NPD_STAES
ID NPD_STAES Reviewed; 246 AA.
AC Q8CNF4;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 115.
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=SE_1789;
OS Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176280;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12228 / FDA PCI 1200;
RX PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT "Genome-based analysis of virulence genes in a non-biofilm-forming
RT Staphylococcus epidermidis strain (ATCC 12228).";
RL Mol. Microbiol. 49:1577-1593(2003).
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}.
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DR EMBL; AE015929; AAO05430.1; -; Genomic_DNA.
DR RefSeq; NP_765344.1; NC_004461.1.
DR RefSeq; WP_001829706.1; NZ_WBME01000007.1.
DR AlphaFoldDB; Q8CNF4; -.
DR SMR; Q8CNF4; -.
DR STRING; 176280.SE_1789; -.
DR EnsemblBacteria; AAO05430; AAO05430; SE_1789.
DR GeneID; 50018107; -.
DR KEGG; sep:SE_1789; -.
DR PATRIC; fig|176280.10.peg.1746; -.
DR eggNOG; COG0846; Bacteria.
DR HOGENOM; CLU_023643_3_0_9; -.
DR OMA; SMQVYPA; -.
DR Proteomes; UP000001411; 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..246
FT /note="NAD-dependent protein deacetylase"
FT /id="PRO_0000110357"
FT DOMAIN 7..246
FT /note="Deacetylase sirtuin-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01968"
FT ACT_SITE 124
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01968"
FT BINDING 24..43
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01968"
FT BINDING 106..109
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01968"
FT BINDING 132
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01968"
FT BINDING 135
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01968"
FT BINDING 152
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01968"
FT BINDING 155
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01968"
FT BINDING 192..194
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01968"
FT BINDING 216..218
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01968"
SQ SEQUENCE 246 AA; 27695 MW; 3EF0E6BE1DA00045 CRC64;
MKKPDIQQLK DIVNNSNQIV FFTGAGVSVA SGIPDFRSMG GLYDEISKDG QSPEYLLSID
HLHDNKESFI NFYHERLLIA DKKPNIVHQW IAQLENQQKS LGVITQNIDG LHEDAGSHNI
DELHGTLNRF YCINCYEEYS KSYVMTHHLK YCEKCGNVIR PDIVLYGEML NQKTVFKALD
KIQHADTLIV LGSSLVVQPA AGFVSEFKGD NLVIINRDAT PYDHTASLVI HDDMTSVIEE
IVNSNS
