AC   PRU01250;
DC   Domain;
TR   PROSITE; PS51902; CLPX_ZB; 1; level=0
XX
Names: 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.
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CC   -!- SIMILARITY: Belongs to the ClpX chaperone family.
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GO   GO:0051082; F:unfolded protein binding
GO   GO:0006457; P:protein folding
case <FTGroup:1>
GO   GO:0046983; F:protein dimerization activity
GO   GO:0008270; F:zinc ion binding
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KW   Metal-binding
KW   Zinc
end case
KW   Chaperone
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FT   From: PS51902
FT   DOMAIN          from..to
FT                   /note="ClpX-type ZB #"
FT   BINDING         13
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   Group: 1; Condition: C
FT   BINDING         16
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   Group: 1; Condition: C
FT   BINDING         35
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   Group: 1; Condition: C
FT   BINDING         38
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   Group: 1; Condition: C
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Chop: Nter=0; Cter=0;
Size: 45-60;
Related: None;
Repeats: 1;
Topology: Undefined;
Example: Q6G177;
Scope:
 Bacteria
 Eukaryota; Euarchontoglires
Comments: None;
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# Revision 1.4 2022/11/19
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