ADPRH_STAAM
ID ADPRH_STAAM Reviewed; 266 AA.
AC P67343; Q99WQ1;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Protein-ADP-ribose hydrolase {ECO:0000305|PubMed:26166706};
DE Short=SpyMacroD {ECO:0000250|UniProtKB:P0DN70};
DE EC=3.2.1.- {ECO:0000269|PubMed:26166706};
GN OrderedLocusNames=SAV0325;
OS Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=158878;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mu50 / ATCC 700699;
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).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=Mu50 / ATCC 700699;
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).
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 (SAV0324), by releasing ADP-
CC ribose from the target protein. May be involved in the modulation of
CC the response to host-derived oxidative stress.
CC {ECO:0000250|UniProtKB:P0DN70, ECO:0000269|PubMed:26166706}.
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: Directly interacts with the lipoylated form of GcvH-L.
CC {ECO:0000250|UniProtKB:P0DN70}.
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DR EMBL; BA000017; BAB56487.1; -; Genomic_DNA.
DR RefSeq; WP_000449069.1; NC_002758.2.
DR AlphaFoldDB; P67343; -.
DR SMR; P67343; -.
DR PaxDb; P67343; -.
DR EnsemblBacteria; BAB56487; BAB56487; SAV0325.
DR KEGG; sav:SAV0325; -.
DR HOGENOM; CLU_046550_2_1_9; -.
DR OMA; AQRFSND; -.
DR PhylomeDB; P67343; -.
DR BioCyc; SAUR158878:SAV_RS01810-MON; -.
DR Proteomes; UP000002481; Chromosome.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; 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..266
FT /note="Protein-ADP-ribose hydrolase"
FT /id="PRO_0000089209"
FT DOMAIN 74..265
FT /note="Macro"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
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