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ECOLI:PA1

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) pldA
Protein Name(s) Phospholipase A1

Detergent-resistant phospholipase A DR-phospholipase A Outer membrane phospholipase A OM PLA OMPLA Phosphatidylcholine 1-acylhydrolase

External Links
UniProt P0A921
EMBL X02143
M87049
U00096
AP009048
M30198
PIR A22133
RefSeq NP_418265.1
YP_491621.1
PDB 1FW2
1FW3
1ILD
1ILZ
1IM0
1QD5
1QD6
PDBsum 1FW2
1FW3
1ILD
1ILZ
1IM0
1QD5
1QD6
ProteinModelPortal P0A921
SMR P0A921
IntAct P0A921
STRING 511145.b3821
PaxDb P0A921
PRIDE P0A921
EnsemblBacteria AAC76824
BAE77480
GeneID 12930309
948307
KEGG ecj:Y75_p3357
eco:b3821
PATRIC 32123143
EchoBASE EB0731
EcoGene EG10738
eggNOG COG2829
HOGENOM HOG000288150
InParanoid P0A921
KO K01058
OMA YNHRQTR
OrthoDB EOG6HQSN6
PhylomeDB P0A921
BioCyc EcoCyc:MONOMER0-341
ECOL316407:JW3794-MONOMER
MetaCyc:MONOMER0-341
EvolutionaryTrace P0A921
PRO PR:P0A921
Proteomes UP000000318
UP000000625
Genevestigator P0A921
GO GO:0045203
GO:0031230
GO:0052740
GO:0005509
GO:0008970
GO:0052739
GO:0004623
GO:0042803
GO:0016042
Gene3D 2.40.230.10
InterPro IPR003187
Pfam PF02253
PRINTS PR01486
SUPFAM SSF56931

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0009279

cell outer membrane

PMID:10806384[1]

ECO:0000314

C

Table 1

complete

enables

GO:0042803

protein homodimerization activity

PMID:11371166[2]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0031230

intrinsic component of cell outer membrane

PMID:11371166[2]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0005509

calcium ion binding

PMID:11371166[2]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0045203

integral component of cell outer membrane

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10738
PANTHER:PTN002220789

C

Seeded From UniProt

complete

enables

GO:0005509

calcium ion binding

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10738
PANTHER:PTN002220789

F

Seeded From UniProt

complete

enables

GO:0004623

phospholipase A2 activity

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10738
PANTHER:PTN002220789

F

Seeded From UniProt

complete

part_of

GO:0045203

integral component of cell outer membrane

PMID:6397463[4]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0009279

cell outer membrane

PMID:10806384[1]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0005509

calcium ion binding

PMID:11371166[2]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0004623

phospholipase A2 activity

PMID:2653433[5]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0004620

phospholipase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR003187
InterPro:IPR036541

F

Seeded From UniProt

complete

involved_in

GO:0006629

lipid metabolic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR003187
InterPro:IPR036541

P

Seeded From UniProt

complete

part_of

GO:0016020

membrane

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR003187
InterPro:IPR036541

C

Seeded From UniProt

complete

enables

GO:0008970

phospholipase A1 activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:3.1.1.32

F

Seeded From UniProt

complete

enables

GO:0052740

1-acyl-2-lysophosphatidylserine acylhydrolase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:3.1.1.32

F

Seeded From UniProt

complete

enables

GO:0102568

phospholipase A2 activity consuming 1,2-dioleoylphosphatidylethanolamine)

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:3.1.1.4

F

Seeded From UniProt

complete

enables

GO:0052739

phosphatidylserine 1-acylhydrolase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:3.1.1.32

F

Seeded From UniProt

complete

enables

GO:0004623

phospholipase A2 activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:3.1.1.4

F

Seeded From UniProt

complete

enables

GO:0102567

phospholipase A2 activity (consuming 1,2-dipalmitoylphosphatidylcholine)

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:3.1.1.4

F

Seeded From UniProt

complete

enables

GO:0008970

phospholipase A1 activity

PMID:11371166[2]

ECO:0000304

author statement supported by traceable reference used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0004623

phospholipase A2 activity

PMID:11371166[2]

ECO:0000304

author statement supported by traceable reference used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0016042

lipid catabolic process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0442

P

Seeded From UniProt

complete

involved_in

GO:0006629

lipid metabolic process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0443

P

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

part_of

GO:0016020

membrane

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0472

C

Seeded From UniProt

complete

part_of

GO:0009279

cell outer membrane

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0998
UniProtKB-SubCell:SL-0040

C

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

part_of

GO:0016021

integral component of membrane

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0812

C

Seeded From UniProt

complete

Notes

References

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

  1. 1.0 1.1 Molloy, MP et al. (2000) Proteomic analysis of the Escherichia coli outer membrane. Eur. J. Biochem. 267 2871-81 PubMed GONUTS page
  2. 2.0 2.1 2.2 2.3 2.4 2.5 Snijder, HJ et al. (2001) Structural investigations of calcium binding and its role in activity and activation of outer membrane phospholipase A from Escherichia coli. J. Mol. Biol. 309 477-89 PubMed GONUTS page
  3. 3.0 3.1 3.2 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  4. Homma, H et al. (1984) Characteristics of detergent-resistant phospholipase A overproduced in E. coli cells bearing its cloned structural gene. J. Biochem. 96 1645-53 PubMed GONUTS page
  5. Horrevoets, AJ et al. (1989) Kinetic characterization of Escherichia coli outer membrane phospholipase A using mixed detergent-lipid micelles. Biochemistry 28 1139-47 PubMed GONUTS page