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ECOLI:OPDA
Contents
| Species (Taxon ID) | Escherichia coli (strain K12). (83333) | |
| Gene Name(s) | prlC (synonyms: opdA) | |
| Protein Name(s) | Oligopeptidase A | |
| External Links | ||
| UniProt | P27298 | |
| EMBL | M93984 U00039 U00096 AP009048 | |
| PIR | S47718 | |
| RefSeq | NP_417955.1 YP_491937.1 | |
| ProteinModelPortal | P27298 | |
| SMR | P27298 | |
| DIP | DIP-10566N | |
| IntAct | P27298 | |
| MINT | MINT-1234260 | |
| STRING | 511145.b3498 | |
| PaxDb | P27298 | |
| PRIDE | P27298 | |
| EnsemblBacteria | AAC76523 BAE77796 | |
| GeneID | 12933512 948016 | |
| KEGG | ecj:Y75_p3679 eco:b3498 | |
| PATRIC | 32122446 | |
| EchoBASE | EB1411 | |
| EcoGene | EG11441 | |
| eggNOG | COG0339 | |
| HOGENOM | HOG000245986 | |
| InParanoid | P27298 | |
| KO | K01414 | |
| OMA | VMRPPAY | |
| OrthoDB | EOG6WHNPN | |
| PhylomeDB | P27298 | |
| BioCyc | EcoCyc:EG11441-MONOMER ECOL316407:JW3465-MONOMER MetaCyc:EG11441-MONOMER | |
| PRO | PR:P27298 | |
| Proteomes | UP000000318 UP000000625 | |
| Genevestigator | P27298 | |
| GO | GO:0005737 GO:0046872 GO:0004222 GO:0008233 GO:0006260 GO:0006465 | |
| Gene3D | 1.10.1370.10 1.20.1050.40 3.40.390.10 | |
| InterPro | IPR024079 IPR024077 IPR024080 IPR001567 | |
| Pfam | PF01432 | |
| PROSITE | PS00142 | |
Annotations
| Qualifier | GO ID | GO term name | Reference | ECO ID | ECO term name | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|---|---|
| GO:0008233 |
peptidase activity |
ECO:0000314 |
F |
Fig. 1 illustrates the products released during signal peptide degradation using radioactivity analysis. |
complete | |||||
|
involved_in |
GO:0006518 |
peptide metabolic process |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
MGI:MGI:1354165 |
P |
Seeded From UniProt |
complete | ||
|
involved_in |
GO:0006508 |
proteolysis |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
PANTHER:PTN000211184 |
P |
Seeded From UniProt |
complete | ||
|
involved_in |
GO:0006465 |
signal peptide processing |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
EcoGene:EG11441 |
P |
Seeded From UniProt |
complete | ||
|
enables |
GO:0004222 |
metalloendopeptidase activity |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
MGI:MGI:1354165 |
F |
Seeded From UniProt |
complete | ||
|
involved_in |
GO:0006465 |
signal peptide processing |
ECO:0000314 |
direct assay evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
enables |
GO:0008233 |
peptidase activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0005829 |
cytosol |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
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:0008233 |
peptidase activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0005737 |
cytoplasm |
ECO:0000304 |
author statement supported by traceable reference used in manual assertion |
C |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0006260 |
DNA replication |
ECO:0000304 |
author statement supported by traceable reference used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
enables |
GO:0008233 |
peptidase activity |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
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 | |||
|
enables |
GO:0008237 |
metallopeptidase 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 | |||
|
enables |
GO:0016787 |
hydrolase 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.
- ↑ Novak, P et al. (1986) Localization and purification of two enzymes from Escherichia coli capable of hydrolyzing a signal peptide. J. Biol. Chem. 261 420-7 PubMed GONUTS page
- ↑ 2.0 2.1 2.2 2.3 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
- ↑ Novak, P & Dev, IK (1988) Degradation of a signal peptide by protease IV and oligopeptidase A. J. Bacteriol. 170 5067-75 PubMed GONUTS page
- ↑ Irisawa, T et al. (1993) Effect of trans-4-guanidinomethylcyclohexanecarboxylic acid 4-tert-butylphenyl ester, a trypsin inhibitor, on the growth of various strains of Escherichia coli. Biol. Pharm. Bull. 16 621-6 PubMed GONUTS page
- ↑ Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page
- ↑ Jiang, X et al. (1998) Escherichia coli prlC gene encodes a trypsin-like proteinase regulating the cell cycle. J. Biochem. 124 980-5 PubMed GONUTS page
- ↑ Kato, M et al. (1992) Purification and characterization of proteinase In, a trypsin-like proteinase, in Escherichia coli. Eur. J. Biochem. 210 1007-14 PubMed GONUTS page
