ID   ADPRH_STAAC             Reviewed;         266 AA.
AC   Q5HIW9;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 88.
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=SACOL0396;
OS   Staphylococcus aureus (strain COL).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93062;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=COL;
RX   PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA   Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA   Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA   Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA   Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA   Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA   Fraser C.M.;
RT   "Insights on evolution of virulence and resistance from the complete genome
RT   analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT   a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT   strain.";
RL   J. Bacteriol. 187:2426-2438(2005).
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; CP000046; AAW38865.1; -; Genomic_DNA.
DR   RefSeq; WP_000449061.1; NC_002951.2.
DR   AlphaFoldDB; Q5HIW9; -.
DR   SMR; Q5HIW9; -.
DR   EnsemblBacteria; AAW38865; AAW38865; SACOL0396.
DR   KEGG; sac:SACOL0396; -.
DR   HOGENOM; CLU_046550_2_1_9; -.
DR   OMA; AQRFSND; -.
DR   Proteomes; UP000000530; 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_0000089208"
FT   DOMAIN          74..265
FT                   /note="Macro"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
SQ   SEQUENCE   266 AA;  30118 MW;  122891D9649F30BC CRC64;
     METLKSNKAR LEYLINDMHR ERNDNDVLVM PSSFEDLWEL YRGLANVRPA LPVSDEYLAV
     QDAMLSDLNR QHVTDLKDLK PIKGDNIFVW QGDITTLKID AIVNAANSRF LGCMQANHDC
     IDNIIHTKAG VQVRLDCAEI IRQQGRNEGV GKAKITRGYN LSAKYIIHTV GPQIRRLPVS
     KMNQDLLAKC YLSCLKLADQ HSLNHVAFCC ISTGVFAFPQ DEAAEIAVRT VESYLKETNS
     TLKVVFNVFT DKDLQLYKEA FNRDAE