ID A0A0D6A1B5_9LACO Unreviewed; 234 AA.
AC A0A0D6A1B5;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=protein acetyllysine N-acetyltransferase {ECO:0000256|ARBA:ARBA00012928};
DE EC=2.3.1.286 {ECO:0000256|ARBA:ARBA00012928};
GN ORFNames=GJR85_07565 {ECO:0000313|EMBL:QGV05238.1}, LBAT_0137
GN {ECO:0000313|EMBL:BAQ56526.1};
OS Lactobacillus acetotolerans.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=1600 {ECO:0000313|EMBL:BAQ56526.1, ECO:0000313|Proteomes:UP000035709};
RN [1] {ECO:0000313|EMBL:BAQ56526.1, ECO:0000313|Proteomes:UP000035709}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 13120 {ECO:0000313|EMBL:BAQ56526.1,
RC ECO:0000313|Proteomes:UP000035709};
RA Toh H., Morita H., Fujita N.;
RT "Complete genome sequence of Lactobacillus acetotolerans NBRC 13120.";
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:QGV05238.1, ECO:0000313|Proteomes:UP000427729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CN247 {ECO:0000313|EMBL:QGV05238.1,
RC ECO:0000313|Proteomes:UP000427729};
RA Luan C.;
RT "Complete genome sequence and characteristic analysis of beer-spoilage
RT bacterium Lactobacillus acetotolerans cn247.";
RL Submitted (DEC-2019) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; AP014808; BAQ56526.1; -; Genomic_DNA.
DR EMBL; CP046528; QGV05238.1; -; Genomic_DNA.
DR RefSeq; WP_060459070.1; NZ_WNWN01000042.1.
DR STRING; 1600.LBAT_0137; -.
DR KEGG; lae:LBAT_0137; -.
DR PATRIC; fig|1600.4.peg.141; -.
DR OrthoDB; 9800582at2; -.
DR Proteomes; UP000035709; Chromosome.
DR Proteomes; UP000427729; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.1600.10; SIR2/SIRT2 'Small Domain; 1.
DR Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR003000; Sirtuin.
DR InterPro; IPR026591; Sirtuin_cat_small_dom_sf.
DR InterPro; IPR026590; Ssirtuin_cat_dom.
DR PANTHER; PTHR11085:SF12; NAD-DEPENDENT PROTEIN DEACYLASE SIRTUIN-5, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11085; NAD-DEPENDENT PROTEIN DEACYLASE SIRTUIN-5, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF02146; SIR2; 1.
DR SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR PROSITE; PS50305; SIRTUIN; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00236};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000035709};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00236}.
FT DOMAIN 1..234
FT /note="Deacetylase sirtuin-type"
FT /evidence="ECO:0000259|PROSITE:PS50305"
FT ACT_SITE 120
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 128
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 131
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 146
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 149
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
SQ SEQUENCE 234 AA; 25992 MW; 9BB90C6D48C427B4 CRC64;
MTDSKQITAL KEDIKNAKHV VFLTGAGVST HSGIPDYRSK NGIYNGVSES PETILSEDTL
FNRPDFFYKF VMNNMYFPHA KPNLIHQKIT EICNEKGSLI TQNVDGLDKK SGNKDVTEFH
GSLYNIYCTK CHKPVSYEEY AKSYRHENCG GIIRPGIVLY GEAINPENLS KSVNAMQNSD
LVIISGTSFV VYPFAQLLAY RQAGAKVWAI NKTEIPAAGI NSIIGDALDV FKQL
//
