 |
|
Annotation rule MF_00249 |
General rule information
[?]
Accession |
MF_00249 |
Dates |
1-JUN-2001 (Created) 18-NOV-2019 (Last updated, Version 29) |
Propagated annotation
[?]
Identifier, protein and gene names
[?]
case <OC:Escherichia> or <OC:Shigella> or <OC:Salmonella>
Protein name |
RecName:
|
Full=ATP-dependent protease ATPase subunit HslU;
|
AltName:
|
Full=Heat shock protein HslU;
|
AltName:
|
Full=Unfoldase HslU;
|
|
end case
case not <OC:Escherichia> and not <OC:Shigella> and not <OC:Salmonella>
Protein name |
RecName:
|
Full=ATP-dependent protease ATPase subunit HslU;
|
AltName:
|
Full=Unfoldase HslU;
|
|
end case
Function |
ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. |
Subunit |
A double ring-shaped homohexamer of HslV is capped on each side by a ring-shaped HslU homohexamer. The assembly of the HslU/HslV complex is dependent on binding of ATP. |
Subcellular location |
Cytoplasm. |
case <OC:Escherichia> or <OC:Shigella> or <OC:Salmonella>
end case
Similarity |
Belongs to the ClpX chaperone family. HslU subfamily. |
case <OC:Escherichia> or <OC:Shigella> or <OC:Salmonella>
end case
From: HSLU_ECOLI (P0A6H5) |
Key
|
|
From
|
|
To
|
|
Description
|
|
Tag
|
|
Condition
|
|
FTGroup
|
NP_BIND
|
|
60
|
|
65
|
|
ATP
|
|
|
|
G-[VIC]-G-K-T-E
|
|
|
BINDING
|
|
18
|
|
18
|
|
ATP; via amide nitrogen and carbonyl oxygen
|
|
|
|
[IV]
|
|
|
BINDING
|
|
256
|
|
256
|
|
ATP
|
|
|
|
D
|
|
|
BINDING
|
|
321
|
|
321
|
|
ATP
|
|
|
|
E
|
|
|
BINDING
|
|
393
|
|
393
|
|
ATP
|
|
|
|
R
|
|
|
Additional information
[?]
Size range |
430-491 amino acids |
Related rules |
MF_00175 (CLPX) |
Fusion |
None |
Comments |
The protease subunit of the HslUV complex is described in MF_00248. Unlike in E.coli, H.influenzae and T.maritima, the family member in B.subtilis (ClpY) was shown to be part of a complex (ClpQY) with serine protease activity and not threonine protease activity. |