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Literature summary extracted from

  • Wan, Z.; Brown, P.J.; Elliott, E.N.; Brun, Y.V.
    The adhesive and cohesive properties of a bacterial polysaccharide adhesin are modulated by a deacetylase (2013), Mol. Microbiol., 88, 486-500.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.1.58 gene hfsH, sequence comparisons Asticcacaulis biprosthecium
3.1.1.58 gene hfsH, sequence comparisons, recombinant expression of wild-type and mutant enzymes in Escherichia coli Caulobacter vibrioides

Protein Variants

EC Number Protein Variants Comment Organism
3.1.1.58 D48A site-directed mutagenesis of the catalytic residue abolishes the esterase activity of the enzyme, the mutant strain is deficient in holdfast anchoring to the cell body, and small holdfasts are shed into the medium. The mutant enzyme has a similar secondary structure compared to the wild-type enzyme based on circular dichroism measurement Caulobacter vibrioides
3.1.1.58 additional information deletion of gene hfsH abolishing surface adhesion of the cell. The gene hfsH deletion mutant synthesizes defective holdfasts with low adhesiveness and cohesiveness that cannot be anchored to the cell body. In contrast, overexpression of HfsH increases cell adherence Caulobacter vibrioides
3.1.1.58 additional information deletion of gene hfsH abolishing surface adhesion of the cell. The gene hfsH deletion mutant synthesizes defective holdfasts with low adhesiveness and cohesiveness that cannot be anchored to the cell body. In contrast, overexpression of HfsH increases cell adherence. Phenotypes of Asticcacaulis biprosthecum transposon mutants with insertions in a number of hfs genes, overview Asticcacaulis biprosthecium

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.1.1.58 membrane
-
 Caulobacter vibrioides 16020
-
3.1.1.58 membrane
-
 Asticcacaulis biprosthecium 16020
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.1.58 Zn2+ required Caulobacter vibrioides
3.1.1.58 Zn2+ required Asticcacaulis biprosthecium

Organism

EC Number Organism UniProt Comment Textmining
3.1.1.58 Asticcacaulis biprosthecium
-
 gene hfsH
-
3.1.1.58 Caulobacter vibrioides
-
 gene hfsH
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.1.58 recombinant expression of wild-type and mutant enzymes from Escherichia coli Caulobacter vibrioides

Synonyms

EC Number Synonyms Comment Organism
3.1.1.58 HfsH
-
 Caulobacter vibrioides
3.1.1.58 HfsH
-
 Asticcacaulis biprosthecium
3.1.1.58 holdfast synthesis protein
-
 Caulobacter vibrioides
3.1.1.58 holdfast synthesis protein
-
 Asticcacaulis biprosthecium
3.1.1.58 polysaccharide deacetylase
-
 Caulobacter vibrioides
3.1.1.58 polysaccharide deacetylase
-
 Asticcacaulis biprosthecium

General Information

EC Number General Information Comment Organism
3.1.1.58 evolution conservation of holdfast synthesis genes in the Caulobacterales clade of the Alphaproteobacteria, gene hfsH is broadly conserved in the hfs gene cluster across several bacterial species Caulobacter vibrioides
3.1.1.58 evolution conservation of holdfast synthesis genes in the Caulobacterales clade of the Alphaproteobacteria, gene hfsH is broadly conserved in the hfs gene cluster across several bacterial species Asticcacaulis biprosthecium
3.1.1.58 malfunction disruption of the hfsH gene, which encodes a putative polysaccharide deacetylase, leads to accumulation of polar polysaccharide holdfast in the culture supernatant. The hfsH deletion mutant strain synthesizes holdfast, but the holdfasts are shed into the medium and have decreased adhesiveness and cohesiveness, phenotype, overview. Site-directed mutagenesis at the predicted catalytic site D48 phenocopied the DELTAhfsH mutant and abolishes the esterase activity of the enzyme Caulobacter vibrioides
3.1.1.58 malfunction disruption of the hfsH gene, which encodes a putative polysaccharide deacetylase, leads to accumulation of polar polysaccharide holdfast in the culture supernatant. The hfsH deletion mutant strain synthesizes holdfast, but the holdfasts are shed into the medium and have decreased adhesiveness and cohesiveness, phenotype, overview. Site-directed mutagenesis at the predicted catalytic site phenocopied the DELTAhfsH mutant and abolishes the esterase activity of the enzyme Asticcacaulis biprosthecium
3.1.1.58 additional information the HfsH protein contains 4 conserved motifs, including the essential acetate binding residues and the zinc-binding triad, the enzyme has all the known essential components required to function as polysaccharide deacetylase Caulobacter vibrioides
3.1.1.58 additional information the HfsH protein contains 4 conserved motifs, including the essential acetate binding residues and the zinc-binding triad, the enzyme has all the known essential components required to function as polysaccharide deacetylase Asticcacaulis biprosthecium
3.1.1.58 physiological function in Asticcacaulis biprosthecum, surface attachment and subsequent biofilm growth depend on the ability to synthesize an adhesive polar polysaccharide known as the holdfast, involving the enzyme. The polysaccharide deacetylase activity of HfsH is required for the adhesive and cohesive properties of the holdfast, as well as for the anchoring of the holdfast to the cell envelope, the holdfast contains beta-1,4-N-acetylglucosamine polymers Asticcacaulis biprosthecium
3.1.1.58 physiological function in Caulobacter crescentus, surface attachment and subsequent biofilm growth depend on the ability to synthesize an adhesive polar polysaccharide known as the holdfast, involving the enzyme. The polysaccharide deacetylase activity of HfsH is required for the adhesive and cohesive properties of the holdfast, as well as for the anchoring of the holdfast to the cell envelope, the holdfast contains beta-1,4-N-acetylglucosamine polymers Caulobacter vibrioides