Type | Description |
---|---|
Definition | periplasmic chaperone Skp |
Date | Results | Publications |
---|---|---|
2019-04-06 12:06:00 | Skp can dissolve aggregated OmpC while SurA cannot convert aggregated OmpC into the monodisperse form and the conformations of OmpC recognized by the two chaperones as well as their stoichiometries of binding are different. | 29543429 |
2016-12-24 10:21:00 | CpxQ combats toxicity at the inner membrane by downregulating the synthesis of the periplasmic chaperone Skp. | 27048800 |
2016-05-07 10:50:00 | Bioinformatic analysis of amino acid conservation, structural analysis of LPS-binding proteins, and MD simulations confirm the absence of a specific lipopolysaccharide binding site on Skp, and reveal a highly conserved salt-bridge network | 25809264 |
2014-01-04 13:11:00 | The global lifetime of the OmpX-Skp and tOmpA-Skp chaperone-substrate complex is seven orders of magnitude longer, emerging from the short local lifetimes by avidity. | 24077225 |
2010-01-21 00:00:00 | Evidence presented suggests that DegP/Skp function to rescue OMPs that fall off the SurA pathway. | 17908933 |
Type | IDs |
---|---|
Synonymous | ECK0177, hlpA, ompH |
Gene |
UniProtKB-ID:
SKP_ECOLI
UniprotKB:
P0AEU7
UniParc:
UPI000012C942
EMBL:
X54797,
AP009048,
M21118,
U00096,
U70214,
X75465
EnsemblGenome:
b0178,
BAA77853
KO:
eco:b0178,
ecj:JW0173
|
Nucleutide sequences |
EMBL-CDS:
BAA77853.1,
CAA53207.1,
CAA38567.1,
AAC73289.1,
AAA24630.1,
AAB08607.1
EnsemblGenome_TRS:
BAA77853,
AAC73289
|
Protein sequencees |
EnsemblGenome_PRO:
AAC73289,
BAA77853
RefSeq:
NP_414720.1
|
Others |
UniRef100:
UniRef100_P0AEU9
UniRef90:
UniRef90_P0AEU9
UniRef50:
UniRef50_P58607
|
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