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ECOLI:OMPT
Contents
Species (Taxon ID) | Escherichia coli (strain K12). (83333) | |
Gene Name(s) | ompT | |
Protein Name(s) | Protease 7
Omptin Outer membrane protein 3B Protease A Protease VII | |
External Links | ||
UniProt | P09169 | |
EMBL | X06903 M23630 U82598 U00096 AP009048 | |
PIR | A31387 | |
RefSeq | NP_415097.1 YP_488852.1 | |
PDB | 1I78 | |
PDBsum | 1I78 | |
ProteinModelPortal | P09169 | |
SMR | P09169 | |
STRING | 511145.b0565 | |
MEROPS | A26.001 | |
TCDB | 9.B.50.1.1 | |
SWISS-2DPAGE | P09169 | |
PaxDb | P09169 | |
PRIDE | P09169 | |
EnsemblBacteria | AAC73666 BAA35199 | |
GeneID | 12934526 945185 | |
KEGG | ecj:Y75_p0552 eco:b0565 | |
PATRIC | 32116296 | |
EchoBASE | EB0667 | |
EcoGene | EG10673 | |
eggNOG | COG4571 | |
HOGENOM | HOG000117799 | |
KO | K01355 | |
OMA | KERVYHP | |
OrthoDB | EOG6Q8HZT | |
BioCyc | EcoCyc:EG10673-MONOMER ECOL316407:JW0554-MONOMER MetaCyc:EG10673-MONOMER | |
BRENDA | 3.4.23.49 | |
EvolutionaryTrace | P09169 | |
PRO | PR:P09169 | |
Proteomes | UP000000318 UP000000625 | |
Genevestigator | P09169 | |
GO | GO:0009279 GO:0016021 GO:0031230 GO:0004190 GO:0004175 GO:0004252 GO:0006508 | |
Gene3D | 2.40.128.90 | |
InterPro | IPR020080 IPR023619 IPR020079 IPR000036 | |
Pfam | PF01278 | |
PIRSF | PIRSF001522 | |
PRINTS | PR00482 | |
SUPFAM | SSF69917 | |
PROSITE | PS00834 PS00835 |
Annotations
Qualifier | GO ID | GO term name | Reference | ECO ID | ECO term name | with/from | Aspect | Extension | Notes | Status |
---|---|---|---|---|---|---|---|---|---|---|
GO:0009279 |
cell outer membrane |
ECO:0000314 |
C |
Table 1 |
complete | |||||
GO:0006508 |
proteolysis |
ECO:0000270 |
P |
figure 1 shows that ompT is a protease |
complete | |||||
part_of |
GO:0031230 |
intrinsic component of cell outer membrane |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
part_of |
GO:0031230 |
intrinsic component of cell outer membrane |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
involved_in |
GO:0006508 |
proteolysis |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
enables |
GO:0004252 |
serine-type endopeptidase activity |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0004175 |
endopeptidase activity |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
part_of |
GO:0009279 |
cell outer membrane |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
part_of |
GO:0009279 |
cell outer membrane |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
part_of |
GO:0009279 |
cell outer membrane |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
part_of |
GO:0009279 |
cell outer membrane |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
part_of |
GO:0009279 |
cell outer membrane |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
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:0004175 |
endopeptidase activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0004190 |
aspartic-type endopeptidase 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 | |||
part_of |
GO:0009279 |
cell outer membrane |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
enables |
GO:0008233 |
peptidase activity |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
part_of |
GO:0009279 |
cell outer membrane |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
enables |
GO:0016787 |
hydrolase activity |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
involved_in |
GO:0006508 |
proteolysis |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
part_of |
GO:0016020 |
membrane |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
part_of |
GO:0016021 |
integral component of membrane |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
enables |
GO:0004190 |
aspartic-type endopeptidase activity |
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.
- ↑ 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
- ↑ Henderson, TA et al. (1994) Artifactual processing of penicillin-binding proteins 7 and 1b by the OmpT protease of Escherichia coli. J. Bacteriol. 176 256-9 PubMed GONUTS page
- ↑ Rupprecht, KR et al. (1983) omp T: Escherichia coli K-12 structural gene for protein a (3b). J. Bacteriol. 153 1104-6 PubMed GONUTS page
- ↑ 4.0 4.1 Kramer, RA et al. (2000) Identification of active site serine and histidine residues in Escherichia coli outer membrane protease OmpT. FEBS Lett. 468 220-4 PubMed GONUTS page
- ↑ 5.0 5.1 Grodberg, J & Dunn, JJ (1988) ompT encodes the Escherichia coli outer membrane protease that cleaves T7 RNA polymerase during purification. J. Bacteriol. 170 1245-53 PubMed GONUTS page
- ↑ Han, MJ et al. (2012) Comparative analysis of envelope proteomes in Escherichia coli B and K-12 strains. J. Microbiol. Biotechnol. 22 470-8 PubMed GONUTS page
- ↑ Zhang, N et al. (2007) Comparison of SDS- and methanol-assisted protein solubilization and digestion methods for Escherichia coli membrane proteome analysis by 2-D LC-MS/MS. Proteomics 7 484-93 PubMed GONUTS page
- ↑ Lopez-Campistrous, A et al. (2005) Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth. Mol. Cell Proteomics 4 1205-9 PubMed GONUTS page
- ↑ Lai, EM et al. (2004) Proteomic screening and identification of differentially distributed membrane proteins in Escherichia coli. Mol. Microbiol. 52 1029-44 PubMed GONUTS page
- ↑ Kramer, RA et al. (2000) In vitro folding, purification and characterization of Escherichia coli outer membrane protease ompT. Eur. J. Biochem. 267 885-93 PubMed GONUTS page