{PDOC51902}
{PS51902; CLPX_ZB}
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* ClpX zinc binding (ZB) domain profile *
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Molecular chaperones  and  proteases  are part of an essential quality control
machinery in  the cell, which ensures the conformational integrity of proteins
under conditions  of  normal  growth  as well as under stress. Prokaryotic and
organellar ClpX  is a molecular chaperone which can also work as a specificity
factor for  the  ClpP  protease. The chaperone ClpX associates with the serine
protease ClpP  to  form  ClpXP, a cylindrical structure that is similar to the
26S proteasome.   ClpX  binds  and,  subsequently,  unfolds  and  translocates
substrate proteins  into  the  ClpP  chamber  in an ATP-dependent manner. 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 [1,2,3,4,5].

The core of the ClpX-type ZB domain is organized into two hairpins followed by
one alpha-helix  (see  <PDB:1OVX>). Dimerization brings the sole alpha-helices
from each  monomer  together  in an anti-parallel orientation when viewed from
one symmetry  axis,  and  the  second  beta-hairpins  together  along a second
symmetry axis.  The  dimer  interface consists of highly conserved hydrophobic
residues. The four conserved cysteines are involved in the coordination of one
Zn(II) ion per monomer [3,4,5].

The profile we developed covers the entire ClpX-type ZB domain.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: August 2019 / First entry.

[ 1] Corydon T.J., Wilsbech M., Jespersgaard C., Andresen B.S.,
     Borglum A.D., Pedersen S., Bolund L., Gregersen N., Bross P.
     "Human and mouse mitochondrial orthologs of bacterial ClpX."
     Mamm. Genome 11:899-905(2000).
     PubMed=11003706
[ 2] Banecki B., Wawrzynow A., Puzewicz J., Georgopoulos C., Zylicz M.
     "Structure-function analysis of the zinc-binding region of the Clpx
     molecular chaperone."
     J. Biol. Chem. 276:18843-18848(2001).
     PubMed=11278349; DOI=10.1074/jbc.M007507200
[ 3] Wojtyra U.A., Thibault G., Tuite A., Houry W.A.
     "The N-terminal zinc binding domain of ClpX is a dimerization domain
     that modulates the chaperone function."
     J. Biol. Chem. 278:48981-48990(2003).
     PubMed=12937164; DOI=10.1074/jbc.M307825200
[ 4] Donaldson L.W., Wojtyra U., Houry W.A.
     "Solution structure of the dimeric zinc binding domain of the
     chaperone ClpX."
     J. Biol. Chem. 278:48991-48996(2003).
     PubMed=14525985; DOI=10.1074/jbc.M307826200
[ 5] Thibault G., Houry W.A.
     "Role of the N-terminal domain of the chaperone ClpX in the
     recognition and degradation of lambda phage protein O."
     J. Phys. Chem. B. 116:6717-6724(2012).
     PubMed=22360725; DOI=10.1021/jp212024b

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