SIRTM_STAAM
ID SIRTM_STAAM Reviewed; 315 AA.
AC A0A0H3JQ59;
DT 20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 1.
DT 03-AUG-2022, entry version 28.
DE RecName: Full=Protein ADP-ribosyltransferase {ECO:0000303|PubMed:26166706};
DE EC=2.4.2.- {ECO:0000269|PubMed:26166706};
DE AltName: Full=Sirtuin class M {ECO:0000303|PubMed:26166706};
DE Short=SirTM {ECO:0000303|PubMed:26166706};
GN OrderedLocusNames=SAV0326 {ECO:0000312|EMBL:BAB56488.1};
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, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, LACK OF PROTEIN
RP DEACYLASE ACTIVITY, ACTIVITY REGULATION, AND MUTAGENESIS OF ASN-124.
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: Catalyzes specifically the mono-ADP-ribosylation of GcvH-L
CC (SAV0324). This activity is dependent on prior lipoylation of the
CC target protein. May be involved in the modulation of the response to
CC host-derived oxidative stress. In contrast to other sirtuin classes,
CC lacks protein deacylase activity, being unable to catalyze
CC delipoylation, debiotinylation, deacetylation and desuccinylation of
CC proteins. {ECO:0000269|PubMed:26166706}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-aspartyl-[protein] + NAD(+) = 4-O-(ADP-D-ribosyl)-L-
CC aspartyl-[protein] + nicotinamide; Xref=Rhea:RHEA:54424, Rhea:RHEA-
CC COMP:9867, Rhea:RHEA-COMP:13832, ChEBI:CHEBI:17154,
CC ChEBI:CHEBI:29961, ChEBI:CHEBI:57540, ChEBI:CHEBI:138102;
CC Evidence={ECO:0000269|PubMed:26166706};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P0DN71};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P0DN71};
CC -!- ACTIVITY REGULATION: Is inhibited by Tenovin-6 in vitro, but not by
CC nicotinamide. {ECO:0000269|PubMed:26166706}.
CC -!- MISCELLANEOUS: The SirTM-mediated ADP-ribosylation can be specifically
CC reversed by the Macro domain-containing protein encoded by the same
CC operon (SAV0325). {ECO:0000269|PubMed:26166706}.
CC -!- SIMILARITY: Belongs to the sirtuin family. Class M subfamily.
CC {ECO:0000305|PubMed:26166706}.
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DR EMBL; BA000017; BAB56488.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0H3JQ59; -.
DR SMR; A0A0H3JQ59; -.
DR PaxDb; A0A0H3JQ59; -.
DR EnsemblBacteria; BAB56488; BAB56488; SAV0326.
DR KEGG; sav:SAV0326; -.
DR HOGENOM; CLU_071599_0_0_9; -.
DR OMA; QGDYGLW; -.
DR Proteomes; UP000002481; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:1990404; F:NAD+-protein ADP-ribosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0006471; P:protein ADP-ribosylation; IDA:UniProtKB.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR026590; Ssirtuin_cat_dom.
DR SUPFAM; SSF52467; SSF52467; 1.
DR PROSITE; PS50305; SIRTUIN; 1.
PE 1: Evidence at protein level;
KW Glycosyltransferase; Metal-binding; NAD; Nucleotidyltransferase;
KW Transferase; Zinc.
FT CHAIN 1..315
FT /note="Protein ADP-ribosyltransferase"
FT /id="PRO_0000435345"
FT DOMAIN 22..315
FT /note="Deacetylase sirtuin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT BINDING 40
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P0DN71"
FT BINDING 123..126
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P0DN71"
FT BINDING 143
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P0DN71"
FT BINDING 151
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P0DN71"
FT BINDING 155
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P0DN71"
FT BINDING 186
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P0DN71"
FT BINDING 189
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P0DN71"
FT BINDING 238..240
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P0DN71"
FT BINDING 264
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P0DN71"
FT BINDING 268
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P0DN71"
FT BINDING 285
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P0DN71"
FT MUTAGEN 124
FT /note="N->A: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:26166706"
SQ SEQUENCE 315 AA; 36549 MW; D04202AA594CA796 CRC64;
MMQSSKWNAM SLLMDEKTKQ AEVLRTAIDE ADAIVIGIGA GMSASDGFTY VGERFTENFP
DFIEKYRFFD MLQASLHPYG SWQEYWAFES RFITLNYLDQ PVGQSYLALK SLVEGKQYHI
ITTNADNAFD AAEYDMTHVF HIQGEYILQQ CSQHCHAQTY RNDDLIRKMV VAQQDMLIPW
EMIPRCPKCD APMEVNKRKA EVGMVEDAEF HAQLQRYNAF LEQHQDDKVL YLEIGIGYTT
PQFVKHPFQR MTRKNENAIY MTMNKKAYRI PNSIQERTIH LTEDISTLIT TALRNDSTTQ
NNNIGETEDV LNRTD
