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annotation rule: PRU01250

General rule information [?]

Accession PRU01250
Dates 15-AUG-2019 (Created)
22-NOV-2019 (Last updated, Version 2)
Data class Domain
Predictors PROSITE; PS51902; CLPX_ZB
Name ClpX zinc binding (ZB) domain
Function ClpX consists of an NH(2)-terminal zinc binding (ZB) domain that is involved in substrate and cofactor recognition and a AAA(+) domain that arranges into a hexamer in an ATP-dependent manner. The ClpX ZB domain contains the characteristic pattern C-X(2)-C-X(18)-C-X(2)-C of four cysteine residues and forms a constitutive dimer that is essential for the degradation of some ClpX substrates such as lambdaO and MuA but is not required for the degradation of other substrates such as green fluorescent protein SsrA.

Propagated annotation [?]


Comments [?]

Similarity Belongs to the ClpX chaperone family.

Gene Ontology [?]

GO:0051082; Molecular function: unfolded protein binding.
GO:0006457; Biological process: protein folding.
case <FTGroup:1>
GO:0046983; Molecular function: protein dimerization activity.
GO:0008270; Molecular function: zinc ion binding.

Keywords [?]

end case


Features [?]

From: PS51902
Key     From     To       Description   Tag   Condition   FTGroup
DOMAIN     from     to       ClpX-type ZB #        
METAL     13     13       Zinc     C   1
METAL     16     16       Zinc     C   1
METAL     35     35       Zinc     C   1
METAL     38     38       Zinc     C   1

Additional information [?]

Size range 45-60 amino acids
Related rules None
Repeats 1
Topology Undefined
Example Q6G177 (CLPX_BARQU)
Scope
Bacteria
Eukaryota; Euarchontoglires
Comments None

Copyright

PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.



UniProtKB rule member sequences [?]