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- *****************************************************
- * Serine proteases, subtilase family, active sites *
- *****************************************************
-
- Subtilases [1,2] are an extensive family of serine proteases whose catalytic
- activity is provided by a charge relay system similar to that of the trypsin
- family of serine proteases but which evolved by independent convergent
- evolution. The sequence around the residues involved in the catalytic triad
- (aspartic acid, serine and histidine) are completely different from that of
- the analogous residues in the trypsin serine proteases and can be used as
- signatures specific to that category of proteases.
-
- The subtilase family currently includes the following proteases:
-
- - Subtilisins (EC 3.4.21.62), these alkaline proteases from various Bacillus
- species have been the target of numerous studies in the past thirty years.
-
- - Alkaline elastase YaB from Bacillus subtilis (gene ale).
- - Alkaline serine exoprotease A from Vibrio alginolyticus (gene proA).
- - Aqualysin I from Thermus aquaticus (gene pstI).
- - Bacillopeptidase F (esterase) from Bacillus subtilis (gene bpf).
- - C5A peptidase from Streptococcus pyogenes (gene scpA).
- - Cell envelope-located proteases PI, PII, and PIII from Lactococcus lactis.
- - Extracellular serine protease from Serratia marcescens.
- - Extracellular protease from Xanthomonas campestris.
- - Intracellular serine protease (ISP) from various Bacillus.
- - Minor extracellular serine protease epr from Bacillus subtilis (gene epr).
- - Minor extracellular serine protease vpr from Bacillus subtilis (gene vpr).
- - Thermitase (EC 3.4.21.66) from Thermoactinomyces vulgaris.
-
- - Calcium-dependent protease from Anabaena variabilis (gene prcA).
- - Halolysin from halophilic bacteria sp. 172p1 (gene hly).
-
- - Alkaline extracellular protease (AEP) from Yarrowia lipolytica (gene xpr2).
- - Alkaline proteinase from Cephalosporium acremonium (gene alp).
- - Cerevisin (EC 3.4.21.48) (vacuolar protease B) from yeast (gene PRB1).
- - Cuticle-degrading protease (pr1) from Metarhizium anisopliae.
- - KEX-1 protease from Kluyveromyces lactis.
- - Kexin (EC 3.4.21.61) from yeast (gene KEX-2).
- - Oryzin (EC 3.4.21.63) (alkaline proteinase) from Aspergillus (gene alp).
- - Proteinase K (EC 3.4.21.64) from Tritirachium album (gene proK).
- - Proteinase R from Tritirachium album (gene proR).
- - Proteinase T from Tritirachium album (gene proT).
- - Subtilisin-like protease III from yeast (gene YSP3).
- - Thermomycolin (EC 3.4.21.65) from Malbranchea sulfurea.
-
- - Furin (EC 3.4.21.85), neuroendocrine convertases 1 to 3 (NEC-1 to -3) and
- PACE4 protease from mammals, other vertebrates, and invertebrates. These
- proteases are involved in the processing of hormone precursors at sites
- comprised of pairs of basic amino acid residues [3].
- - Tripeptidyl-peptidase II (EC 3.4.14.10) (tripeptidyl aminopeptidase) from
- Human.
-
- -Consensus pattern: [SAIV]-x-[LIVM](2)-D-[DSTA]-G-[LIVMFC]-x(2,3)-[DNH]
- [D is the active site residue]
- -Sequences known to belong to this class detected by the pattern: the majority
- of subtilases with a few exceptions.
- -Other sequence(s) detected in SWISS-PROT: 15.
-
- -Consensus pattern: H-G-T-x-[VC]-[STAG]-[GS]-x-[LIVMA]
- [H is the active site residue]
- -Sequences known to belong to this class detected by the pattern: ALL, except
- for L. lactis cell envelope-located proteases PI, PII, and PIII.
- -Other sequence(s) detected in SWISS-PROT: Drosophila neurogenic locus delta
- protein.
-
- -Consensus pattern: G-T-S-x-[SA]-x-P-x(2)-[STAVC]-[AG]
- [S is the active site residue]
- -Sequences known to belong to this class detected by the pattern: ALL.
- -Other sequence(s) detected in SWISS-PROT: human fosB and rabbit apomucin.
-
- -Note: if a protein includes at least two of the three active site signatures,
- the probability of it being a serine protease from the subtilase family is
- 100%
-
- -Expert(s) to contact by email: Brannigan J.
- jab5@vaxa.york.ac.uk
- Siezen R.J.
- nizo@caos.caos.kun.nl
-
- -Last update: June 1994 / Text revised.
-
- [ 1] Siezen R.J., de Vos W.M., Leunissen J.A.M., Dijkstra B.W.
- Protein Eng. 4:719-737(1991).
- [ 2] Siezen R.J.
- (In) Proceeding subtilisin symposium, Hamburg, (1992).
- [ 3] Barr P.J.
- Cell 66:1-3(1991).
-