ID   ARSC2_STAS1             Reviewed;         131 AA.
AC   Q49UH1;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   16-JUN-2009, entry version 30.
DE   RecName: Full=Protein arsC 2;
DE   AltName: Full=Arsenate reductase 2;
DE            EC=1.20.4.-;
DE   AltName: Full=Arsenical pump modifier 2;
DE   AltName: Full=Low molecular weight protein-tyrosine-phosphatase 2;
DE            EC=3.1.3.48;
GN   Name=arsC2; OrderedLocusNames=SSPP114;
OS   Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 /
OS   DSM 20229).
OG   Plasmid pSSP1.
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=342451;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16135568; DOI=10.1073/pnas.0502950102;
RA   Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K.,
RA   Higashide M., Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S.,
RA   Hattori M., Ohta T.;
RT   "Whole genome sequence of Staphylococcus saprophyticus reveals the
RT   pathogenesis of uncomplicated urinary tract infection.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(2005).
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; AP008935; BAE19605.1; -; Genomic_DNA.
DR   RefSeq; YP_302550.1; -.
DR   SMR; Q49UH1; 1-128.
DR   GeneID; 3617381; -.
DR   GenomeReviews; AP008935_GR; SSPP114.
DR   KEGG; ssp:SSPP114; -.
DR   NMPDR; fig|342451.4.peg.2460; -.
DR   HOGENOM; Q49UH1; -.
DR   OMA; Q49UH1; DSANDAC.
DR   BioCyc; SSAP342451:SSPP114-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; Plasmid; Redox-active center.
FT   CHAIN         1    131       Protein arsC 2.
FT                                /FTId=PRO_0000162533.
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;  14908 MW;  1B1C91593047D803 CRC64;
     MDKKTIYFIC TGNSCRSQMA EGWGREILGE EWNVYSAGIE THGVNPKAIE AMKEVDIDIS
     NHTSDLIDNK ILRQSDLVVT LCSDADENCP VIPPNVKKEH WGFDDPAGKS WSEFQRVRDE
     IGQKIKQFYD N
//