ID   ADPRH_STAAR             Reviewed;         266 AA.
AC   Q6GJZ1;
DT   21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Protein-ADP-ribose hydrolase {ECO:0000250|UniProtKB:P67343};
DE            Short=SpyMacroD {ECO:0000250|UniProtKB:P0DN70};
DE            EC=3.2.1.- {ECO:0000250|UniProtKB:P67343};
GN   OrderedLocusNames=SAR0322;
OS   Staphylococcus aureus (strain MRSA252).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282458;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MRSA252;
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA   Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA   Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA   Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA   Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT   for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
CC   -!- FUNCTION: ADP-ribose glycohydrolase that hydrolyzes ADP-ribosyl-
CC       cysteine bonds (By similarity). Specifically reverses the SirTM-
CC       mediated mono-ADP-ribosylation of GcvH-L, by releasing ADP-ribose from
CC       the target protein. May be involved in the modulation of the response
CC       to host-derived oxidative stress. {ECO:0000250|UniProtKB:P0DN70,
CC       ECO:0000250|UniProtKB:P67343}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-O-(ADP-D-ribosyl)-L-aspartyl-[protein] + H2O = ADP-D-ribose
CC         + H(+) + L-aspartyl-[protein]; Xref=Rhea:RHEA:54428, Rhea:RHEA-
CC         COMP:9867, Rhea:RHEA-COMP:13832, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29961, ChEBI:CHEBI:57967,
CC         ChEBI:CHEBI:138102; Evidence={ECO:0000250|UniProtKB:P67343};
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DR   EMBL; BX571856; CAG39346.1; -; Genomic_DNA.
DR   RefSeq; WP_000449073.1; NC_002952.2.
DR   AlphaFoldDB; Q6GJZ1; -.
DR   SMR; Q6GJZ1; -.
DR   PRIDE; Q6GJZ1; -.
DR   KEGG; sar:SAR0322; -.
DR   HOGENOM; CLU_046550_2_1_9; -.
DR   OMA; AQRFSND; -.
DR   OrthoDB; 1812319at2; -.
DR   Proteomes; UP000000596; Chromosome.
DR   GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd02906; Macro_1; 1.
DR   Gene3D; 3.40.220.10; -; 1.
DR   InterPro; IPR035801; Macro_1.
DR   InterPro; IPR002589; Macro_dom.
DR   InterPro; IPR043472; Macro_dom-like.
DR   Pfam; PF01661; Macro; 1.
DR   SMART; SM00506; A1pp; 1.
DR   SUPFAM; SSF52949; SSF52949; 1.
DR   PROSITE; PS51154; MACRO; 1.
PE   3: Inferred from homology;
KW   Glycosidase; Hydrolase.
FT   CHAIN           1..266
FT                   /note="Protein-ADP-ribose hydrolase"
FT                   /id="PRO_0000089211"
FT   DOMAIN          74..265
FT                   /note="Macro"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
SQ   SEQUENCE   266 AA;  30135 MW;  905E9B1542415BE9 CRC64;
     METLKSNKAR LEYLINDMRR ERNDNDVLVM PSSFEDLWEL YRGLANVRPA LPVSDEYLAV
     QDAMLSDLNR QHVTDLKDLK PIKGDNIFVW QGDITTLKID AIVNAANSRF LGCMQANHDC
     IDNIIHTKAG VQVRLDCAEI IRQQGRNEGV GKAKITRGYN LPAKYIIHTV GPQIRRLPVS
     KLNQDLLAKC YLSCLKLADQ QSLNHIAFCC ISTGVFAFPQ DEAAEIAVRT VESYLKETNS
     TLKVVFNVFT DKDLQLYKEA FNRDAE