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ECOLI:LEP
Contents
| Species (Taxon ID) | Escherichia coli (strain K12). (83333) | |
| Gene Name(s) | lepB | |
| Protein Name(s) | Signal peptidase I
SPase I Leader peptidase I | |
| External Links | ||
| UniProt | P00803 | |
| EMBL | K00426 D64044 U00096 AP009048 | |
| PIR | G65034 | |
| RefSeq | NP_417063.1 WP_000002541.1 | |
| PDB | 1B12 1KN9 1T7D 3IIQ 3S04 | |
| PDBsum | 1B12 1KN9 1T7D 3IIQ 3S04 | |
| ProteinModelPortal | P00803 | |
| SMR | P00803 | |
| BioGrid | 4259467 | |
| STRING | 511145.b2568 | |
| BindingDB | P00803 | |
| ChEMBL | CHEMBL4470 | |
| MEROPS | S26.001 | |
| PaxDb | P00803 | |
| PRIDE | P00803 | |
| EnsemblBacteria | AAC75621 BAE76744 | |
| GeneID | 947040 | |
| KEGG | ecj:JW2552 eco:b2568 | |
| PATRIC | 32120535 | |
| EchoBASE | EB0525 | |
| EcoGene | EG10530 | |
| eggNOG | ENOG4105C3F COG0681 | |
| HOGENOM | HOG000003674 | |
| InParanoid | P00803 | |
| KO | K03100 | |
| OMA | FKWAPAR | |
| PhylomeDB | P00803 | |
| BioCyc | EcoCyc:EG10530-MONOMER MetaCyc:EG10530-MONOMER | |
| BRENDA | 3.4.21.89 | |
| SABIO-RK | P00803 | |
| EvolutionaryTrace | P00803 | |
| PRO | PR:P00803 | |
| Proteomes | UP000000318 UP000000625 | |
| GO | GO:0016021 GO:0005887 GO:0005886 GO:0004175 GO:0008233 GO:0004252 GO:0015643 GO:0016485 GO:0006508 GO:0006465 | |
| Gene3D | 2.10.109.10 | |
| InterPro | IPR000223 IPR019758 IPR019757 IPR019756 IPR028360 IPR019759 IPR015927 IPR019533 | |
| Pfam | PF00717 PF10502 | |
| PRINTS | PR00727 | |
| SUPFAM | SSF51306 | |
| TIGRFAMs | TIGR02227 | |
| PROSITE | PS00501 PS00760 PS00761 | |
Annotations
| Qualifier | GO ID | GO term name | Reference | ECO ID | ECO term name | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|---|---|
|
involved_in |
GO:0006465 |
signal peptide processing |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
EcoGene:EG10530 |
P |
Seeded From UniProt |
complete | ||
|
part_of |
GO:0005887 |
integral component of plasma membrane |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
EcoGene:EG10530 |
C |
Seeded From UniProt |
complete | ||
|
enables |
GO:0004252 |
serine-type endopeptidase activity |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
EcoGene:EG10530 |
F |
Seeded From UniProt |
complete | ||
|
involved_in |
GO:0016485 |
protein processing |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0016485 |
protein processing |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0016021 |
integral component of membrane |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
|
enables |
GO:0015643 |
toxic substance binding |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0008233 |
peptidase activity |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0008233 |
peptidase activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0006508 |
proteolysis |
ECO:0000315 |
mutant phenotype 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 | |||
|
part_of |
GO:0005886 |
plasma membrane |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0006465 |
signal peptide processing |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
P |
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 | |||
|
involved_in |
GO:0006465 |
signal peptide processing |
ECO:0000314 |
direct assay evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0005887 |
integral component of plasma membrane |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0005886 |
plasma membrane |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0005886 |
plasma membrane |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0005886 |
plasma membrane |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
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 | |||
|
enables |
GO:0004175 |
endopeptidase activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0004175 |
endopeptidase activity |
ECO:0000314 |
direct assay evidence used in manual 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:0008236 |
serine-type peptidase activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
InterPro:IPR000223 |
F |
Seeded From UniProt |
complete | ||
|
part_of |
GO:0016020 |
membrane |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0016021 |
integral component of membrane |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0016020 |
membrane |
ECO:0000322 |
imported manually asserted information 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:0016021 |
integral component of 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 | |||
|
part_of |
GO:0005886 |
plasma membrane |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
UniProtKB-KW:KW-0997 |
C |
Seeded From UniProt |
complete | ||
|
involved_in |
GO:0006508 |
proteolysis |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
Notes
References
See Help:References for how to manage references in GONUTS.
- ↑ 1.0 1.1 1.2 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
- ↑ 2.0 2.1 Karla, A et al. (2005) The identification of residues that control signal peptidase cleavage fidelity and substrate specificity. J. Biol. Chem. 280 6731-41 PubMed GONUTS page
- ↑ 3.0 3.1 de Zamaroczy, M et al. (2001) Cleavage of colicin D is necessary for cell killing and requires the inner membrane peptidase LepB. Mol. Cell 8 159-68 PubMed GONUTS page
- ↑ 4.0 4.1 4.2 Stein, RL et al. (2000) Kinetic and mechanistic studies of signal peptidase I from Escherichia coli. Biochemistry 39 7973-83 PubMed GONUTS page
- ↑ 5.0 5.1 Kim, YT et al. (2004) Identification of arginine residues important for the activity of Escherichia coli signal peptidase I. Biol. Chem. 385 381-8 PubMed GONUTS page
- ↑ 6.0 6.1 Dalbey, RE & Wickner, W (1985) Leader peptidase catalyzes the release of exported proteins from the outer surface of the Escherichia coli plasma membrane. J. Biol. Chem. 260 15925-31 PubMed GONUTS page
- ↑ 7.0 7.1 Chatterjee, S et al. (1995) Determination of Km and kcat for signal peptidase I using a full length secretory precursor, pro-OmpA-nuclease A. J. Mol. Biol. 245 311-4 PubMed GONUTS page
- ↑ 8.0 8.1 Zwizinski, C & Wickner, W (1980) Purification and characterization of leader (signal) peptidase from Escherichia coli. J. Biol. Chem. 255 7973-7 PubMed GONUTS page
- ↑ Wolfe, PB et al. (1983) Sequence of the leader peptidase gene of Escherichia coli and the orientation of leader peptidase in the bacterial envelope. J. Biol. Chem. 258 12073-80 PubMed GONUTS page
- ↑ Chang, CN et al. (1978) Detection of prokaryotic signal peptidase in an Escherichia coli membrane fraction: endoproteolytic cleavage of nascent f1 pre-coat protein. Proc. Natl. Acad. Sci. U.S.A. 75 361-5 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
- ↑ Daley, DO et al. (2005) Global topology analysis of the Escherichia coli inner membrane proteome. Science 308 1321-3 PubMed GONUTS page
- ↑ Sung, M & Dalbey, RE (1992) Identification of potential active-site residues in the Escherichia coli leader peptidase. J. Biol. Chem. 267 13154-9 PubMed GONUTS page
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