P14756 · ELAS_PSEAE

Function

function

Cleaves host elastin, collagen, IgG, and several complement components as well as endogenous pro-aminopeptidase (PubMed:11533066).
Autocatalyses processing of its pro-peptide (PubMed:1744034, PubMed:9642203).
Processes the pro-peptide of pro-chitin-binding protein (cbpD) (PubMed:9642203).
Involved in the pathogenesis of P.aeruginosa infections

Catalytic activity

  • Hydrolysis of proteins including elastin, collagen types III and IV, fibronectin and immunoglobulin A, generally with bulky hydrophobic group at P1'. Insulin B chain cleavage pattern identical to that of thermolysin, but specificity differs in other respects.
    EC:3.4.24.26 (UniProtKB | ENZYME | Rhea)

Cofactor

Protein has several cofactor binding sites:
Ca2+ (UniProtKB | Rhea| CHEBI:29108 )

Note: Binds 1 Ca2+ ion per subunit.
Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 1 Zn2+ ion per subunit.

Activity regulation

Inhibited by phosphoramidon.

Features

Showing features for site, binding site, active site.

TypeIDPosition(s)Description
Site197-198Cleavage; by autolysis
Binding site333Ca2+ (UniProtKB | ChEBI)
Binding site337Zn2+ (UniProtKB | ChEBI); catalytic
Active site338
Binding site341Zn2+ (UniProtKB | ChEBI); catalytic
Binding site361Zn2+ (UniProtKB | ChEBI); catalytic
Binding site369Ca2+ (UniProtKB | ChEBI)
Binding site372Ca2+ (UniProtKB | ChEBI)
Binding site380Ca2+ (UniProtKB | ChEBI)
Binding site382Ca2+ (UniProtKB | ChEBI)
Active site420Proton donor

GO annotations

AspectTerm
Cellular Componentextracellular region
Molecular Functionendopeptidase activity
Molecular Functionmetal ion binding
Molecular Functionmetalloendopeptidase activity
Biological Processbacterial-type flagellum-dependent swarming motility
Biological Processprotein secretion by the type II secretion system
Biological Processprotein transport by the Sec complex
Biological Processproteolysis
Biological Processsingle-species biofilm formation

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Elastase
  • EC number
  • Alternative names
    • Neutral metalloproteinase
    • PAE
    • Pseudolysin
  • Cleaved into 1 chains

Gene names

    • Name
      lasB
    • Ordered locus names
      PA3724

Organism names

Accessions

  • Primary accession
    P14756

Proteomes

Organism-specific databases

Subcellular Location

Secreted
Note: Secreted in an Xcp-dependent fashion (a type II secretion pathway).

Keywords

Phenotypes & Variants

Disruption phenotype

Loss of processing of its own pro-peptide and pro-chitin-binding protein CbpD (PubMed:9642203).
Loss of processing of pro-aminopeptidase to mature aminopeptidase (PubMed:11533066).

Features

Showing features for natural variant, mutagenesis.

TypeIDPosition(s)Description
Natural variant75in strain: PA103 and N-10
Natural variant102in strain: PA103 and N-10
Natural variant185in strain: PA103 and N-10
Natural variant211in strain: 569B
Natural variant241in strain: PA103 and N-10
Natural variant282in strain: PA103 and N-10
Natural variant325in strain: IFO 3455
Mutagenesis420Loss of proteolytic and elastolytic activity; significantly decreased processing of proelastase, proelastase accumulates in the periplasm (in E.coli).
Natural variant471in strain: PA103

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 8 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Miscellaneous

Chemistry

PTM/Processing

Features

Showing features for signal, propeptide, chain, disulfide bond.

TypeIDPosition(s)Description
Signal1-23
PropeptidePRO_000002861624-197
ChainPRO_000043132224-498Pro-elastase
ChainPRO_0000028617198-498Elastase
Disulfide bond227↔255
Disulfide bond467↔494

Post-translational modification

Made as a membrane-associated pre-pro-protein, which is exported to the periplasm (yielding pro-elastase) with removal of the signal peptide. Under certain conditions pro-elastase can accumulate. The pro-peptide is removed in the periplasm yielding a (mature length) 33 kDa protein, probably by autocatalysis (PubMed:1744034).
The pro-peptide probably remains associated with elastase and can be secreted (PubMed:9642203).
Further alterations (perhaps processing) seems to be required before secretion into the extracellular space (PubMed:1744034).

Keywords

Proteomic databases

Expression

Induction

Optimal protein expression in vivo requires both Zn2+ and Ca2+ during growth (at protein level).

Interaction

Subunit

Monomer.

Protein-protein interaction databases

Chemistry

Family & Domains

Sequence similarities

Belongs to the peptidase M4 family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    498
  • Mass (Da)
    53,687
  • Last updated
    1990-04-01 v1
  • Checksum
    4B6AA96A569D9615
MKKVSTLDLLFVAIMGVSPAAFAADLIDVSKLPSKAAQGAPGPVTLQAAVGAGGADELKAIRSTTLPNGKQVTRYEQFHNGVRVVGEAITEVKGPGKSVAAQRSGHFVANIAADLPGSTTAAVSAEQVLAQAKSLKAQGRKTENDKVELVIRLGENNIAQLVYNVSYLIPGEGLSRPHFVIDAKTGEVLDQWEGLAHAEAGGPGGNQKIGKYTYGSDYGPLIVNDRCEMDDGNVITVDMNSSTDDSKTTPFRFACPTNTYKQVNGAYSPLNDAHFFGGVVFKLYRDWFGTSPLTHKLYMKVHYGRSVENAYWDGTAMLFGDGATMFYPLVSLDVAAHEVSHGFTEQNSGLIYRGQSGGMNEAFSDMAGEAAEFYMRGKNDFLIGYDIKKGSGALRYMDQPSRDGRSIDNASQYYNGIDVHHSSGVYNRAFYLLANSPGWDTRKAFEVFVDANRYYWTATSNYNSGACGVIRSAQNRNYSAADVTRAFSTVGVTCPSAL

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
M19472
EMBL· GenBank· DDBJ
AAB36615.1
EMBL· GenBank· DDBJ
Genomic DNA
M24531
EMBL· GenBank· DDBJ
AAA25811.1
EMBL· GenBank· DDBJ
Genomic DNA
AB029328
EMBL· GenBank· DDBJ
BAB79621.1
EMBL· GenBank· DDBJ
Genomic DNA
AE004091
EMBL· GenBank· DDBJ
AAG07111.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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