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ECOLI:OPPA
Contents
| Species (Taxon ID) | Escherichia coli (strain K12). (83333) | |
| Gene Name(s) | oppA | |
| Protein Name(s) | Periplasmic oligopeptide-binding protein | |
| External Links | ||
| UniProt | P23843 | |
| EMBL | J05433 M60918 U00096 AP009048 X59501 D83137 | |
| PIR | F64871 | |
| RefSeq | NP_415759.1 YP_489511.1 | |
| PDB | 3TCF 3TCG 3TCH | |
| PDBsum | 3TCF 3TCG 3TCH | |
| ProteinModelPortal | P23843 | |
| SMR | P23843 | |
| DIP | DIP-10405N | |
| IntAct | P23843 | |
| STRING | 511145.b1243 | |
| SWISS-2DPAGE | P23843 | |
| PaxDb | P23843 | |
| PRIDE | P23843 | |
| EnsemblBacteria | AAC74325 BAA14775 | |
| GeneID | 12934488 945830 | |
| KEGG | ecj:Y75_p1217 eco:b1243 | |
| PATRIC | 32117746 | |
| EchoBASE | EB0668 | |
| EcoGene | EG10674 | |
| eggNOG | COG4166 | |
| HOGENOM | HOG000179191 | |
| InParanoid | P23843 | |
| KO | K15580 | |
| OMA | PEWFSWS | |
| OrthoDB | EOG6V7BH5 | |
| PhylomeDB | P23843 | |
| BioCyc | EcoCyc:OPPA-MONOMER ECOL316407:JW1235-MONOMER | |
| EvolutionaryTrace | P23843 | |
| PRO | PR:P23843 | |
| Proteomes | UP000000318 UP000000625 | |
| Genevestigator | P23843 | |
| GO | GO:0042597 GO:0005215 GO:0006857 GO:0015031 GO:0009408 | |
| InterPro | IPR000914 IPR023765 | |
| Pfam | PF00496 | |
| PROSITE | PS01040 | |
Annotations
| Qualifier | GO ID | GO term name | Reference | ECO ID | ECO term name | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|---|---|
| GO:0006857 |
oligopeptide transport |
ECO:0000315 |
P |
Table 4. Table 5 |
complete | |||||
|
enables |
GO:1904680 |
peptide transmembrane transporter activity |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
PANTHER:PTN000767645 |
F |
Seeded From UniProt |
complete | ||
|
part_of |
GO:0030288 |
outer membrane-bounded periplasmic space |
ECO:0000318 |
biological aspect of ancestor evidence used in manual assertion |
EcoGene:EG10248 |
C |
Seeded From UniProt |
complete | ||
|
involved_in |
GO:0006857 |
oligopeptide transport |
ECO:0000314 |
direct assay evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
enables |
GO:1900750 |
oligopeptide binding |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:1900750 |
oligopeptide binding |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0061077 |
chaperone-mediated protein folding |
ECO:0000314 |
direct assay evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0061077 |
chaperone-mediated protein folding |
ECO:0000314 |
direct assay evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0030288 |
outer membrane-bounded periplasmic space |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0030288 |
outer membrane-bounded periplasmic space |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0030288 |
outer membrane-bounded periplasmic space |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0030288 |
outer membrane-bounded periplasmic space |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0030288 |
outer membrane-bounded periplasmic space |
ECO:0000314 |
direct assay evidence used in manual assertion |
C |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0009408 |
response to heat |
ECO:0000315 |
mutant phenotype evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0006857 |
oligopeptide transport |
ECO:0000314 |
direct assay evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0043190 |
ATP-binding cassette (ABC) transporter complex |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0055085 |
transmembrane transport |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0015833 |
peptide transport |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0015031 |
protein transport |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
|
part_of |
GO:0042597 |
periplasmic space |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
Notes
References
See Help:References for how to manage references in GONUTS.
- ↑ Andrews, JC & Short, SA (1986) opp-lac Operon fusions and transcriptional regulation of the Escherichia coli trp-linked oligopeptide permease. J. Bacteriol. 165 434-42 PubMed GONUTS page
- ↑ 2.0 2.1 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
- ↑ Guyer, CA et al. (1985) Purification and characterization of a periplasmic oligopeptide binding protein from Escherichia coli. J. Biol. Chem. 260 10812-8 PubMed GONUTS page
- ↑ Guyer, CA et al. (1986) Binding specificity of the periplasmic oligopeptide-binding protein from Escherichia coli. J. Bacteriol. 168 775-9 PubMed GONUTS page
- ↑ 5.0 5.1 5.2 Klepsch, MM et al. (2011) Escherichia coli peptide binding protein OppA has a preference for positively charged peptides. J. Mol. Biol. 414 75-85 PubMed GONUTS page
- ↑ Richarme, G & Caldas, TD (1997) Chaperone properties of the bacterial periplasmic substrate-binding proteins. J. Biol. Chem. 272 15607-12 PubMed GONUTS page
- ↑ Lennon, CW et al. (2015) Folding Optimization In Vivo Uncovers New Chaperones. J. Mol. Biol. 427 2983-94 PubMed GONUTS page
- ↑ Han, MJ et al. (2014) Comparison of the large-scale periplasmic proteomes of the Escherichia coli K-12 and B strains. J. Biosci. Bioeng. 117 437-42 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
- ↑ Molloy, MP et al. (2000) Proteomic analysis of the Escherichia coli outer membrane. Eur. J. Biochem. 267 2871-81 PubMed GONUTS page
- ↑ Krisko, A et al. (2014) Inferring gene function from evolutionary change in signatures of translation efficiency. Genome Biol. 15 R44 PubMed GONUTS page
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