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P09598

- PHLC_BACCE

UniProt

P09598 - PHLC_BACCE

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Protein
Phospholipase C
Gene
plc
Organism
Bacillus cereus
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Required, with sphingomyelinase, to effect target cell lysis (hemolysis).

Catalytic activityi

A phosphatidylcholine + H2O = 1,2-diacyl-sn-glycerol + phosphocholine.

Cofactori

Binds 3 zinc ions per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi39 – 391Zinc 3
Metal bindingi52 – 521Zinc 3
Metal bindingi93 – 931Zinc 1
Metal bindingi107 – 1071Zinc 1
Metal bindingi156 – 1561Zinc 1
Metal bindingi160 – 1601Zinc 1
Metal bindingi160 – 1601Zinc 3
Metal bindingi166 – 1661Zinc 2
Metal bindingi180 – 1801Zinc 2
Metal bindingi184 – 1841Zinc 2

GO - Molecular functioni

  1. phosphatidylcholine phospholipase C activity Source: UniProtKB-EC
  2. zinc ion binding Source: InterPro
Complete GO annotation...

GO - Biological processi

  1. hemolysis in other organism Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Cytolysis, Hemolysis

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

SABIO-RKP09598.

Names & Taxonomyi

Protein namesi
Recommended name:
Phospholipase C (EC:3.1.4.3)
Short name:
PLC
Alternative name(s):
Cereolysin A
Phosphatidylcholine cholinephosphohydrolase
Gene namesi
Name:plc
OrganismiBacillus cereus
Taxonomic identifieri1396 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424 Reviewed prediction
Add
BLAST
Propeptidei25 – 3814
PRO_0000023927Add
BLAST
Chaini39 – 283245Phospholipase C
PRO_0000023928Add
BLAST

Keywords - PTMi

Zymogen

Interactioni

Subunit structurei

Monomer.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi43 – 453
Helixi47 – 493
Helixi51 – 6515
Helixi72 – 809
Helixi82 – 9110
Turni92 – 943
Turni96 – 1038
Helixi105 – 1073
Turni111 – 1133
Helixi124 – 14017
Helixi144 – 16118
Turni164 – 1696
Beta strandi174 – 1763
Helixi179 – 19012
Helixi191 – 1944
Helixi210 – 22314
Helixi225 – 2273
Helixi231 – 24010
Helixi244 – 28037

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AH7X-ray1.50A39-283[»]
1P5XX-ray2.00A39-283[»]
1P6DX-ray2.00A39-283[»]
1P6EX-ray2.30A39-283[»]
2FFZX-ray2.05A39-283[»]
2FGNX-ray2.04A39-283[»]
2HUCX-ray1.90A39-283[»]
ProteinModelPortaliP09598.
SMRiP09598. Positions 39-283.

Miscellaneous databases

EvolutionaryTraceiP09598.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini39 – 283245Zn-dependent PLC
Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Signal

Family and domain databases

Gene3Di1.10.575.10. 1 hit.
InterProiIPR008947. PLipase_C/P1_nuclease.
IPR001531. PLipaseC_domain.
IPR029002. PLPC/GPLD1.
[Graphical view]
PfamiPF00882. Zn_dep_PLPC. 1 hit.
[Graphical view]
PRINTSiPR00479. PRPHPHLPASEC.
ProDomiPD003946. PLipaseC_Zn-bd_prok. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00770. Zn_dep_PLPC. 1 hit.
[Graphical view]
SUPFAMiSSF48537. SSF48537. 1 hit.
PROSITEiPS00384. PROKAR_ZN_DEPEND_PLPC_1. 1 hit.
PS51346. PROKAR_ZN_DEPEND_PLPC_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P09598-1 [UniParc]FASTAAdd to Basket

« Hide

MKKKVLALAA AITVVAPLQS VAFAHENDGG SKIKIVHRWS AEDKHKEGVN    50
SHLWIVNRAI DIMSRNTTLV KQDRVAQLNE WRTELENGIY AADYENPYYD 100
NSTFASHFYD PDNGKTYIPF AKQAKETGAK YFKLAGESYK NKDMKQAFFY 150
LGLSLHYLGD VNQPMHAANF TNLSYPQGFH SKYENFVDTI KDNYKVTDGN 200
GYWNWKGTNP EEWIHGAAVV AKQDYSGIVN DNTKDWFVKA AVSQEYADKW 250
RAEVTPMTGK RLMDAQRVTA GYIQLWFDTY GDR 283
Length:283
Mass (Da):32,383
Last modified:July 1, 1989 - v1
Checksum:iAC5452EFF2E22B19
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti212 – 2121E → D in strain: IAM 1208.
Natural varianti226 – 2261S → A in strain: IAM 1208.
Natural varianti239 – 2391K → R in strain: IAM 1208.
Natural varianti282 – 2821D → N in strain: IAM 1208.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRiS18978. PS0197.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRi S18978. PS0197.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali P09598.
SMRi P09598. Positions 39-283.
ModBasei Search...

Chemistry

BindingDBi P09598.
ChEMBLi CHEMBL1293202.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

SABIO-RK P09598.

Miscellaneous databases

EvolutionaryTracei P09598.

Family and domain databases

Gene3Di 1.10.575.10. 1 hit.
InterProi IPR008947. PLipase_C/P1_nuclease.
IPR001531. PLipaseC_domain.
IPR029002. PLPC/GPLD1.
[Graphical view ]
Pfami PF00882. Zn_dep_PLPC. 1 hit.
[Graphical view ]
PRINTSi PR00479. PRPHPHLPASEC.
ProDomi PD003946. PLipaseC_Zn-bd_prok. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SMARTi SM00770. Zn_dep_PLPC. 1 hit.
[Graphical view ]
SUPFAMi SSF48537. SSF48537. 1 hit.
PROSITEi PS00384. PROKAR_ZN_DEPEND_PLPC_1. 1 hit.
PS51346. PROKAR_ZN_DEPEND_PLPC_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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. 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).

Entry informationi

Entry nameiPHLC_BACCE
AccessioniPrimary (citable) accession number: P09598
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: June 11, 2014
This is version 102 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, Direct protein sequencing

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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