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P14262

- PLC_BACCE

UniProt

P14262 - PLC_BACCE

Protein

1-phosphatidylinositol phosphodiesterase

Gene
N/A
Organism
Bacillus cereus
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 84 (01 Oct 2014)
      Sequence version 1 (01 Jan 1990)
      Previous versions | rss
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    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

    GO - Biological processi

    1. lipid catabolic process Source: UniProtKB-KW

    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

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3131Add
    BLAST
    Chaini32 – 3292981-phosphatidylinositol phosphodiesterasePRO_0000024294Add
    BLAST

    Structurei

    Secondary structure

    1
    329
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP14262.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini53 – 194142PI-PLC X-boxPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 PI-PLC X-box domain.PROSITE-ProRule annotation

    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

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    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...
    MobiDBi 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 1, 2014
    This is version 84 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