Q8GB88 · SCPA_ALISE

Function

function

Thermostable pepstatin-insensitive serine-carboxyl proteinase (PubMed:12513991, PubMed:15014068).
Can specifically and efficiently degrade collagen (PubMed:12513991, PubMed:15014068).
In vitro, preferentially cleaves the bovine collagen alpha-1 chain at a single specific cleavage site (PubMed:15014068).
Can also hydrolyze the chromogenic substrate azocoll and synthetic peptides derived from collagen (PubMed:12513991, PubMed:15014068).
Also shows low activity with albumin and casein, but cannot use keratin azure and elastin (PubMed:12513991).
May play a saprophytic role in soils through degradation of collagenous materials (such as those from carcasses) in cooperation with other saprophytes under thermoacidophilic conditions and play an important role in global cycling of nitrogen (PubMed:15014068).

Miscellaneous

Kumamolisin-As does not make a specific three-quarters/one-quarter cut of the triple-helical, native collagen, characteristic for the previously described collagenases.

Cofactor

Ca2+ (UniProtKB | Rhea| CHEBI:29108 )

Note: Binds 1 Ca2+ ion per subunit.

Activity regulation

Partially inhibited by L-alanyl-L-alanyl-L-phenylalanyl-chloromethane, leupeptin, 1 mM Fe2+ or 1 mM Hg2+ (PubMed:12513991).
Insensitive to specific inhibitors of aspartic proteinases, such as pepstatin and diazoacetyl-DL-norleucine methyl ester (DAN), to specific inhibitors of metalloproteinases (EDTA), cysteine proteinases (N-ethylmaleimide) and serine proteinases (PMSF) (PubMed:12513991).

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
32 μMPhe-Gly-Pro-Ala-Gly-Pro-Ile-Gly
214 μMMet-Gly-Pro-Arg-Gly-Phe-Pro-Gly-Ser
1 μM(N-methylanthranilic acid)-Met-Gly-Pro-His-Phe-Phe-Pro-N-(2,4-dinitrophenyl)-Lys-D-Arg-D-Arg (IQF)4.040
kcat is 5.41 sec-1 with Phe-Gly-Pro-Ala-Gly-Pro-Ile-Gly as substrate (PubMed:12513991).
kcat is 351 sec-1 with Met-Gly-Pro-Arg-Gly-Phe-Pro-Gly-Ser as substrate (PubMed:12513991).
kcat is 395 sec-1 with IQF as substrate (at 40 degrees Celsius and pH 4.0) (PubMed:15014068).

pH Dependence

Optimum pH is 3.9 (for degradation of azocoll) (PubMed:12513991).
Stable at pH 3.5 to 5.0 (PubMed:12513991).

Temperature Dependence

Optimum temperature is 60 degrees Celsius (for degradation of azocoll).

Features

Showing features for active site, binding site.

Type
IDPosition(s)Description
Active site267Charge relay system
Active site271Charge relay system
Active site467Charge relay system
Binding site505Ca2+ (UniProtKB | ChEBI)
Binding site506Ca2+ (UniProtKB | ChEBI)
Binding site523Ca2+ (UniProtKB | ChEBI)
Binding site525Ca2+ (UniProtKB | ChEBI)
Binding site527Ca2+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Molecular Functionmetal ion binding
Molecular Functionserine-type endopeptidase activity
Molecular Functiontripeptidyl-peptidase activity
Biological Processproteolysis

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Kumamolisin-As
  • EC number
  • Alternative names
    • Acid collagenase
    • Collagenolytic serine protease

Gene names

    • Name
      scpA

Organism names

  • Taxonomic identifier
  • Strain
    • ATCC BAA-609 / DSM 17614 / JCM 11817 / NBRC 100866 / NTAP-1
  • Taxonomic lineage
    Bacteria > Bacillota > Bacilli > Bacillales > Alicyclobacillaceae > Alicyclobacillus

Accessions

  • Primary accession
    Q8GB88

Subcellular Location

Secreted

Keywords

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis267Loses both auto-processing activity and proteolytic activity; when associated with N-353.
Mutagenesis267Can be very slowly converted during the acid treatment into a mature form. Almost loss of activity with IQF as substrate. Exists as an equilibrated mixture of nicked and intact forms of the precursor and retains very low activity; when associated with N-353.
Mutagenesis353Retains auto-processing activity but only low activity. Exists as an equilibrated mixture of nicked and intact forms of the precursor and retains very low activity; when associated with H-267. Loses both auto-processing activity and proteolytic activity; when associated with A-267 or Q-267.

PTM/Processing

Features

Showing features for propeptide, chain.

Type
IDPosition(s)Description
PropeptidePRO_00004611571-189Removed in mature form
ChainPRO_0000461158190-553Kumamolisin-As

Post-translational modification

Autocatalytically processed.

Keywords

Expression

Induction

Constitutively expressed.

Interaction

Subunit

Monomer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain194-547Peptidase S53

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    553
  • Mass (Da)
    57,154
  • Last updated
    2003-03-01 v1
  • MD5 Checksum
    64CA434B76934708EED800B6934324C9
MSDMEKPWKEGEEARAVLQGHARAQAPQAVDKGPVAGDERMAVTVVLRRQRAGELAAHVERQAAIAPHAREHLKREAFAASHGASLDDFAELRRFADAHGLALDRANVAAGTAVLSGPVDAINRAFGVELRHFDHPDGSYRSYLGEVTVPASIAPMIEAVLGLDTRPVARPHFRMQRRAEGGFEARSQAAAPTAYTPLDVAQAYQFPEGLDGQGQCIAIIELGGGYDEASLAQYFASLGVPAPQVVSVSVDGASNQPTGDPSGPDGEVELDIEVAGALAPGAKFAVYFAPNTDAGFLDAITTAIHDPTLKPSVVSISWGGPEDSWTSAAIAAMNRAFLDAAALGVTVLAAAGDSGSTDGEQDGLYHVDFPAASPYVLACGGTRLVASGGRIAQETVWNDGPDGGATGGGVSRIFPLPAWQEHANVPPSANPGASSGRGVPDLAGNADPATGYEVVIDGEATVIGGTSAVAPLFAALVARINQKLGKAVGYLNPTLYQLPADVFHDITEGNNDIANRAQIYQAGPGWDPCTGLGSPIGVRLLQALLPSASQPQP

Mass Spectrometry

Molecular mass is 36,960 Da. Determined by MALDI. The measured mass is that of the mature ScpA.

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AB085855
EMBL· GenBank· DDBJ
BAC41257.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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