P34024 (PLC_LISMO) 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

Gene names

Name:	plcA
Synonyms:	pic
Ordered Locus Names:	lmo0201

Organism

Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e) [Reference proteome] [HAMAP]

Taxonomic identifier

169963 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Listeriaceae › Listeria › Listeria monocytogenes

Protein attributes

Sequence length	317 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. Important factor in pathogenesis, PI-PLC activity is present only in virulent listeria species. It may participate in the lysis of the phagolysosomal membrane.
Catalytic activity	1-phosphatidyl-1D-myo-inositol = 1D-myo-inositol 1,2-cyclic phosphate + 1,2-diacyl-sn-glycerol.
Subunit structure	Monomer.
Subcellular location	Secreted. Cytoplasm. Note: Secreted and, to a lesser extent, cytoplasmic.
Sequence similarities	Contains 1 PI-PLC X-box domain.

Ontologies

Keywords
Biological process	Lipid degradation Lipid metabolism Virulence
Cellular component	Cytoplasm Secreted
Domain	Signal
Molecular function	Lyase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	lipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW pathogenesis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell 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 – 22

22

Potential

Chain

23 – 317

295

1-phosphatidylinositol phosphodiesterase

PRO_0000024296

Regions

Domain

58 – 196

139

PI-PLC X-box

Sites

Active site

67

1

Proton acceptor

Active site

115

1

Proton donor

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

317

Helix Strand Turn

Details...

Helix

45 – 47

3

Helix

49 – 51

3

Helix

58 – 60

3

Beta strand

61 – 66

6

Turn

67 – 72

6

Helix

76 – 80

5

Helix

82 – 85

4

Helix

92 – 97

6

Beta strand

102 – 107

6

Beta strand

111 – 115

5

Beta strand

118 – 123

6

Helix

124 – 137

14

Beta strand

143 – 149

7

Helix

156 – 167

12

Helix

168 – 171

4

Beta strand

174 – 178

5

Turn

187 – 192

6

Beta strand

194 – 200

7

Beta strand

206 – 208

3

Beta strand

211 – 216

6

Beta strand

222 – 225

4

Helix

233 – 249

17

Beta strand

251 – 258

8

Beta strand

264 – 266

3

Helix

268 – 288

21

Beta strand

295 – 301

7

Helix

304 – 311

8

Sequences

	Sequence		Length	Mass (Da)
	P34024 [UniParc]. Last modified February 1, 1994. Version 1. Checksum: 5D0E33649A983DA2	FASTA	317	36,318
	10 20 30 40 50 60 MYKNYLQRTL VLLLCFILYF FTFPLGGKAY SLNNWNKPIK NSVTTKQWMS ALPDTTNLAA 70 80 90 100 110 120 LSIPGTHDTM SYNGDITWTL TKPLAQTQTM SLYQQLEAGI RYIDIRAKDN LNIYHGPIFL 130 140 150 160 170 180 NASLSGVLET ITQFLKKNPK ETIIMRLKDE QNSNDSFDYR IQPLINIYKD YFYTTPRTDT 190 200 210 220 230 240 SNKIPTLKDV RGKILLLSEN HTKKPLVINS RKFGMQFGAP NQVIQDDYNG PSVKTKFKEI 250 260 270 280 290 300 VQTAYQASKA DNKLFLNHIS ATSLTFTPRQ YAAALNNKVE QFVLNLTSEK VRGLGILIMD 310 FPEKQTIKNI IKNNKFN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of phosphatidylinositol-specific phospholipase C activity in Listeria monocytogenes: a novel type of virulence factor?" Mengaud J., Braun-Breton C., Cossart P. Mol. Microbiol. 5:367-372(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: LO28 / Serovar 1/2c.
[2]	"Detection of a gene encoding a phosphatidylinositol-specific phospholipase C that is co-ordinately expressed with listeriolysin in Listeria monocytogenes." Leimeister-Waechter M., Domann E., Chakraborty T. Mol. Microbiol. 5:361-366(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: EGD / Serovar 1/2a.
[3]	"Comparative genomics of Listeria species." Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F., Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A., Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E., Dominguez-Bernal G., Duchaud E. , Durant L., Dussurget O., Entian K.-D., Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W., Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U., Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A., Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B., Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N., Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P. Science 294:849-852(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-679 / EGD-e.
[4]	"Transcriptional mapping and nucleotide sequence of the Listeria monocytogenes hlyA region reveal structural features that may be involved in regulation." Mengaud J., Vicente M.-F., Cossart P. Infect. Immun. 57:3695-3701(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 70-317.
[5]	"Crystal structure of the phosphatidylinositol-specific phospholipase C from the human pathogen Listeria monocytogenes." Moser J., Gerstel B., Meyer J.E., Chakraborty T., Wehland J., Heinz D.W. J. Mol. Biol. 273:269-282(1997) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 43-317. Strain: EGD / Serovar 1/2a.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X54618 Genomic DNA. Translation: CAA38438.1.
AL591974 Genomic DNA. Translation: CAD00728.1.

PIR

AB1100.
A37204. S15336.

RefSeq

NP_463732.1. NC_003210.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AOD	X-ray	2.60	A	29-317	[»]
2PLC	X-ray	2.00	A	43-316	[»]

ProteinModelPortal

P34024.

SMR

P34024. Positions 43-316.

ModBase

Search...

Protein-protein interaction databases

STRING

169963.lmo0201.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

CAD00728; CAD00728; CAD00728.

GeneID

987032.

KEGG

lmo:lmo0201.

PATRIC

20309409. VBILisMon69206_0206.

Organism-specific databases

GenoList

LMO0201.

Phylogenomic databases

eggNOG

NOG14688.

KO

K01771.

OMA

MRVKEEY.

ProtClustDB

CLSK536910.

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

P34024.

Entry information

Entry name

PLC_LISMO

Accession

Primary (citable) accession number: P34024

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	February 1, 1994
Last modified:	May 1, 2013
This is version 107 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program