Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Combined Automated Annotation using Multiple IEA Methods
A secreted aminopeptidase of Pseudomonas aeruginosa. Identification, primary structure, and relationship to other aminopeptidases.
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PaAP was identified as a secreted, heat-stable, zinc-dependent aminopeptidase (AP56, activated to AP28) encoded by PA2939.
"This activity was inhibited by Zn chelators but not by inhibitors of serine- or thiol-proteases, suggesting that AP(28) is a Zn-dependent enzyme."
Secretion of elastinolytic enzymes and their propeptides by Pseudomonas aeruginosa.
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The uncharacterised SGAP-like protein (later PaAP) accumulated in the medium of strains with reduced extracellular proteolysis.
"Furthermore, a hitherto undefined protein with homology to a Streptomyces griseus aminopeptidase accumulated under these conditions."
Purification of outer membrane vesicles from Pseudomonas aeruginosa and their activation of an IL-8 response.
Extracellular aminopeptidase modulates biofilm development of Pseudomonas aeruginosa by affecting matrix exopolysaccharide and bacterial cell death.
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paaP deletion alters biofilm development; extracellular catalytic activity is required.
"PaAP functioned extracellularly and aminopeptidase catalytic activity was essential for its effect on biofilm development."
Pseudomonas aeruginosa Leucine Aminopeptidase Influences Early Biofilm Composition and Structure via Vesicle-Associated Antibiofilm Activity.
Cooperation and Cheating through a Secreted Aminopeptidase in the Pseudomonas aeruginosa RpoS Response.
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PaAP is an RpoS-controlled public good needed for growth on protein.
"Our results suggest that PaAP is an integral part of a proteolytic sequence in P. aeruginosa that permits the utilization of protein as a nutrient source."
Extracellular proteolytic activation of Pseudomonas aeruginosa aminopeptidase (PaAP) and insight into the role of its non-catalytic N-terminal domain.
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LysC activates pro-PaAP by C-terminal cleavage.
"pointed at LysC as the principal activating protease, cleaving a Lys512-Ala513 peptide bond at the C-terminal end of pro-PaAP."
An anti-biofilm cyclic peptide targets a secreted aminopeptidase from P. aeruginosa.
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Crystal structures show a binuclear zinc active site and C-terminal propeptide autoinhibition; PaAP is a promiscuous aminopeptidase.
"The active site contains two zinc ions; Zn1 is coordinated by D306, H296 and D369, while Zn2 is coordinated by E341, H467 and D306."
The Secreted Aminopeptidase of Pseudomonas aeruginosa (PaAP).
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Review: PaAP is secreted via the Xcp T2SS and cleaves short peptides with a free N-terminus.
"Leu-Ala and Ala4, having free N-termini, are both cleaved readily [17]."
UniProt entry Q9HZQ8 (LAP_PSEAE)