Type | Description |
---|---|
Definition | periplasmic folding chaperone |
Date | Results | Publications |
---|---|---|
2021-02-27 13:48:00 | The Central Spike Complex of Bacteriophage T4 Contacts PpiD in the Periplasm of Escherichia coli. | 33036312 |
2020-07-18 11:41:00 | The results of this study indicate that the PpiD/YfgM chaperone complex is a primary interaction partner of the SecYEG translocon. | 31699901 |
2018-04-21 11:21:00 | PpiD contributes to the efficient detachment of newly secreted OmpA from the inner membrane and in doing so, seems to cooperate in a hierarchical manner with other periplasmic chaperones such as SurA, DegP, and Skp. | 29097228 |
2010-12-04 10:49:00 | PpiD functions as a chaperone and contributes to the network of periplasmic chaperone activities | 20920237 |
2010-01-21 00:00:00 | although PpiD and SurA have partially overlapping substrate specificities, they fulfil different functions in the cell | 18498364 |
Type | IDs |
---|---|
Synonymous | ECK0435, ybaU |
Gene |
UniProtKB-ID:
PPID_ECOLI
UniprotKB:
P0ADY1
UniParc:
UPI0000132078
EMBL:
AP009048,
U00096,
U82664,
D82943
EnsemblGenome:
b0441,
BAE76221
KO:
eco:b0441,
ecj:JW0431
|
Nucleutide sequences |
EMBL-CDS:
BAE76221.1,
AAB40197.1,
AAC73544.1,
BAA11645.1
EnsemblGenome_TRS:
BAE76221,
AAC73544
|
Protein sequencees |
EnsemblGenome_PRO:
BAE76221,
AAC73544
RefSeq:
NP_414975.1
|
Others |
UniRef100:
UniRef100_P0ADY2
UniRef90:
UniRef90_P0ADY2
UniRef50:
UniRef50_P0ADY2
|
{{proteinIndex+1}} | mRNA | Protein | UniprotKB | Description | ||||
---|---|---|---|---|---|---|---|---|
Refseq |
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Conserved domain | Region: {{conservedDomain.region == '' || conservedDomain.region == null ? "-": conservedDomain.region}} GFID: {{conservedDomain.gfid == '' || conservedDomain.gfid == null ? "-": conservedDomain.gfid}} Family: {{conservedDomain.family == '' || conservedDomain.family == null ? "-": conservedDomain.family}} CDD: {{conservedDomain.cdd}} - |
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