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Literature summary for 2.3.1.48 extracted from

  • Carabetta, V.J.; Greco, T.M.; Cristea, I.M.; Dubnau, D.
    YfmK is an Nepsilon-lysine acetyltransferase that directly acetylates the histone-like protein HBsu in Bacillus subtilis (2019), Proc. Natl. Acad. Sci. USA, 116, 3752-3757 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.3.1.48

Cloned(Commentary)

Cloned (Comment) Organism
gene yfmK, recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) Bacillus subtilis

Protein Variants

Protein Variants Comment Organism
F124A site-directed mutagenesis Bacillus subtilis
F129A site-directed mutagenesis Bacillus subtilis
G88A site-directed mutagenesis, yfmKG88A is found to phenocopy the yfmK mutant most closely in vivo. HbsK41Q is able to bypass the yfmKG88A phenotype, suggesting that the cognate protein is catalytically inactive Bacillus subtilis
additional information generation of mutations that mimic the acetylated and unacetylated forms of the protein, resulting in the inability to acetylate key HBsu lysine residues leading to a more compacted nucleoid Bacillus subtilis
Y89A site-directed mutagenesis Bacillus subtilis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
acetyl-CoA + [HBsu]-L-lysine Bacillus subtilis essential histone-like protein HBsu contains seven acetylation sites in vivo, mutational analysis using mutants hbsK86Q, hbsK41Q, hbsK3Q, hbsK41R, and hbsK37R CoA + [HBsu]-N6-acetyl-L-lysine
-
 ?
acetyl-CoA + [HBsu]-L-lysine Bacillus subtilis 168 essential histone-like protein HBsu contains seven acetylation sites in vivo, mutational analysis using mutants hbsK86Q, hbsK41Q, hbsK3Q, hbsK41R, and hbsK37R CoA + [HBsu]-N6-acetyl-L-lysine
-
 ?
acetyl-CoA + [protein]-L-lysine Bacillus subtilis
-
 CoA + [protein]-N6-acetyl-L-lysine
-
 ?
acetyl-CoA + [protein]-L-lysine Bacillus subtilis 168
-
 CoA + [protein]-N6-acetyl-L-lysine
-
 ?

Organism

Organism UniProt Comment Textmining
Bacillus subtilis O34536
-
-
Bacillus subtilis 168 O34536
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
additional information YfmK does not acetylate itself Bacillus subtilis

Purification (Commentary)

Purification (Comment) Organism
recombinant wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by heparin affinity chromatography Bacillus subtilis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetyl-CoA + AVDSVFDTILDALK histone-like protein HBsu peptide Bacillus subtilis CoA + AVDSVFDTILDALKac
-
 ?
acetyl-CoA + AVDSVFDTILDALK histone-like protein HBsu peptide Bacillus subtilis 168 CoA + AVDSVFDTILDALKac
-
 ?
acetyl-CoA + VPAFKPGK histone-like protein HBsu peptide Bacillus subtilis CoA + VPAFKPGKac
-
 ?
acetyl-CoA + [HBsu]-L-lysine essential histone-like protein HBsu contains seven acetylation sites in vivo, mutational analysis using mutants hbsK86Q, hbsK41Q, hbsK3Q, hbsK41R, and hbsK37R Bacillus subtilis CoA + [HBsu]-N6-acetyl-L-lysine
-
 ?
acetyl-CoA + [HBsu]-L-lysine histone-like protein HBsu Bacillus subtilis CoA + [HBsu]-N6-acetyl-L-lysine
-
 ?
acetyl-CoA + [HBsu]-L-lysine essential histone-like protein HBsu contains seven acetylation sites in vivo, mutational analysis using mutants hbsK86Q, hbsK41Q, hbsK3Q, hbsK41R, and hbsK37R Bacillus subtilis 168 CoA + [HBsu]-N6-acetyl-L-lysine
-
 ?
acetyl-CoA + [HBsu]-L-lysine histone-like protein HBsu Bacillus subtilis 168 CoA + [HBsu]-N6-acetyl-L-lysine
-
 ?
acetyl-CoA + [protein]-L-lysine
-
 Bacillus subtilis CoA + [protein]-N6-acetyl-L-lysine
-
 ?
acetyl-CoA + [protein]-L-lysine
-
 Bacillus subtilis 168 CoA + [protein]-N6-acetyl-L-lysine
-
 ?
additional information quantification of HBsu acetylation by parallel reaction monitoring-tandem mass spectrometry Bacillus subtilis ?
-
-
additional information quantification of HBsu acetylation by parallel reaction monitoring-tandem mass spectrometry Bacillus subtilis 168 ?
-
-

Synonyms

Synonyms Comment Organism
KAT
-
 Bacillus subtilis
lysine acetyltransferase
-
 Bacillus subtilis
Nepsilon-lysine acetyltransferase
-
 Bacillus subtilis
YfmK
-
 Bacillus subtilis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Bacillus subtilis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 assay at Bacillus subtilis

Cofactor

Cofactor Comment Organism Structure
acetyl-CoA
-
 Bacillus subtilis

General Information

General Information Comment Organism
malfunction the compaction phenotype of the yfmK deletions is partially bypassed by the hbsK41Q allele. This partial bypass may be explained by the action of more than one acetyltransferase at K41 or that YfmK acts at multiple sites. YfmK also acts at K3, K18, and K80, while YdgE may also act at K86 Bacillus subtilis
additional information characterization of the Bacillus subtilis acetylome Bacillus subtilis
physiological function at least one physiological function of the acetylation of HBsu at key lysine residues by lysine acetyltransferase YfmK is to regulate nucleoid compaction, analogous to the role of histone acetylation in eukaryotes. Acetylation is a regulatory component of the function of HBsu in nucleoid compaction. HBsu belongs to the highly conserved HU family of nucleoid-associated proteins (NAPs) and is essential for viability in Bacillus subtilis. In bacteria, the NAPs are largely responsible for chromosome compaction Bacillus subtilis