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P81054

- PLMP_GRIFR

UniProt

P81054 - PLMP_GRIFR

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Protein
Peptidyl-Lys metalloendopeptidase
Gene
MEP
Organism
Grifola frondosa (Maitake) (Polyporus frondosus)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

Preferential cleavage in proteins: -Xaa-|-Lys-(in which Xaa may be Pro).

Cofactori

Binds 1 zinc ion per subunit.

Enzyme regulationi

Inhibited by chelating agents such as EDTA and 1,10-phenanthroline.1 Publication

pH dependencei

Optimum pH is 9.5. Active from pH 6 to pH 10.5. Stable from pH 5 to pH 10.1 Publication

Temperature dependencei

Thermostable for 3 hours up to 80 degrees Celsius.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi298 – 2981Zinc; catalytic
Active sitei299 – 2991 By similarity
Metal bindingi302 – 3021Zinc; catalytic
Metal bindingi311 – 3111Zinc; catalytic
Sitei314 – 3141Transition state stabilizer Inferred

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. metalloendopeptidase activity Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.4.24.20. 2512.

Protein family/group databases

MEROPSiM35.004.

Names & Taxonomyi

Protein namesi
Recommended name:
Peptidyl-Lys metalloendopeptidase (EC:3.4.24.20)
Short name:
MEP
Alternative name(s):
GfMEP
Gene namesi
Name:MEP
OrganismiGrifola frondosa (Maitake) (Polyporus frondosus)
Taxonomic identifieri5627 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesAgaricomycetidaeAgaricalesSchizophyllaceaeGrifola

Subcellular locationi

Secreted Inferred
Note: Binds strongly to beta-1,3-glucan and chitin, major polysaccharides constituting the fungal cell wall.

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 – 18181 Publication
Add
BLAST
Propeptidei19 – 181163
PRO_0000043399Add
BLAST
Chaini182 – 348167Peptidyl-Lys metalloendopeptidase
PRO_0000043400Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi186 ↔ 256
Glycosylationi223 – 2231O-linked (Man); partial
Disulfide bondi258 ↔ 278

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi183 – 1853
Helixi188 – 21427
Helixi220 – 2267
Helixi231 – 24515
Helixi249 – 2513
Beta strandi253 – 2553
Beta strandi274 – 2774
Helixi279 – 2835
Beta strandi286 – 2883
Helixi292 – 30211
Helixi304 – 3063
Helixi315 – 32511
Helixi327 – 3304
Helixi334 – 3429

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1G12X-ray1.60A182-348[»]
1GE5X-ray2.00A182-348[»]
1GE6X-ray2.20A182-348[»]
1GE7X-ray2.00A/B182-348[»]
ProteinModelPortaliP81054.
SMRiP81054. Positions 182-348.

Miscellaneous databases

EvolutionaryTraceiP81054.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi193 – 2019Poly-Ala

Sequence similaritiesi

Belongs to the peptidase M35 family.

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.40.390.10. 1 hit.
InterProiIPR029463. Lys_MEP.
IPR024079. MetalloPept_cat_dom.
[Graphical view]
PfamiPF14521. Aspzincin_M35. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P81054-1 [UniParc]FASTAAdd to Basket

« Hide

MFSSVMVALV SLAVAVSANP GLSLKVSGPE AVDGVNNLKV VTTITNTGDE    50
TLKLLNDPRG ALHTMPTDTF AITNESGETP SFIGVKVKYV PSMAAKSTGE 100
NVFAVIAPGQ SVNVEHDLSA AYNFTSSGAG TYALEALNVF NYIDPETNEP 150
VEIWADAEAH TTAVSGKLAV VRATPTLTRP VTYNGCSSSE QSALAAAASA 200
AQSYVAESLS YLQTHTAATP RYTTWFGSYI SSRHSTVLQH YTDMNSNDFS 250
SYSFDCTCTA AGTFAYVYPN RFGTVYLCGA FWKAPTTGTD SQAGTLVHES 300
SHFTRNGGTK DYAYGQAAAK SLATMDPDKA VMNADNHEYF SENNPAQS 348
Length:348
Mass (Da):36,879
Last modified:December 6, 2005 - v2
Checksum:i5F3859F10B423C79
GO

Mass spectrometryi

Molecular mass is 18028 Da from positions 182 - 348. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB076805 mRNA. Translation: BAB82381.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB076805 mRNA. Translation: BAB82381.1 .

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1G12 X-ray 1.60 A 182-348 [» ]
1GE5 X-ray 2.00 A 182-348 [» ]
1GE6 X-ray 2.20 A 182-348 [» ]
1GE7 X-ray 2.00 A/B 182-348 [» ]
ProteinModelPortali P81054.
SMRi P81054. Positions 182-348.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi M35.004.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

BRENDAi 3.4.24.20. 2512.

Miscellaneous databases

EvolutionaryTracei P81054.

Family and domain databases

Gene3Di 3.40.390.10. 1 hit.
InterProi IPR029463. Lys_MEP.
IPR024079. MetalloPept_cat_dom.
[Graphical view ]
Pfami PF14521. Aspzincin_M35. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "PCR cloning and heterologous expression of cDNA encoding a peptidyl-Lys metalloendopeptidase precursor of Grifola frondosa."
    Saito T., Dohmae N., Tsujimoto M., Takio K.
    J. Gen. Appl. Microbiol. 48:287-292(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 19-28; 96-105 AND 167-178.
    Strain: S.F. Gray.
  2. "Amino acid sequences of metalloendopeptidases specific for acyl-lysine bonds from Grifola frondosa and Pleurotus ostreatus fruiting bodies."
    Nonaka T., Dohmae N., Hashimoto Y., Takio K.
    J. Biol. Chem. 272:30032-30039(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 182-348, MASS SPECTROMETRY.
  3. "Characterization of a thermostable lysine-specific metalloendopeptidase from the fruiting bodies of a basidiomycete, Grifola frondosa."
    Nonaka T., Ishikawa H., Tsumuraya Y., Hashimoto Y., Dohmae N., Takio K.
    J. Biochem. 118:1014-1020(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 182-196, BIOPHYSICOCHEMICAL PROPERTIES, ZINC-BINDING, ENZYME REGULATION, BINDING TO BETA-GLUCANS AND CHITIN.
  4. "Kinetic characterization of lysine-specific metalloendopeptidases from Grifola frondosa and Pleurotus ostreatus fruiting bodies."
    Nonaka T., Hashimoto Y., Takio K.
    J. Biochem. 124:157-162(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBSTRATE SPECIFICITY.
  5. "Structure of a new 'aspzincin' metalloendopeptidase from Grifola frondosa: implications for the catalytic mechanism and substrate specificity based on several different crystal forms."
    Hori T., Kumasaka T., Yamamoto M., Nonaka N., Tanaka N., Hashimoto Y., Ueki U., Takio K.
    Acta Crystallogr. D 57:361-368(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF MATURE FORM.

Entry informationi

Entry nameiPLMP_GRIFR
AccessioniPrimary (citable) accession number: P81054
Secondary accession number(s): Q8WZH2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: December 6, 2005
Last modified: September 3, 2014
This is version 84 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal 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. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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