ADPRH_STAAS
ID ADPRH_STAAS Reviewed; 266 AA.
AC Q6GCE6;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-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=SAS0302;
OS Staphylococcus aureus (strain MSSA476).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=282459;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MSSA476;
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; BX571857; CAG42073.1; -; Genomic_DNA.
DR RefSeq; WP_000449060.1; NC_002953.3.
DR AlphaFoldDB; Q6GCE6; -.
DR SMR; Q6GCE6; -.
DR KEGG; sas:SAS0302; -.
DR HOGENOM; CLU_046550_2_1_9; -.
DR OMA; AQRFSND; -.
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_0000089212"
FT DOMAIN 74..265
FT /note="Macro"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
SQ SEQUENCE 266 AA; 30129 MW; 11D8AD2AABA3C083 CRC64;
METLKSNKAR LEYLINDMHR ERNDNDVLVM PSSFEDLWEL YRGLANVRPA LPVSDEYLAV
QDAMLSDLNR QHVTDLKDLK PIKGDNIFVW QGDITTLKID AIVNAANSRF LGCMQANHDC
IDNIIHTKAG VQVRLDCAEI IRQQGRNEGV GKAKITRGYN LPAKYIIHTV GPQIRRLPVS
KMNQDLLAKC YLSCLKLADQ HSLNHVAFCC ISTGVFAFPQ DEAAEIAVRT VESYLKETNS
TLKVVFNVFT DKDLQLYKEA FNRDAE