PRU01250

Accession	PRU01250
Dates	15-AUG-2019 (Created) 19-NOV-2022 (Last updated, Version 4)

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.

Similarity

Belongs to the ClpX chaperone family.

GO:0051082; Molecular function: unfolded protein binding.
GO:0006457; Biological process: protein folding.

GO:0046983; Molecular function: protein dimerization activity.
GO:0008270; Molecular function: zinc ion binding.

Metal-binding
Zinc

Chaperone

From: PS51902

Key

From

To

Description

Tag

Condition

FTGroup

DOMAIN

from

to

ClpX-type ZB #

BINDING

13

13

/ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105

C

1

BINDING

16

16

/ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105

C

1

BINDING

35

35

/ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105

C

1

BINDING

38

38

/ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105

C

1

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.

View rule in raw text format (no links)

• UniProtKB/Swiss-Prot sets
  

  Bacteria	[648]
  Eukaryota	[4]
  All	[ 652 ]

  
  
• Retrieve set of proteins with 3D structure for this domain