ID   NAGD_STAA8              Reviewed;         259 AA.
AC   Q2FZX0;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Acid sugar phosphatase {ECO:0000250|UniProtKB:Q99VE8};
DE            EC=3.1.3.- {ECO:0000250|UniProtKB:Q99VE8};
GN   Name=nagD; OrderedLocusNames=SAOUHSC_00865;
OS   Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 8325 / PS 47;
RA   Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT   "The Staphylococcus aureus NCTC 8325 genome.";
RL   (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL   Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL   D.C. (2006).
RN   [2]
RP   VIRULENCE STUDIES.
RX   PubMed=15664928; DOI=10.1128/iai.73.2.872-877.2005;
RA   Begun J., Sifri C.D., Goldman S., Calderwood S.B., Ausubel F.M.;
RT   "Staphylococcus aureus virulence factors identified by using a high-
RT   throughput Caenorhabditis elegans-killing model.";
RL   Infect. Immun. 73:872-877(2005).
CC   -!- FUNCTION: Catalyzes the dephosphorylation of 2-6 carbon acid sugars in
CC       vitro. {ECO:0000250|UniProtKB:Q99VE8}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q99VE8};
CC   -!- MISCELLANEOUS: In murine kidney infection models nagD mutant was
CC       attenuated in virulence.
CC   -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. NagD family.
CC       {ECO:0000305}.
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DR   EMBL; CP000253; ABD29990.1; -; Genomic_DNA.
DR   RefSeq; WP_000816184.1; NZ_LS483365.1.
DR   RefSeq; YP_499418.1; NC_007795.1.
DR   AlphaFoldDB; Q2FZX0; -.
DR   SMR; Q2FZX0; -.
DR   STRING; 1280.SAXN108_0924; -.
DR   EnsemblBacteria; ABD29990; ABD29990; SAOUHSC_00865.
DR   GeneID; 3918995; -.
DR   KEGG; sao:SAOUHSC_00865; -.
DR   PATRIC; fig|93061.5.peg.786; -.
DR   eggNOG; COG0647; Bacteria.
DR   HOGENOM; CLU_043473_1_1_9; -.
DR   OMA; PPMHRET; -.
DR   Proteomes; UP000008816; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016791; F:phosphatase activity; IBA:GO_Central.
DR   Gene3D; 3.40.50.1000; -; 2.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR006357; HAD-SF_hydro_IIA.
DR   InterPro; IPR006354; HAD-SF_hydro_IIA_hyp1.
DR   InterPro; IPR023214; HAD_sf.
DR   Pfam; PF13344; Hydrolase_6; 1.
DR   PIRSF; PIRSF000915; PGP-type_phosphatase; 1.
DR   SUPFAM; SSF56784; SSF56784; 1.
DR   TIGRFAMs; TIGR01460; HAD-SF-IIA; 1.
DR   TIGRFAMs; TIGR01457; HAD-SF-IIA-hyp2; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Magnesium; Metal-binding; Reference proteome.
FT   CHAIN           1..259
FT                   /note="Acid sugar phosphatase"
FT                   /id="PRO_0000271223"
SQ   SEQUENCE   259 AA;  27946 MW;  F120BAB9E006C355 CRC64;
     MKQYKAYLID LDGTMYMGTD EIDGAKQFID YLNVKGIPHL YVTNNSTKTP EQVTEKLREM
     HIDAKPEEVV TSALATADYI SEQSPGASVY MLGGSGLNTA LTEAGLVIKN DEHVDYVVIG
     LDEQVTYEKL AIATLGVRNG ATFISTNPDV SIPKERGLLP GNGAITSVVS VSTGVSPQFI
     GKPEPIIMVK ALEILGLDKS EVAMVGDLYD TDIMSGINVG MDTIHVQTGV STLEDVQNKN
     VPPTYSFKDL NEAIAELEK