{PDOC51353}
{PS51353; ARSC}
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* Arsenate reductase arsC family profile *
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Several  bacterial  taxon have a chromosomal resistance system, encoded by the
ars  operon, for the detoxification of arsenate, arsenite, and antimonite [1].
This  system  transports  arsenite  and  antimonite out of the cell. Arsenate,
however,  must  first be reduced to arsenite before it is extruded. ArsC is an
~150-residue arsenate reductase that uses reduced glutathione (GSH) to convert
arsenate  to arsenite with a redox active cysteine residue in the active site.
ArsC forms an active quaternary complex with GSH, arsenate, and glutaredoxin 1
(Grx1).  The  three  ligands  must  be present simultaneously for reduction to
occur [2].

The  arsC  family  also  comprises  the  Spx  proteins which are GRAM-positive
bacterial  transcription  factors  that regulate the transcription of multiple
genes in response to disulfide stress [3].

The arsC protein structure has been solved (see <PDB:1I9D>) [4]. It belongs to
the  thioredoxin  superfamily  fold  which  is  defined  by  a beta-sheet core
surrounded by alpha-helices. The active cysteine residue of ArsC is located in
the  loop  between  the  first  beta-strand and the first helix, which is also
conserved in the Spx protein and its homologs.

The profile we developed covers the whole arsC conserved region.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: December 2007 / First entry.

[ 1] Carlin A., Shi W., Dey S., Rosen B.P.
     "The ars operon of Escherichia coli confers arsenical and antimonial
     resistance."
     J. Bacteriol. 177:981-986(1995).
     PubMed=7860609
[ 2] Liu J., Rosen B.P.
     "Ligand interactions of the ArsC arsenate reductase."
     J. Biol. Chem. 272:21084-21089(1997).
     PubMed=9261111
[ 3] Zuber P.
     "Spx-RNA polymerase interaction and global transcriptional control
     during oxidative stress."
     J. Bacteriol. 186:1911-1918(2004).
     PubMed=15028674
[ 4] Martin P., DeMel S., Shi J., Gladysheva T., Gatti D.L., Rosen B.P.,
     Edwards B.F.
     "Insights into the structure, solvation, and mechanism of ArsC
     arsenate reductase, a novel arsenic detoxification enzyme."
     Structure 9:1071-1081(2001).
     PubMed=11709171

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