ID   ADPRH_STAAN             Reviewed;         266 AA.
AC   P67344; Q99WQ1;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   25-MAY-2022, entry version 86.
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=SA0314;
OS   Staphylococcus aureus (strain N315).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=158879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=N315;
RX   PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA   Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA   Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA   Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA   Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA   Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA   Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA   Hiramatsu K.;
RT   "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL   Lancet 357:1225-1240(2001).
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; BA000018; BAB41538.1; -; Genomic_DNA.
DR   PIR; G89797; G89797.
DR   RefSeq; WP_000449069.1; NC_002745.2.
DR   PDB; 5KIV; X-ray; 1.75 A; A=1-266.
DR   PDBsum; 5KIV; -.
DR   AlphaFoldDB; P67344; -.
DR   SMR; P67344; -.
DR   EnsemblBacteria; BAB41538; BAB41538; BAB41538.
DR   KEGG; sau:SA0314; -.
DR   HOGENOM; CLU_046550_2_1_9; -.
DR   OMA; AQRFSND; -.
DR   Proteomes; UP000000751; 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   1: Evidence at protein level;
KW   3D-structure; Glycosidase; Hydrolase.
FT   CHAIN           1..266
FT                   /note="Protein-ADP-ribose hydrolase"
FT                   /id="PRO_0000089210"
FT   DOMAIN          74..265
FT                   /note="Macro"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT   HELIX           1..20
FT                   /evidence="ECO:0007829|PDB:5KIV"
FT   HELIX           34..47
FT                   /evidence="ECO:0007829|PDB:5KIV"
FT   HELIX           55..69
FT                   /evidence="ECO:0007829|PDB:5KIV"
FT   TURN            70..72
FT                   /evidence="ECO:0007829|PDB:5KIV"
FT   HELIX           76..78
FT                   /evidence="ECO:0007829|PDB:5KIV"
FT   TURN            84..86
FT                   /evidence="ECO:0007829|PDB:5KIV"
FT   STRAND          87..92
FT                   /evidence="ECO:0007829|PDB:5KIV"
FT   HELIX           94..96
FT                   /evidence="ECO:0007829|PDB:5KIV"
FT   STRAND          97..106
FT                   /evidence="ECO:0007829|PDB:5KIV"
FT   HELIX           121..129
FT                   /evidence="ECO:0007829|PDB:5KIV"
FT   HELIX           131..144
FT                   /evidence="ECO:0007829|PDB:5KIV"
FT   STRAND          154..157
FT                   /evidence="ECO:0007829|PDB:5KIV"
FT   STRAND          161..170
FT                   /evidence="ECO:0007829|PDB:5KIV"
FT   STRAND          176..178
FT                   /evidence="ECO:0007829|PDB:5KIV"
FT   HELIX           181..200
FT                   /evidence="ECO:0007829|PDB:5KIV"
FT   STRAND          204..208
FT                   /evidence="ECO:0007829|PDB:5KIV"
FT   HELIX           220..238
FT                   /evidence="ECO:0007829|PDB:5KIV"
FT   STRAND          243..248
FT                   /evidence="ECO:0007829|PDB:5KIV"
FT   HELIX           251..261
FT                   /evidence="ECO:0007829|PDB:5KIV"
SQ   SEQUENCE   266 AA;  30110 MW;  5BB7528F6BC4F16B CRC64;
     METLKSNKAR LEYLINDMRR ERNDNDVLVM PSSFEDLWEL YRGLANVRPA LPVSDEYLAV
     QDAMLSDLNH QHVTDLKDLK PIKGDNIFVW QGDITTLKID AIVNAANSRF LGCMQANHDC
     IDNIIHTKAG VQVRLDCAEI IRQQGRNEGV GKAKKTRGYN LPAKYIIHTV GPQIRRLPVS
     KMNQDLLAKC YLSCLKLADQ HSLNHVAFCC ISTGVFAFPQ DEAAEIAVRT VESYLKETNS
     TLKVVFNVFT DKDLQLYKEA LNRDAE