UniProt functional annotation for P00780



	UniProt functional annotation for P00780

UniProt code: P00780.

Organism: Bacillus licheniformis.

Taxonomy: Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.

Function: Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides (Ref.4, PubMed:11109488). Shows high specificity for aromatic and hydrophobic amino acids in the P1 substrate position (PubMed:11109488). May play an important role in the degradation of feather keratin (PubMed:11109488). {ECO:0000269|PubMed:11109488, ECO:0000269|Ref.4}.

Catalytic activity: Reaction=Hydrolysis of proteins with broad specificity for peptide bonds, and a preference for a large uncharged residue in P1. Hydrolyzes peptide amides.; EC=3.4.21.62; Evidence={ECO:0000269|PubMed:11109488, ECO:0000269|Ref.4};

Cofactor: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:8512925}; Note=Binds 2 calcium ions per subunit. {ECO:0000269|PubMed:8512925};

Activity regulation: Inhibited by p-chlorophenyl and 1-naphthyl boronic acid derivatives. {ECO:0000269|PubMed:9425066}.

Biophysicochemical properties: Kinetic parameters: KM=1.2 mM for Suc-Ala(2)-Ala-pNA {ECO:0000269|Ref.4}; KM=0.79 mM for Suc-Ala(2)-Phe-pNA {ECO:0000269|Ref.4}; KM=0.851 mM for Suc-Ala(2)-Phe-pNA {ECO:0000269|PubMed:11109488}; KM=0.22 mM for MeO-Suc-Ala(2)-Phe-pNA {ECO:0000269|Ref.4}; KM=5.6 mM for Suc-Gly(2)-Phe-pNA {ECO:0000269|PubMed:11109488}; KM=0.334 mM for Suc-Ala(2)-Pro-Phe-pNA {ECO:0000269|PubMed:11109488}; KM=0.062 mM for Suc-Ala(2)-Pro-Leu-pNA {ECO:0000269|PubMed:11109488}; KM=0.422 mM for Suc-Ala(2)-Pro-Arg-pNA {ECO:0000269|PubMed:11109488}; KM=0.245 mM for Suc-Ala(2)-Pro-Glu-pNA {ECO:0000269|PubMed:11109488}; KM=0.042 mM for Suc-Ala-Glu-Pro-Phe-pNA {ECO:0000269|PubMed:11109488}; Note=kcat is 1.6 sec(-1) with Suc-Ala(2)-Ala-pNA as substrate. kcat is 57 sec(-1) with Suc-Ala(2)-Phe-pNA as substrate. kcat is 97 sec(- 1) with MeO-Suc-Ala(2)-Phe-pNA as substrate (Ref.4). kcat is 0.990 sec(-1) with Suc-Gly(2)-Phe-pNA as substrate. kcat is 20.3 sec(-1) with Suc-Ala(2)-Phe-pNA as substrate. kcat is 646 sec(-1) with Suc- Ala(2)-Pro-Phe-pNA as substrate. kcat is 137 sec(-1) with Suc-Ala(2)- Pro-Leu-pNA as substrate. kcat is 5.31 sec(-1) with Suc-Ala(2)-Pro- Arg-pNA as substrate. kcat is 1.92 sec(-1) with Suc-Ala(2)-Pro-Glu- pNA as substrate. kcat is 375 sec(-1) with Suc-Ala-Glu-Pro-Phe-pNA as substrate (PubMed:11109488). {ECO:0000269|PubMed:11109488, ECO:0000269|Ref.4};

Subcellular location: Secreted {ECO:0000269|PubMed:11109488}.

Biotechnology: Used as a detergent protease. Sold under the name Alcalase by Novozymes.

Similarity: Belongs to the peptidase S8 family. {ECO:0000255|PROSITE- ProRule:PRU01240}.

Annotations taken from UniProtKB at the EBI.


Organism:		Bacillus licheniformis.
Taxonomy:		Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.



Function:		Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides (Ref.4, PubMed:11109488). Shows high specificity for aromatic and hydrophobic amino acids in the P1 substrate position (PubMed:11109488). May play an important role in the degradation of feather keratin (PubMed:11109488). {ECO:0000269\|PubMed:11109488, ECO:0000269\|Ref.4}.


Catalytic activity:		Reaction=Hydrolysis of proteins with broad specificity for peptide bonds, and a preference for a large uncharged residue in P1. Hydrolyzes peptide amides.; EC=3.4.21.62; Evidence={ECO:0000269\|PubMed:11109488, ECO:0000269\|Ref.4};
Cofactor:		Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269\|PubMed:8512925}; Note=Binds 2 calcium ions per subunit. {ECO:0000269\|PubMed:8512925};
Activity regulation:		Inhibited by p-chlorophenyl and 1-naphthyl boronic acid derivatives. {ECO:0000269\|PubMed:9425066}.
Biophysicochemical properties:		Kinetic parameters: KM=1.2 mM for Suc-Ala(2)-Ala-pNA {ECO:0000269\|Ref.4}; KM=0.79 mM for Suc-Ala(2)-Phe-pNA {ECO:0000269\|Ref.4}; KM=0.851 mM for Suc-Ala(2)-Phe-pNA {ECO:0000269\|PubMed:11109488}; KM=0.22 mM for MeO-Suc-Ala(2)-Phe-pNA {ECO:0000269\|Ref.4}; KM=5.6 mM for Suc-Gly(2)-Phe-pNA {ECO:0000269\|PubMed:11109488}; KM=0.334 mM for Suc-Ala(2)-Pro-Phe-pNA {ECO:0000269\|PubMed:11109488}; KM=0.062 mM for Suc-Ala(2)-Pro-Leu-pNA {ECO:0000269\|PubMed:11109488}; KM=0.422 mM for Suc-Ala(2)-Pro-Arg-pNA {ECO:0000269\|PubMed:11109488}; KM=0.245 mM for Suc-Ala(2)-Pro-Glu-pNA {ECO:0000269\|PubMed:11109488}; KM=0.042 mM for Suc-Ala-Glu-Pro-Phe-pNA {ECO:0000269\|PubMed:11109488}; Note=kcat is 1.6 sec(-1) with Suc-Ala(2)-Ala-pNA as substrate. kcat is 57 sec(-1) with Suc-Ala(2)-Phe-pNA as substrate. kcat is 97 sec(- 1) with MeO-Suc-Ala(2)-Phe-pNA as substrate (Ref.4). kcat is 0.990 sec(-1) with Suc-Gly(2)-Phe-pNA as substrate. kcat is 20.3 sec(-1) with Suc-Ala(2)-Phe-pNA as substrate. kcat is 646 sec(-1) with Suc- Ala(2)-Pro-Phe-pNA as substrate. kcat is 137 sec(-1) with Suc-Ala(2)- Pro-Leu-pNA as substrate. kcat is 5.31 sec(-1) with Suc-Ala(2)-Pro- Arg-pNA as substrate. kcat is 1.92 sec(-1) with Suc-Ala(2)-Pro-Glu- pNA as substrate. kcat is 375 sec(-1) with Suc-Ala-Glu-Pro-Phe-pNA as substrate (PubMed:11109488). {ECO:0000269\|PubMed:11109488, ECO:0000269\|Ref.4};
Subcellular location:		Secreted {ECO:0000269\|PubMed:11109488}.
Biotechnology:		Used as a detergent protease. Sold under the name Alcalase by Novozymes.
Similarity:		Belongs to the peptidase S8 family. {ECO:0000255\|PROSITE- ProRule:PRU01240}.