ID   ADPRH_STRPG             Reviewed;         270 AA.
AC   P0DN70;
DT   20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT   20-JAN-2016, sequence version 1.
DT   25-MAY-2022, entry version 21.
DE   RecName: Full=Protein-ADP-ribose hydrolase {ECO:0000305|PubMed:26166706};
DE            Short=SpyMacroD {ECO:0000303|PubMed:33769608};
DE            EC=3.2.1.- {ECO:0000269|PubMed:26166706};
GN   OrderedLocusNames=SpyM50868 {ECO:0000312|EMBL:CAM30196.1};
OS   Streptococcus pyogenes serotype M5 (strain Manfredo).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=160491;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Manfredo;
RX   PubMed=17012393; DOI=10.1128/jb.01227-06;
RA   Holden M.T.G., Scott A., Cherevach I., Chillingworth T., Churcher C.,
RA   Cronin A., Dowd L., Feltwell T., Hamlin N., Holroyd S., Jagels K.,
RA   Moule S., Mungall K., Quail M.A., Price C., Rabbinowitsch E., Sharp S.,
RA   Skelton J., Whitehead S., Barrell B.G., Kehoe M., Parkhill J.;
RT   "Complete genome of acute rheumatic fever-associated serotype M5
RT   Streptococcus pyogenes strain Manfredo.";
RL   J. Bacteriol. 189:1473-1477(2007).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND INTERACTION WITH GCVH-L.
RC   STRAIN=Manfredo;
RX   PubMed=26166706; DOI=10.1016/j.molcel.2015.06.013;
RA   Rack J.G., Morra R., Barkauskaite E., Kraehenbuehl R., Ariza A., Qu Y.,
RA   Ortmayer M., Leidecker O., Cameron D.R., Matic I., Peleg A.Y., Leys D.,
RA   Traven A., Ahel I.;
RT   "Identification of a class of protein ADP-ribosylating sirtuins in
RT   microbial pathogens.";
RL   Mol. Cell 59:309-320(2015).
RN   [3]
RP   FUNCTION.
RX   PubMed=33769608; DOI=10.1002/chem.202100337;
RA   Voorneveld J., Rack J.G.M., van Gijlswijk L., Meeuwenoord N.J., Liu Q.,
RA   Overkleeft H.S., van der Marel G.A., Ahel I., Filippov D.V.;
RT   "Molecular Tools for the Study of ADP-Ribosylation: A Unified and Versatile
RT   Method to Synthesise Native Mono-ADP-Ribosylated Peptides.";
RL   Chemistry 27:10621-10627(2021).
CC   -!- FUNCTION: ADP-ribose glycohydrolase that hydrolyzes ADP-ribosyl-
CC       cysteine bonds (PubMed:33769608). Specifically reverses the SirTM-
CC       mediated mono-ADP-ribosylation of GcvH-L (SpyM50867), by releasing ADP-
CC       ribose from the target protein (PubMed:26166706). May be involved in
CC       the modulation of the response to host-derived oxidative stress
CC       (PubMed:26166706). {ECO:0000269|PubMed:26166706,
CC       ECO:0000269|PubMed:33769608}.
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:0000269|PubMed:26166706};
CC   -!- SUBUNIT: Interacts with the lipoylated form of GcvH-L.
CC       {ECO:0000269|PubMed:26166706}.
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DR   EMBL; AM295007; CAM30196.1; -; Genomic_DNA.
DR   RefSeq; WP_011888850.1; NC_009332.1.
DR   AlphaFoldDB; P0DN70; -.
DR   SMR; P0DN70; -.
DR   KEGG; spf:SpyM50868; -.
DR   HOGENOM; CLU_046550_2_1_9; -.
DR   OMA; QGHEEPT; -.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IDA:UniProtKB.
DR   GO; GO:0004649; F:poly(ADP-ribose) glycohydrolase activity; IDA:UniProtKB.
DR   GO; GO:0051725; P:protein de-ADP-ribosylation; IDA:UniProtKB.
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   1: Evidence at protein level;
KW   Glycosidase; Hydrolase.
FT   CHAIN           1..270
FT                   /note="Protein-ADP-ribose hydrolase"
FT                   /id="PRO_0000435343"
FT   DOMAIN          73..267
FT                   /note="Macro"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
SQ   SEQUENCE   270 AA;  30239 MW;  D48E01EFF260BE1B CRC64;
     MPSSFDLLGE MIDLLQTEQL TSYWACPLPN ALTKRQDLWR ALINQRPALP LSKDYLNLED
     TYLDDWRASF VPVSVKDCQK TNYTSLFLYH GDIRYLAVDA IVNAANSELL GCFIPNHGCI
     DNAIHTFAGS RLRLACQAIM TEQGRKEAIG QAKLTSAYHL PASYIIHTVG PRITKGRHVS
     PIRADLLARC YRSSLDLAVK AGLTSLAFCS ISTGEFGFPK KEAAQIAIKT VLKWQAEHPE
     SKTLTIIFNT FTSEDKALYD TYLQKENNCE