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P14262

- PLC_BACCE

UniProt

P14262 - PLC_BACCE

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Protein
1-phosphatidylinositol phosphodiesterase
Gene
N/A
Organism
Bacillus cereus
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Cleaves glycosylphosphatidylinositol (GPI) and phosphatidylinositol (PI) anchors but not PI phosphates.

Catalytic activityi

1-phosphatidyl-1D-myo-inositol = 1D-myo-inositol 1,2-cyclic phosphate + 1,2-diacyl-sn-glycerol.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei63 – 631Proton acceptor
Active sitei113 – 1131Proton donor

GO - Molecular functioni

  1. phosphatidylinositol diacylglycerol-lyase activity Source: UniProtKB-EC
  2. phosphoric diester hydrolase activity Source: InterPro
Complete GO annotation...

GO - Biological processi

  1. lipid catabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-15192.

Names & Taxonomyi

Protein namesi
Recommended name:
1-phosphatidylinositol phosphodiesterase (EC:4.6.1.13)
Alternative name(s):
Phosphatidylinositol diacylglycerol-lyase
Phosphatidylinositol-specific phospholipase C
Short name:
PI-PLC
OrganismiBacillus cereus
Taxonomic identifieri1396 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3131
Add
BLAST
Chaini32 – 3292981-phosphatidylinositol phosphodiesterase
PRO_0000024294Add
BLAST

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi35 – 395
Helixi41 – 433
Turni44 – 474
Turni54 – 563
Beta strandi59 – 624
Helixi65 – 673
Helixi73 – 797
Helixi86 – 905
Turni91 – 933
Beta strandi96 – 1038
Beta strandi109 – 1135
Beta strandi116 – 1216
Helixi122 – 13514
Beta strandi141 – 1477
Helixi159 – 1668
Turni167 – 1693
Beta strandi170 – 1734
Helixi182 – 1854
Beta strandi188 – 1947
Beta strandi211 – 2188
Beta strandi220 – 2223
Beta strandi224 – 2285
Helixi235 – 25016
Turni251 – 2544
Beta strandi258 – 2636
Beta strandi271 – 2755
Helixi276 – 29419
Beta strandi301 – 3055
Beta strandi311 – 3133
Helixi315 – 3217
Helixi322 – 3265

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GYMX-ray2.20A32-329[»]
1PTDX-ray2.60A32-329[»]
1PTGX-ray2.60A32-329[»]
2PTDX-ray2.00A32-329[»]
3PTDX-ray2.20A32-329[»]
4PTDX-ray2.30A32-329[»]
5PTDX-ray2.70A32-329[»]
6PTDX-ray2.60A32-329[»]
7PTDX-ray2.60A32-329[»]
ProteinModelPortaliP14262.
SMRiP14262. Positions 32-327.

Miscellaneous databases

EvolutionaryTraceiP14262.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini53 – 194142PI-PLC X-box
Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.20.20.190. 1 hit.
InterProiIPR017946. PLC-like_Pdiesterase_TIM-brl.
IPR000909. PLipase_C_PInositol-sp_X_dom.
[Graphical view]
PfamiPF00388. PI-PLC-X. 1 hit.
[Graphical view]
SMARTiSM00148. PLCXc. 1 hit.
[Graphical view]
SUPFAMiSSF51695. SSF51695. 1 hit.
PROSITEiPS50007. PIPLC_X_DOMAIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P14262-1 [UniParc]FASTAAdd to Basket

« Hide

MSNKKLILKL FICSTIFITF VFALHDKRVV AASSVNELEN WSKWMQPIPD    50
SIPLARISIP GTHDSGTFKL QNPIKQVWGM TQEYDFRYQM DHGARIFDIR 100
GRLTDDNTIV LHHGPLYLYV TLHEFINEAK QFLKDNPSET IIMSLKKEYE 150
DMKGAEDSFS STFEKKYFVD PIFLKTEGNI KLGDARGKIV LLKRYSGSNE 200
PGGYNNFYWP DNETFTTTVN QNANVTVQDK YKVSYDEKVK SIKDTMDETM 250
NNSEDLNHLY INFTSLSSGG TAWNSPYYYA SYINPEIANY IKQKNPARVG 300
WVIQDYINEK WSPLLYQEVI RANKSLIKE 329
Length:329
Mass (Da):38,109
Last modified:January 1, 1990 - v1
Checksum:i0D731F5604135CB4
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M30809 Genomic DNA. Translation: AAA22665.1.
PIRiA33493.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M30809 Genomic DNA. Translation: AAA22665.1 .
PIRi A33493.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali P14262.
SMRi P14262. Positions 32-327.
ModBasei Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

BioCyci MetaCyc:MONOMER-15192.

Miscellaneous databases

EvolutionaryTracei P14262.

Family and domain databases

Gene3Di 3.20.20.190. 1 hit.
InterProi IPR017946. PLC-like_Pdiesterase_TIM-brl.
IPR000909. PLipase_C_PInositol-sp_X_dom.
[Graphical view ]
Pfami PF00388. PI-PLC-X. 1 hit.
[Graphical view ]
SMARTi SM00148. PLCXc. 1 hit.
[Graphical view ]
SUPFAMi SSF51695. SSF51695. 1 hit.
PROSITEi PS50007. PIPLC_X_DOMAIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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).

Entry informationi

Entry nameiPLC_BACCE
AccessioniPrimary (citable) accession number: P14262
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: October 16, 2013
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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