ID   ADPRH_STRP1             Reviewed;         270 AA.
AC   Q99ZI6; Q48YM4;
DT   16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 120.
DE   RecName: Full=Protein-ADP-ribose hydrolase {ECO:0000250|UniProtKB:P0DN70};
DE            Short=SpyMacroD {ECO:0000250|UniProtKB:P0DN70};
DE            EC=3.2.1.- {ECO:0000250|UniProtKB:P0DN70};
GN   OrderedLocusNames=SPy_1216, M5005_Spy0930;
OS   Streptococcus pyogenes serotype M1.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=301447;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700294 / SF370 / Serotype M1;
RX   PubMed=11296296; DOI=10.1073/pnas.071559398;
RA   Ferretti J.J., McShan W.M., Ajdic D.J., Savic D.J., Savic G., Lyon K.,
RA   Primeaux C., Sezate S., Suvorov A.N., Kenton S., Lai H.S., Lin S.P.,
RA   Qian Y., Jia H.G., Najar F.Z., Ren Q., Zhu H., Song L., White J., Yuan X.,
RA   Clifton S.W., Roe B.A., McLaughlin R.E.;
RT   "Complete genome sequence of an M1 strain of Streptococcus pyogenes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:4658-4663(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-947 / MGAS5005 / Serotype M1;
RX   PubMed=16088826; DOI=10.1086/432514;
RA   Sumby P., Porcella S.F., Madrigal A.G., Barbian K.D., Virtaneva K.,
RA   Ricklefs S.M., Sturdevant D.E., Graham M.R., Vuopio-Varkila J., Hoe N.P.,
RA   Musser J.M.;
RT   "Evolutionary origin and emergence of a highly successful clone of serotype
RT   M1 group A Streptococcus involved multiple horizontal gene transfer
RT   events.";
RL   J. Infect. Dis. 192:771-782(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   -!- 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:P0DN70};
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DR   EMBL; AE004092; AAK34075.1; -; Genomic_DNA.
DR   EMBL; CP000017; AAZ51548.1; -; Genomic_DNA.
DR   RefSeq; NP_269354.1; NC_002737.2.
DR   AlphaFoldDB; Q99ZI6; -.
DR   SMR; Q99ZI6; -.
DR   STRING; 1314.HKU360_00975; -.
DR   PaxDb; Q99ZI6; -.
DR   EnsemblBacteria; AAK34075; AAK34075; SPy_1216.
DR   KEGG; spy:SPy_1216; -.
DR   KEGG; spz:M5005_Spy0930; -.
DR   PATRIC; fig|160490.10.peg.1062; -.
DR   HOGENOM; CLU_046550_2_1_9; -.
DR   OMA; QGHEEPT; -.
DR   Proteomes; UP000000750; Chromosome.
DR   GO; GO:0004649; F:poly(ADP-ribose) glycohydrolase activity; ISS:UniProtKB.
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; Reference proteome.
FT   CHAIN           1..270
FT                   /note="Protein-ADP-ribose hydrolase"
FT                   /id="PRO_0000089217"
FT   DOMAIN          73..267
FT                   /note="Macro"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
SQ   SEQUENCE   270 AA;  30017 MW;  4FAA9F94422FFFB6 CRC64;
     MPSSFDLLGE MIGLLQTEQL TSSWACPLPN ALTKRQDLWR ALINQRPALP LSKDYLNLED
     AYLDDWRASF VPVSVKDCQK TNYTSLFLYH GDIRYLAVDA IVNAANSELL GCFSPNHGCI
     DNAIHTFAGS RLRLACQAIM TEQGRKEAIG QAKLTSAYHL PASYIIHTVG PRITKGHHVS
     PIRADLLARC YRSSLDLAVK AGLTSLAFCS ISTGEFGFPK KEAAQIAIKT VLKWQAEHPE
     SKTLTTIFNT FTSEDKALYD TYLQKENNCE