Reviewed, UniProtKB/Swiss-Prot Q9Y7F7 (PLMP_ARMME)

Names and origin

Protein names

Recommended name:
    Peptidyl-Lys metalloendopeptidase
      Short name=MEP
    EC=3.4.24.20
Alternative name(s):
    AmMEP

Gene names

Name:

MEP

Organism

Armillaria mellea (Shoestring root rot fungus) (Honey mushroom)

Taxonomic identifier

47429 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Basidiomycota › Agaricomycotina › Homobasidiomycetes › Agaricomycetidae › Agaricales › Tricholomataceae › Armillaria

Protein attributes

Sequence length	351 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)

Catalytic activity	Preferential cleavage in proteins: -Xaa-|-Lys-(in which Xaa may be Pro).
Cofactor	Binds 1 zinc ion per subunit.
Enzyme regulation	Inhibited by chelating agents such as imidazole, alpha,alpha'-bipyridine, and 1,10-phenanthroline. Ref.3
Subcellular location	Secreted By similarity. Note: Binds strongly to beta-1,3-glucan and chitin, major polysaccharides constituting the fungal cell wall By similarity.
Sequence similarities	Belongs to the peptidase M35 family.
biophysicochemical properties	pH dependence: Optimum pH is 7-7.5. Active from pH 5.25 to pH 9.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Ligand	Metal-binding Zinc
Molecular function	Hydrolase Metalloprotease Protease
PTM	Cleavage on pair of basic residues Disulfide bond Zymogen
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: InterPro
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	metalloendopeptidase activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 22	22	Potential
	Propeptide	23 – 183	161	Potential		PRO_0000043401
	Chain	184 – 351	168	Peptidyl-Lys metalloendopeptidase		PRO_0000043402
Sites
	Active site	302	1	By similarity
	Metal binding	301	1	Zinc; catalytic By similarity
	Metal binding	305	1	Zinc; catalytic By similarity
	Metal binding	314	1	Zinc; catalytic By similarity
	Site	317	1	Transition state stabilizer By similarity
Amino acid modifications
	Disulfide bond	189 ↔ 259		By similarity
	Disulfide bond	261 ↔ 281		By similarity
Experimental info
	Sequence conflict	189	1	C → W AA sequence Ref.2
	Sequence conflict	204	1	A → W AA sequence Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q9Y7F7-1 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: 396F2999FFD06833	FASTA	351	37,551
	10 20 30 40 50 60 MFSLSSRFFL YSLCLSAVAV SAAPGLSLSL SGADSVVDVE NLNVAATLTN TGDTTLKILN 70 80 90 100 110 120 DPSSILSSKF ATHTFDISSD NGSPAFTGVK VKYDPNYVVK KNADSSFTVL APGESVTVNH 130 140 150 160 170 180 ALGAAYNFTG SGAASYSIEP SSLFYYVDPD TNELASINAD TQQHTTKISG TLAVARRSNL 190 200 210 220 230 240 GKRISYNGCT SSRQTTLVSA AAAAQTYAQS SYNYLSSHTA STTRYVTWFG PYTSARHSTV 250 260 270 280 290 300 LSCFSNMLAY PYANYEYDCT CTESDVYAYV YPSQFGTIYL CGAFWQTTTT GTDSRGGTLI 310 320 330 340 350 HESSHFTIIC GTQDYAYGQS AAKSLASSNP SEAIKNADNY EYFAENNPAQ S

References

[1]	"Cloning and expression of an Armillaria mellea metalloendopeptidase." Vad K., Thim L. Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The lysine-specific proteinase from Armillaria mellea is a member of a novel class of metalloendopeptidases located in Basidiomycetes." Healy V., O'Connell J., McCarthy T.V., Doonan S. Biochem. Biophys. Res. Commun. 262:60-63(1999) [PubMed: 10448068] [Abstract] Cited for: PROTEIN SEQUENCE OF 184-209.
[3]	"Specificity and inhibition studies of Armillaria mellea protease." Lewis W.G., Basford J.M., Walton P.L. Biochim. Biophys. Acta 522:551-560(1978) [PubMed: 23849] [Abstract] Cited for: BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, ENZYME REGULATION, ZINC-BINDING.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AJ238718 Genomic DNA. Translation: CAB42792.1.
3D structure databases
HSSP	HSSP built from PDB template 1G12 based on UniProtKB P81054.
ModBase	Search...
Protein family/group databases
MEROPS	M35.004.
Enzyme and pathway databases
BRENDA	3.4.24.20. 19000.
Family and domain databases
InterPro	IPR006025. Pept_M_Zn_BS. IPR001384. Peptidase_M35. [Graphical view]
Pfam	PF02102. Peptidase_M35. 1 hit. [Graphical view]
PROSITE	PS00142. ZINC_PROTEASE. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PLMP_ARMME

Accession

Primary (citable) accession number: Q9Y7F7

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 6, 2005
Last sequence update:	November 1, 1999
Last modified:	June 16, 2009
This is version 36 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)