GONUTS has been updated to MW1.31 Most things seem to be working but be sure to report problems.

Have any questions? Please email us at ecoliwiki@gmail.com

PSEAE:LASA

From GONUTS
Jump to: navigation, search
Species (Taxon ID) Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 /JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1). (208964)
Gene Name(s) lasA
Protein Name(s) Protease LasA

Staphylolytic protease

External Links
UniProt P14789
EMBL M20982
X55904
U68175
AE004091
PIR A46076
F83411
RefSeq NP_250562.1
WP_010895585.1
PDB 3IT5
3IT7
PDBsum 3IT5
3IT7
ProteinModelPortal P14789
SMR P14789
STRING 208964.PA1871
MEROPS M23.002
PaxDb P14789
PRIDE P14789
EnsemblBacteria AAG05260
GeneID 878260
KEGG pae:PA1871
PATRIC fig|208964.12.peg.1948
PseudoCAP PA1871
eggNOG ENOG4108VC8
COG0739
HOGENOM HOG000274301
InParanoid P14789
KO K08642
OMA ATNYYHM
BioCyc PAER208964:G1FZ6-1911-MONOMER
BRENDA 3.4.24.B16
EvolutionaryTrace P14789
Proteomes UP000002438
GO GO:0005615
GO:0004175
GO:0046872
GO:0004222
GO:0009405
GO:0015628
GO:0043952
GO:0006508
InterPro IPR011055
IPR000841
IPR016047
Pfam PF01551
PRINTS PR00933
SUPFAM SSF51261

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0004175

peptidase inhibitor activity

PMID:30227935[1]

ECO:0000314

F

The third group of columns in Fig. 4A (labeled lasA protease) Shows that the protease (peptidase) activity of P. aeruginosa lasA is inhibited by the introduction of A. alternata extract.

complete
CACAO 13335

GO:0009253

peptidoglycan catabolic process

PMID:30227935[1]

ECO:0000314

P

The fourth group of columns in Fig. 4A (labeled lasA staphylolytic activity) Shows that the peptidoglycan degradation (staphylolytic) activity of P. aeruginosa lasA is inhibited by the introduction of A. alternata extract.

complete
CACAO 13390

GO:0061785

peptidoglycan endopeptidase activity

PMID:30227935[1]

ECO:0000314

F

The fourth group of columns in Fig. 4A (labeled lasA staphylolytic activity) Shows that the peptidoglycan degradation (staphylolytic) activity of P. aeruginosa lasA is inhibited by the introduction of A. alternata extract.

complete

involved_in

GO:0043952

protein transport by the Sec complex

PMID:9642203[2]

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

PMID:9642203[2]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006508

proteolysis

PMID:1597429[3]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005615

extracellular space

PMID:25488299[4]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0004175

endopeptidase activity

PMID:9642203[2]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0004222

metalloendopeptidase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000841

F

Seeded From UniProt

complete

involved_in

GO:0006508

proteolysis

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000841

P

Seeded From UniProt

complete

involved_in

GO:0006508

proteolysis

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0645

P

Seeded From UniProt

complete

enables

GO:0008237

metallopeptidase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0482

F

Seeded From UniProt

complete

enables

GO:0046872

metal ion binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0479

F

Seeded From UniProt

complete

enables

GO:0016787

hydrolase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0378

F

Seeded From UniProt

complete

enables

GO:0008233

peptidase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0645

F

Seeded From UniProt

complete

involved_in

GO:0009405

pathogenesis

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0843

P

Seeded From UniProt

complete

part_of

GO:0005576

extracellular region

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0964
UniProtKB-SubCell:SL-0243

C

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. 1.0 1.1 1.2 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
  2. 2.0 2.1 2.2 Braun, P et al. (1998) Secretion of elastinolytic enzymes and their propeptides by Pseudomonas aeruginosa. J. Bacteriol. 180 3467-9 PubMed GONUTS page
  3. 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
  4. Passmore, IJ et al. (2015) Mep72, a metzincin protease that is preferentially secreted by biofilms of Pseudomonas aeruginosa. J. Bacteriol. 197 762-73 PubMed GONUTS page