NPD_STAAW
ID NPD_STAAW Reviewed; 243 AA.
AC Q8NVC8;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=NAD-dependent protein deacetylase {ECO:0000255|HAMAP-Rule:MF_01968};
DE EC=2.3.1.286 {ECO:0000255|HAMAP-Rule:MF_01968};
DE AltName: Full=Regulatory protein SIR2 homolog {ECO:0000255|HAMAP-Rule:MF_01968};
GN Name=cobB {ECO:0000255|HAMAP-Rule:MF_01968}; OrderedLocusNames=MW2123;
OS Staphylococcus aureus (strain MW2).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=196620;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MW2;
RX PubMed=12044378; DOI=10.1016/s0140-6736(02)08713-5;
RA Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y.,
RA Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
RT "Genome and virulence determinants of high virulence community-acquired
RT MRSA.";
RL Lancet 359:1819-1827(2002).
CC -!- FUNCTION: NAD-dependent protein deacetylase which modulates the
CC activities of several enzymes which are inactive in their acetylated
CC form. {ECO:0000255|HAMAP-Rule:MF_01968}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(6)-acetyl-L-lysyl-[protein] + NAD(+) = 2''-O-acetyl-
CC ADP-D-ribose + L-lysyl-[protein] + nicotinamide;
CC Xref=Rhea:RHEA:43636, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10731,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:61930, ChEBI:CHEBI:83767;
CC EC=2.3.1.286; Evidence={ECO:0000255|HAMAP-Rule:MF_01968};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01968};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01968};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01968}.
CC -!- SIMILARITY: Belongs to the sirtuin family. Class U subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01968}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BA000033; BAB95988.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8NVC8; -.
DR SMR; Q8NVC8; -.
DR EnsemblBacteria; BAB95988; BAB95988; BAB95988.
DR KEGG; sam:MW2123; -.
DR HOGENOM; CLU_023643_3_0_9; -.
DR OMA; SMQVYPA; -.
DR Proteomes; UP000000418; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0070403; F:NAD+ binding; IEA:UniProtKB-UniRule.
DR GO; GO:0034979; F:NAD-dependent protein deacetylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006476; P:protein deacetylation; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.1600.10; -; 1.
DR HAMAP; MF_01968; Sirtuin_ClassU; 1.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR003000; Sirtuin.
DR InterPro; IPR026591; Sirtuin_cat_small_dom_sf.
DR InterPro; IPR028628; Sirtuin_class_U.
DR InterPro; IPR026590; Ssirtuin_cat_dom.
DR Pfam; PF02146; SIR2; 1.
DR SUPFAM; SSF52467; SSF52467; 1.
DR PROSITE; PS50305; SIRTUIN; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Metal-binding; NAD; Transferase; Zinc.
FT CHAIN 1..243
FT /note="NAD-dependent protein deacetylase"
FT /id="PRO_0000110356"
FT DOMAIN 6..243
FT /note="Deacetylase sirtuin-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01968"
FT ACT_SITE 123
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01968"
FT BINDING 23..42
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01968"
FT BINDING 105..108
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01968"
FT BINDING 131
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01968"
FT BINDING 134
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01968"
FT BINDING 151
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01968"
FT BINDING 154
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01968"
FT BINDING 191..193
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01968"
FT BINDING 215..217
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01968"
SQ SEQUENCE 243 AA; 27088 MW; 6303BBD01672EB67 CRC64;
MRNDLETLKH IIDSSNRITF FTGAGVSVAS GVPDFRSMGG LFDEISKDGL SPEYLLSRDY
LEDDPEGFIN FCHKRLLFVD TKPNIVHDWI AKLERNQQSL GVITQNIDGL HSDAGSQHVD
ELHGTLNRFY CNACHKSYTK SDVIDRTLKH CDNCGGAIRP DIVLYGEMLD QPTIIRSLNK
IEHADTLVVL GSSLVVQPAA GLISNFKGDN LIIINKDRTP YDRDATLVIH DDMVSVVKSL
MTE
