P14756 · ELAS_PSEAE
- ProteinElastase
- GenelasB
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids498 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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
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
Cofactor
Protein has several cofactor binding sites:
Note: Binds 1 Ca2+ ion per subunit.
Note: Binds 1 Zn2+ ion per subunit.
Activity regulation
Inhibited by phosphoramidon.
Features
Showing features for site, binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 197-198 | Cleavage; by autolysis | ||||
Sequence: HA | ||||||
Binding site | 333 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 337 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Active site | 338 | |||||
Sequence: E | ||||||
Binding site | 341 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 361 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: E | ||||||
Binding site | 369 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 372 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 380 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 382 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: L | ||||||
Active site | 420 | Proton donor | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Molecular Function | endopeptidase activity | |
Molecular Function | metal ion binding | |
Molecular Function | metalloendopeptidase activity | |
Biological Process | bacterial-type flagellum-dependent swarming motility | |
Biological Process | protein secretion by the type II secretion system | |
Biological Process | protein transport by the Sec complex | |
Biological Process | proteolysis | |
Biological Process | single-species biofilm formation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameElastase
- EC number
- Alternative names
- Cleaved into 1 chains
Gene names
Organism names
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Pseudomonadales > Pseudomonadaceae > Pseudomonas
Accessions
- Primary accessionP14756
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Secreted in an Xcp-dependent fashion (a type II secretion pathway).
Keywords
- Cellular component
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).
Loss of processing of pro-aminopeptidase to mature aminopeptidase (PubMed:11533066).
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | 75 | in strain: PA103 and N-10 | ||||
Sequence: Y → T | ||||||
Natural variant | 102 | in strain: PA103 and N-10 | ||||
Sequence: Q → R | ||||||
Natural variant | 185 | in strain: PA103 and N-10 | ||||
Sequence: T → Y | ||||||
Natural variant | 211 | in strain: 569B | ||||
Sequence: K → I | ||||||
Natural variant | 241 | in strain: PA103 and N-10 | ||||
Sequence: S → G | ||||||
Natural variant | 282 | in strain: PA103 and N-10 | ||||
Sequence: K → D | ||||||
Natural variant | 325 | in strain: IFO 3455 | ||||
Sequence: M → V | ||||||
Mutagenesis | 420 | Loss of proteolytic and elastolytic activity; significantly decreased processing of proelastase, proelastase accumulates in the periplasm (in E.coli). | ||||
Sequence: H → D or Y | ||||||
Natural variant | 471 | in strain: PA103 | ||||
Sequence: R → S |
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.
Miscellaneous
Chemistry
PTM/Processing
Features
Showing features for signal, propeptide, chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-23 | |||||
Sequence: MKKVSTLDLLFVAIMGVSPAAFA | ||||||
Propeptide | PRO_0000028616 | 24-197 | ||||
Sequence: ADLIDVSKLPSKAAQGAPGPVTLQAAVGAGGADELKAIRSTTLPNGKQVTRYEQFHNGVRVVGEAITEVKGPGKSVAAQRSGHFVANIAADLPGSTTAAVSAEQVLAQAKSLKAQGRKTENDKVELVIRLGENNIAQLVYNVSYLIPGEGLSRPHFVIDAKTGEVLDQWEGLAH | ||||||
Chain | PRO_0000431322 | 24-498 | Pro-elastase | |||
Sequence: ADLIDVSKLPSKAAQGAPGPVTLQAAVGAGGADELKAIRSTTLPNGKQVTRYEQFHNGVRVVGEAITEVKGPGKSVAAQRSGHFVANIAADLPGSTTAAVSAEQVLAQAKSLKAQGRKTENDKVELVIRLGENNIAQLVYNVSYLIPGEGLSRPHFVIDAKTGEVLDQWEGLAHAEAGGPGGNQKIGKYTYGSDYGPLIVNDRCEMDDGNVITVDMNSSTDDSKTTPFRFACPTNTYKQVNGAYSPLNDAHFFGGVVFKLYRDWFGTSPLTHKLYMKVHYGRSVENAYWDGTAMLFGDGATMFYPLVSLDVAAHEVSHGFTEQNSGLIYRGQSGGMNEAFSDMAGEAAEFYMRGKNDFLIGYDIKKGSGALRYMDQPSRDGRSIDNASQYYNGIDVHHSSGVYNRAFYLLANSPGWDTRKAFEVFVDANRYYWTATSNYNSGACGVIRSAQNRNYSAADVTRAFSTVGVTCPSAL | ||||||
Chain | PRO_0000028617 | 198-498 | Elastase | |||
Sequence: AEAGGPGGNQKIGKYTYGSDYGPLIVNDRCEMDDGNVITVDMNSSTDDSKTTPFRFACPTNTYKQVNGAYSPLNDAHFFGGVVFKLYRDWFGTSPLTHKLYMKVHYGRSVENAYWDGTAMLFGDGATMFYPLVSLDVAAHEVSHGFTEQNSGLIYRGQSGGMNEAFSDMAGEAAEFYMRGKNDFLIGYDIKKGSGALRYMDQPSRDGRSIDNASQYYNGIDVHHSSGVYNRAFYLLANSPGWDTRKAFEVFVDANRYYWTATSNYNSGACGVIRSAQNRNYSAADVTRAFSTVGVTCPSAL | ||||||
Disulfide bond | 227↔255 | |||||
Sequence: CEMDDGNVITVDMNSSTDDSKTTPFRFAC | ||||||
Disulfide bond | 467↔494 | |||||
Sequence: CGVIRSAQNRNYSAADVTRAFSTVGVTC |
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).
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
- PTM
Proteomic databases
Expression
Induction
Optimal protein expression in vivo requires both Zn2+ and Ca2+ during growth (at protein level).
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length498
- Mass (Da)53,687
- Last updated1990-04-01 v1
- Checksum4B6AA96A569D9615
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |