ID   ARSC_BACCZ              Reviewed;         134 AA.
AC   Q639D2;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   16-JUN-2009, entry version 31.
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=BCE33L2898;
OS   Bacillus cereus (strain ZK / E33L).
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=288681;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16621833; DOI=10.1128/JB.188.9.3382-3390.2006;
RA   Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S.,
RA   Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O.,
RA   Cleland C., Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T.,
RA   Goodwin L.A., Hill K.K., Hitchcock P., Jackson P.J., Keim P.,
RA   Kewalramani A.R., Longmire J., Lucas S., Malfatti S., McMurry K.,
RA   Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C.,
RA   Okinaka R.T., Parson-Quintana B., Reilly L.P., Richardson P.,
RA   Robinson D.L., Rubin E., Saunders E., Tapia R., Tesmer J.G.,
RA   Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L.,
RA   Brettin T.S., Gilna P.;
RT   "Pathogenomic sequence analysis of Bacillus cereus and Bacillus
RT   thuringiensis isolates closely related to Bacillus anthracis.";
RL   J. Bacteriol. 188:3382-3390(2006).
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.
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DR   EMBL; CP000001; AAU17365.1; -; Genomic_DNA.
DR   RefSeq; YP_084485.1; -.
DR   SMR; Q639D2; 5-134.
DR   GeneID; 3024191; -.
DR   GenomeReviews; CP000001_GR; BCE33L2898.
DR   KEGG; bcz:BCZK2898; -.
DR   HOGENOM; Q639D2; -.
DR   OMA; Q639D2; EVNIDIT.
DR   BioCyc; BCER288681:BCE33L2898-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    134       Protein arsC.
FT                                /FTId=PRO_0000162515.
FT   ACT_SITE     11     11       Nucleophile; for reductase activity and
FT                                phosphatase activity (By similarity).
FT   ACT_SITE     83     83       Nucleophile; for reductase activity (By
FT                                similarity).
FT   ACT_SITE     90     90       Nucleophile; for reductase activity (By
FT                                similarity).
FT   DISULFID     11     83       Redox-active; alternate (By similarity).
FT   DISULFID     83     90       Redox-active; alternate (By similarity).
SQ   SEQUENCE   134 AA;  15078 MW;  715F16EC0EA10F9D CRC64;
     MENKKTIYFL CTGNSCRSQM AEAWGKQYLG DKWNVYSAGI EVHGVNPNAI KAMNEVNIDI
     TNQTSDIIDA NILNRADLVV TLCSHADSVC PSTPPDVNRV HWGFDDPAGK EWSEFQRVRD
     EIGERIKRFS ETGE
//