Summary for peptidase S16.001: Lon-A peptidase

Summary Alignment Tree Sequences Sequence features Distribution Structure Literature Substrates Inhibitors

 

Names
MEROPS NameLon-A peptidase
Other namesATP-dependent serine proteinase, endopeptidase La, BsgA protease (Myxococcus xanthus), EcLon peptidase (Escherichia coli), Lon g.p. (Escherichia coli), Lon protease, Lon peptidase (type 1)
Domain architecture
MEROPS Classification
Classification Clan SJ >> Subclan (none) >> Family S16 >> Subfamily (none) >> S16.001
HolotypeLon-A peptidase (Escherichia coli), Uniprot accession P0A9M0 (peptidase unit: 537-784), MERNUM MER0000485
History Identifier created: Handbook of Proteolytic Enzymes (1998) Academic Press, London.
Activity
Catalytic typeSerine
PeplistIncluded in the Peplist with identifier PL00384
NC-IUBMBSubclass 3.4 (Peptidases) >> Sub-subclass 3.4.21 (Serine endopeptidases) >> Peptidase 3.4.21.53
EnzymologyBRENDA database
Proteolytic eventsCutDB database (6 cleavages)
PhysiologyThought to contribute to elimination of damaged proteins in heat shock.
Pharmaceutical relevanceContributes to the virulence of Salmonella enterica serovar typhimurium in mice (Takaya et al., 2003).
Cleavage site specificity Explanations of how to interpret the following cleavage site sequence logo and specificity matrix can be found here.
Cleavage pattern-/-/-/lafScissile bonds/-/-/- (based on 21 cleavages)
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Specificity matrix
 
Amino acid P4 P3 P2 P1 P1' P2' P3' P4'
Gly 3 1 0 0 1 4 0 0
Pro 0 0 0 0 0 2 0 1
Ala 0 2 1 5 0 1 1 0
Val 2 2 1 1 0 0 1 0
Leu 3 4 3 7 1 0 2 0
Ile 1 2 0 0 1 0 0 0
Met 0 0 0 1 1 1 2 1
Phe 1 1 1 3 0 0 0 1
Tyr 1 1 0 0 1 0 1 1
Trp 1 1 1 0 0 0 1 1
Ser 2 3 1 1 6 0 1 1
Thr 1 0 2 2 3 2 1 0
Cys 0 0 0 1 0 0 1 0
Asn 0 0 0 0 1 1 2 3
Gln 2 3 5 0 0 2 4 3
Asp 0 0 0 0 1 1 0 1
Glu 0 0 1 0 2 2 1 2
Lys 0 0 3 0 1 1 0 2
Arg 2 1 2 0 0 2 1 1
His 0 0 0 0 0 0 0 1