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PSEAE:ELAS
Contents
| Species (Taxon ID) | Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG12228). (208964) | |
| Gene Name(s) | lasB | |
| Protein Name(s) | Elastase
Neutral metalloproteinase PAE (ECO:0000303 with PMID:1899664[1]) Pseudolysin Pro-elastase | |
| External Links | ||
| UniProt | P14756 | |
| EMBL | M19472 M24531 AB029328 AE004091 | |
| PIR | A32359 | |
| RefSeq | NP_252413.1 WP_003113835.1 | |
| PDB | 1EZM 1U4G 3DBK | |
| PDBsum | 1EZM 1U4G 3DBK | |
| ProteinModelPortal | P14756 | |
| SMR | P14756 | |
| STRING | 208964.PA3724 | |
| BindingDB | P14756 | |
| ChEMBL | CHEMBL1075146 | |
| MEROPS | M04.005 | |
| EnsemblBacteria | AAG07111 | |
| GeneID | 880368 | |
| KEGG | pae:PA3724 | |
| PATRIC | 19842075 | |
| PseudoCAP | PA3724 | |
| eggNOG | COG3227 | |
| HOGENOM | HOG000272374 | |
| InParanoid | P14756 | |
| KO | K01399 | |
| OMA | VTIRYIE | |
| OrthoDB | EOG6DJXWM | |
| PhylomeDB | P14756 | |
| BioCyc | MetaCyc:MONOMER-14569 | |
| EvolutionaryTrace | P14756 | |
| PMAP-CutDB | P14756 | |
| Proteomes | UP000002438 | |
| GO | GO:0005576 GO:0046872 GO:0004222 GO:0051542 GO:0060309 | |
| Gene3D | 3.10.170.10 | |
| InterPro | IPR011096 IPR025711 IPR023612 IPR001570 IPR013856 | |
| Pfam | PF07504 PF03413 PF01447 PF02868 | |
| PRINTS | PR00730 | |
| PROSITE | PS00142 | |
Annotations
| Qualifier | GO ID | GO term name | Reference | ECO ID | ECO term name | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|---|---|
| GO:0004175 |
endopeptidase activity |
ECO:0000314 |
F |
The fifth group of columns in Fig. 4A (labeled lasB elastase activity) shows that the elastase activity of P. aeruginosa lasB (identified in Uniprot as elastase) is inhibited by the introduction of A. alternata extract. |
complete | |||||
|
involved_in |
GO:0071978 |
bacterial-type flagellum-dependent swarming motility |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0052051 |
interaction with host via protein secreted by type II secretion system |
ECO:0000314 |
direct assay evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0044010 |
single-species biofilm formation |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0043952 |
protein transport by the Sec complex |
ECO:0000314 |
direct assay evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0015628 |
protein secretion by the type II secretion system |
ECO:0000314 |
direct assay evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0006508 |
proteolysis |
ECO:0000314 |
direct assay evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
enables |
GO:0004222 |
metalloendopeptidase activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0006508 |
proteolysis |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
|
enables |
GO:0016787 |
hydrolase activity |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0005576 |
extracellular region |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
|
enables |
GO:0008237 |
metallopeptidase activity |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0008233 |
peptidase activity |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0009405 |
pathogenesis |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0006508 |
proteolysis |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
|
enables |
GO:0046872 |
metal ion binding |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
Notes
References
See Help:References for how to manage references in GONUTS.
- ↑ Thayer, MM et al. (1991) Three-dimensional structure of the elastase of Pseudomonas aeruginosa at 1.5-A resolution. J. Biol. Chem. 266 2864-71 PubMed GONUTS page
- ↑ Rashmi, M et al. (2018) Anti-quorum sensing and antibiofilm potential of Alternaria alternata, a foliar endophyte of Carica papaya, evidenced by QS assays and in-silico analysis. Fungal Biol 122 998-1012 PubMed GONUTS page
- ↑ 3.0 3.1 Overhage, J et al. (2008) Swarming of Pseudomonas aeruginosa is a complex adaptation leading to increased production of virulence factors and antibiotic resistance. J. Bacteriol. 190 2671-9 PubMed GONUTS page
- ↑ Alcorn, JF & Wright, JR (2004) Degradation of pulmonary surfactant protein D by Pseudomonas aeruginosa elastase abrogates innate immune function. J. Biol. Chem. 279 30871-9 PubMed GONUTS page
- ↑ 5.0 5.1 Braun, P et al. (1998) Secretion of elastinolytic enzymes and their propeptides by Pseudomonas aeruginosa. J. Bacteriol. 180 3467-9 PubMed GONUTS page
- ↑ Olson, JC & Ohman, DE (1992) Efficient production and processing of elastase and LasA by Pseudomonas aeruginosa require zinc and calcium ions. J. Bacteriol. 174 4140-7 PubMed GONUTS page
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