General rule information
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Accession |
PRU01250 |
Dates |
15-AUG-2019 (Created) 22-NOV-2019 (Last updated, Version 2) |
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
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Similarity |
Belongs to the ClpX chaperone family. |
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.
end case
From: PS51902 |
Key
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From
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To
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Description
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Tag
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Condition
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FTGroup
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DOMAIN
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from
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to
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ClpX-type ZB #
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METAL
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13
|
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13
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Zinc
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C
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1
|
METAL
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16
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16
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Zinc
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|
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C
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1
|
METAL
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|
35
|
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35
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Zinc
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|
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C
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1
|
METAL
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38
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38
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Zinc
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C
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1
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Additional information
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Size range |
45-60 amino acids |
Related rules |
None |
Repeats |
1 |
Topology |
Undefined |
Example |
Q6G177 (CLPX_BARQU) |
Scope |
Bacteria
Eukaryota; Euarchontoglires |
Comments |
None |
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
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