Short name=PI-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	329 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	Cleaves glycosylphosphatidylinositol (GPI) and phosphatidylinositol (PI) anchors but not PI phosphates.
Catalytic activity	1-phosphatidyl-1D-myo-inositol = 1D-myo-inositol 1,2-cyclic phosphate + 1,2-diacyl-sn-glycerol.
Subcellular location	Secreted.
Sequence similarities	Contains 1 PI-PLC X-box domain.

Ontologies

Keywords
Biological process	Lipid degradation Lipid metabolism
Cellular component	Secreted
Domain	Signal
Molecular function	Lyase
Technical term	3D-structure
Gene Ontology (GO)
Biological_process	lipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	phosphatidylinositol diacylglycerol-lyase activity Inferred from electronic annotation. Source: EC phosphoric diester hydrolase activity 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 – 31

31

Chain

32 – 329

298

1-phosphatidylinositol phosphodiesterase

PRO_0000024294

Regions

Domain

53 – 194

142

PI-PLC X-box

Sites

Active site

63

1

Proton acceptor

Active site

113

1

Proton donor

Secondary structure

1

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329

Helix Strand Turn

Details...

Helix

35 – 39

5

Helix

41 – 43

3

Turn

44 – 47

4

Turn

54 – 56

3

Beta strand

59 – 62

4

Helix

65 – 67

3

Helix

73 – 79

7

Helix

86 – 90

5

Turn

91 – 93

3

Beta strand

96 – 103

8

Beta strand

109 – 113

5

Beta strand

116 – 121

6

Helix

122 – 135

14

Beta strand

141 – 147

7

Helix

159 – 166

8

Turn

167 – 169

3

Beta strand

170 – 173

4

Helix

182 – 185

4

Beta strand

188 – 194

7

Beta strand

211 – 218

8

Beta strand

220 – 222

3

Beta strand

224 – 228

5

Helix

235 – 250

16

Turn

251 – 254

4

Beta strand

258 – 263

6

Beta strand

271 – 275

5

Helix

276 – 294

19

Beta strand

301 – 305

5

Beta strand

311 – 313

3

Helix

315 – 321

7

Helix

322 – 326

5

Sequences

	Sequence		Length	Mass (Da)
	P14262 [UniParc]. Last modified January 1, 1990. Version 1. Checksum: 0D731F5604135CB4	FASTA	329	38,109
	10 20 30 40 50 60 MSNKKLILKL FICSTIFITF VFALHDKRVV AASSVNELEN WSKWMQPIPD SIPLARISIP 70 80 90 100 110 120 GTHDSGTFKL QNPIKQVWGM TQEYDFRYQM DHGARIFDIR GRLTDDNTIV LHHGPLYLYV 130 140 150 160 170 180 TLHEFINEAK QFLKDNPSET IIMSLKKEYE DMKGAEDSFS STFEKKYFVD PIFLKTEGNI 190 200 210 220 230 240 KLGDARGKIV LLKRYSGSNE PGGYNNFYWP DNETFTTTVN QNANVTVQDK YKVSYDEKVK 250 260 270 280 290 300 SIKDTMDETM NNSEDLNHLY INFTSLSSGG TAWNSPYYYA SYINPEIANY IKQKNPARVG 310 320 WVIQDYINEK WSPLLYQEVI RANKSLIKE

References

[1]	"Phosphatidylinositol-specific phospholipase C of Bacillus cereus: cloning, sequencing, and relationship to other phospholipases." Kuppe A., Evans L.M., McMillen D.A., Griffith O.H. J. Bacteriol. 171:6077-6083(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Crystal structure of the phosphatidylinositol-specific phospholipase C from Bacillus cereus in complex with myo-inositol." Heinz D.W., Ryan M., Bullock T.L., Griffith O.H. EMBO J. 14:3855-3863(1995) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
[3]	"Crystal structure of phosphatidylinositol-specific phospholipase C from Bacillus cereus in complex with glucosaminyl(alpha 1-->6)-D-myo-inositol, an essential fragment of GPI anchors." Heinz D.W., Ryan M., Smith M.P., Weaver L.H., Keana J.F., Griffith O.H. Biochemistry 35:9496-9504(1996) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
[4]	"Probing the roles of active site residues in phosphatidylinositol-specific phospholipase C from Bacillus cereus by site-directed mutagenesis." Gassler C.S., Ryan M., Liu T., Griffith O.H., Heinz D.W. Biochemistry 36:12802-12813(1997) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M30809 Genomic DNA. Translation: AAA22665.1.

PIR

A33493.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1GYM	X-ray	2.20	A	32-329	[»]
1PTD	X-ray	2.60	A	32-329	[»]
1PTG	X-ray	2.60	A	32-329	[»]
2PTD	X-ray	2.00	A	32-329	[»]
3PTD	X-ray	2.20	A	32-329	[»]
4PTD	X-ray	2.30	A	32-329	[»]
5PTD	X-ray	2.70	A	32-329	[»]
6PTD	X-ray	2.60	A	32-329	[»]
7PTD	X-ray	2.60	A	32-329	[»]

ProteinModelPortal

P14262.

SMR

P14262. Positions 32-327.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Enzyme and pathway databases

BioCyc

MetaCyc:MONOMER-15192.

Family and domain databases

Gene3D

3.20.20.190. 1 hit.

InterPro

IPR017946. PLC-like_Pdiesterase_TIM-brl.
IPR000909. PLipase_C_PInositol-sp_X_dom.
[Graphical view]

Pfam

PF00388. PI-PLC-X. 1 hit.
[Graphical view]

SMART

SM00148. PLCXc. 1 hit.
[Graphical view]

SUPFAM

SSF51695. PLC-like_Pdiesterase_TIM-brl. 1 hit.

PROSITE

PS50007. PIPLC_X_DOMAIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P14262.

Entry information

Entry name

PLC_BACCE

Accession

Primary (citable) accession number: P14262

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	January 1, 1990
Last modified:	April 3, 2013
This is version 82 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program