Subtilisin Savinase
Details
- Name
- Subtilisin Savinase
- Synonyms
- 3.4.21.62
- Alkaline protease
- Gene Name
- Not Available
- Organism
- Bacillus lentus
- Amino acid sequence
>lcl|BSEQ0010890|Subtilisin Savinase AQSVPWGISRVQAPAAHNRGLTGSGVKVAVLDTGISTHPDLNIRGGASFVPGEPSTQDGN GHGTHVAGTIAALNNSIGVLGVAPSAELYAVKVLGASGSGSVSSIAQGLEWAGNNGMHVA NLSLGSPSPSATLEQAVNSATSRGVLVVAASGNSGAGSISYPARYANAMAVGATDQNNNR ASFSQYGAGLDIVAPGVNVQSTYPGSTYASLNGTSMATPHVAGAAALVKQKNPSWSNVQI RNHLKNTATSLGSTNLYGSGLVNAEAATR
- Number of residues
- 269
- Molecular Weight
- 26698.32
- Theoretical pI
- 9.63
- GO Classification
- Functionsmetal ion binding / serine-type endopeptidase activityProcessessporulation resulting in formation of a cellular sporeComponentsextracellular region
- General Function
- Serine-type endopeptidase activity
- Specific Function
- Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides.
- Pfam Domain Function
- Peptidase_S8 (PF00082)
- Transmembrane Regions
- Not Available
- Cellular Location
- Secreted
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P29600 UniProtKB Entry Name SUBS_BACLE - General References
- Betzel C, Klupsch S, Papendorf G, Hastrup S, Branner S, Wilson KS: Crystal structure of the alkaline proteinase Savinase from Bacillus lentus at 1.4 A resolution. J Mol Biol. 1992 Jan 20;223(2):427-45. [Article]
- Remerowski ML, Pepermans HA, Hilbers CW, Van De Ven FJ: Backbone dynamics of the 269-residue protease Savinase determined from 15N-NMR relaxation measurements. Eur J Biochem. 1996 Feb 1;235(3):629-40. [Article]
- Kuhn P, Knapp M, Soltis SM, Ganshaw G, Thoene M, Bott R: The 0.78 A structure of a serine protease: Bacillus lentus subtilisin. Biochemistry. 1998 Sep 29;37(39):13446-52. [Article]