ID   ARSC_STAES              Reviewed;         131 AA.
AC   Q8CQF5;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   16-JUN-2009, entry version 39.
DE   RecName: Full=Protein arsC;
DE   AltName: Full=Arsenate reductase;
DE            EC=1.20.4.-;
DE   AltName: Full=Arsenical pump modifier;
DE   AltName: Full=Low molecular weight protein-tyrosine-phosphatase;
DE            EC=3.1.3.48;
GN   Name=arsC; OrderedLocusNames=SE_0134;
OS   Staphylococcus epidermidis (strain ATCC 12228).
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=176280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=22832016; PubMed=12950922;
RX   DOI=10.1046/j.1365-2958.2003.03671.x;
RA   Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J.,
RA   Qin Z.-Q., Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z.,
RA   Yuan Z.-H., Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT   "Genome-based analysis of virulence genes in a non-biofilm-forming
RT   Staphylococcus epidermidis strain (ATCC 12228).";
RL   Mol. Microbiol. 49:1577-1593(2003).
CC   -!- FUNCTION: Reduces arsenate [As(V)] to arsenite [As(III)] and
CC       dephosphorylates tyrosine phosphorylated proteins, low-MW aryl
CC       phosphates and natural and synthetic acyl phosphates. Could switch
CC       between different functions in different circumstances (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
CC       tyrosine + phosphate.
CC   -!- CATALYTIC ACTIVITY: Arsenate + thioredoxin = arsenite +
CC       thioredoxin disulfide + H(2)O.
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SIMILARITY: Belongs to the low molecular weight phosphotyrosine
CC       protein phosphatase superfamily. ArsC family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AE015929; AAO03731.1; -; Genomic_DNA.
DR   RefSeq; NP_763689.1; -.
DR   HSSP; P30330; 1LJL.
DR   SMR; Q8CQF5; 1-131.
DR   GeneID; 1056548; -.
DR   GenomeReviews; AE015929_GR; SE_0134.
DR   KEGG; sep:SE0134; -.
DR   HOGENOM; Q8CQF5; -.
DR   OMA; Q8CQF5; EMRIVIT.
DR   BioCyc; SEPI176280:SE_0134-MON; -.
DR   GO; GO:0030612; F:arsenate reductase (thioredoxin) activity; IEA:HAMAP.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:HAMAP.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0006470; P:protein amino acid dephosphorylation; IEA:InterPro.
DR   GO; GO:0046685; P:response to arsenic; IEA:UniProtKB-KW.
DR   HAMAP; MF_01624; -; 1.
DR   InterPro; IPR014064; Arsenate_reductase_StaphA.
DR   InterPro; IPR017867; Tyr_phospatase_low_mol_wt.
DR   PANTHER; PTHR11717; Low_mwt_PTPase; 1.
DR   Pfam; PF01451; LMWPc; 1.
DR   SMART; SM00226; LMWPc; 1.
DR   TIGRFAMs; TIGR02691; arsC_pI258_fam; 1.
PE   3: Inferred from homology;
KW   Arsenical resistance; Complete proteome; Disulfide bond; Hydrolase;
KW   Oxidoreductase; Redox-active center.
FT   CHAIN         1    131       Protein arsC.
FT                                /FTId=PRO_0000162527.
FT   ACT_SITE     10     10       Nucleophile; for reductase activity and
FT                                phosphatase activity (By similarity).
FT   ACT_SITE     82     82       Nucleophile; for reductase activity (By
FT                                similarity).
FT   ACT_SITE     89     89       Nucleophile; for reductase activity (By
FT                                similarity).
FT   DISULFID     10     82       Redox-active; alternate (By similarity).
FT   DISULFID     82     89       Redox-active; alternate (By similarity).
SQ   SEQUENCE   131 AA;  14693 MW;  405C72DCE141F55C CRC64;
     MDKKTIYFIC TGNSCRSQMA EGWGKKILGD EWQVYSGGIE AHGVNPKAIE AMKEVGIDIS
     NHTSNLIDQN ILHQSDLVVT LCSDADKNCP ILPPSVKKEH WGFDDPAGKP WSEFQRVRDE
     IKTAIESFKT R
//