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PROSITE documentation PDOC00125

Serine proteases, subtilase family, active sites

Description:

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 sp. (gene ale).
  • Alkaline serine exoprotease A from Vibrio alginolyticus (gene proA).
  • Aqualysin I from Thermus aquaticus (gene pstI).
  • AspA from Aeromonas salmonicida.
  • 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).
  • Nisin leader peptide processing protease nisP from Lactococcus lactis.
  • Serotype-specific antigene 1 from Pasteurella haemolytica (gene ssa1).
  • 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 3.4.21.75), 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.
  • Prestalk-specific proteins tagB and tagC from slime mold [4]. Both proteins consist of two domains: a N-terminal subtilase catalytic domain and a C- terminal ABC transporter domain (see <PDOC00185>).

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%

Note:

These proteins belong to family S8 in the classification of peptidases [5,E1].

Expert(s) to contact by email:

Brannigan J.
 Siezen R.J.

Last update:

April 2006 / Pattern revised.

Technical section:

PROSITE methods (with tools and information) covered by this documentation:

SUBTILASE_ASP, PS00136; Serine proteases, subtilase family, aspartic acid active site  (PATTERN)
Consensus pattern: [STAIV]-{ERDL}-[LIVMF]-[LIVM]-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: 55.
• Retrieve an alignment of Swiss-Prot true positive hits:
  Clustal format, color, condensed view  / Clustal format, color  / Clustal format, plain text  / Fasta format
• Retrieve the sequence logo from the alignment
• Taxonomic tree view of all Swiss-Prot/TrEMBL entries matching PS00136
• Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS00136
• Scan Swiss-Prot/TrEMBL entries against PS00136
• view ligand binding statistics
Matching PDB structures: 1A2Q 1AF4 1AH2 1AK9 ... [ALL]
SUBTILASE_HIS, PS00137; Serine proteases, subtilase family, histidine active site  (PATTERN)
Consensus pattern: H-G-[STM]-x-[VIC]-[STAGC]-[GS]-x-[LIVMA]-[STAGCLV]-[SAGM]
H is the active site residue
Sequences known to belong to this class detected by the pattern: ALL, except for aspA and ssa1 which both seem to lack the histidine active site
Other sequence(s) detected in Swiss-Prot: adenylate cyclase type VIII.
• Retrieve an alignment of Swiss-Prot true positive hits:
  Clustal format, color, condensed view  / Clustal format, color  / Clustal format, plain text  / Fasta format
• Retrieve the sequence logo from the alignment
• Taxonomic tree view of all Swiss-Prot/TrEMBL entries matching PS00137
• Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS00137
• Scan Swiss-Prot/TrEMBL entries against PS00137
• view ligand binding statistics
Matching PDB structures: 1A2Q 1AF4 1AH2 1AK9 ... [ALL]
SUBTILASE_SER, PS00138; Serine proteases, subtilase family, serine active site  (PATTERN)
Consensus pattern: G-T-S-x-[SA]-x-P-x-{L}-[STAVC]-[AG]
S is the active site residue
Sequences known to belong to this class detected by the pattern: ALL, except for nisP, tagC and S.marcescens extracellular serine protease
Other sequence(s) detected in Swiss-Prot: 7.
• Retrieve an alignment of Swiss-Prot true positive hits:
  Clustal format, color, condensed view  / Clustal format, color  / Clustal format, plain text  / Fasta format
• Retrieve the sequence logo from the alignment
• Taxonomic tree view of all Swiss-Prot/TrEMBL entries matching PS00138
• Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS00138
• Scan Swiss-Prot/TrEMBL entries against PS00138
• view ligand binding statistics
Matching PDB structures: 1AF4 1AH2 1AK9 1AQN ... [ALL]

References:

1 AuthorsSiezen R.J., de Vos W.M., Leunissen J.A.M., Dijkstra B.W.
TitleHomology modelling and protein engineering strategy of subtilases, the family of subtilisin-like serine proteinases.
SourceProtein Eng. 4:719-737(1991).
PubMed ID1798697
2 AuthorsSiezen R.J.
Source(In) Proceeding subtilisin symposium, Hamburg, (1992).
3 AuthorsBarr P.J.
SourceCell 66:1-3(1991).
4 AuthorsShaulsky G., Kuspa A., Loomis W.F.
TitleA multidrug resistance transporter/serine protease gene is required for prestalk specialization in Dictyostelium.
SourceGenes Dev. 9:1111-1122(1995).
PubMed ID7744252
5 AuthorsRawlings N.D., Barrett A.J.
TitleFamilies of serine peptidases.
SourceMethods Enzymol. 244:19-61(1994).
PubMed ID7845208
E1
Sourcehttp://www.expasy.org/cgi-bin/lists?peptidas.txt

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