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Literature summary for 3.1.1.58 extracted from

  • Itoh, Y.; Rice, J.D.; Goller, C.; Pannuri, A.; Taylor, J.; Meisner, J.; Beveridge, T.J.; Preston, J.F.; Romeo, T.
    Roles of pgaABCD genes in synthesis, modification, and export of the Escherichia coli biofilm adhesin poly-beta-1,6-N-acetyl-D-glucosamine (2008), J. Bacteriol., 190, 3670-3680.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.1.1.58

Cloned(Commentary)

Cloned (Comment) Organism
from chromosomal DNA in pUC19 and subsequently in pCR2.1-TOPO for site directed mutagenesis and complementation experiments Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
alignment with PDB database: hits to tetratricopeptide repeat domains of human nucleoporin O-linked N-acetylglucosamine transferase, yeast mitochondrial outer membrane translocon protein Tom70p, and human peroxisomal targeting signal-1 receptor PEX5, putative domains: porin domain for export of poly-beta-1,6-N-acetyl-D-glucosamine, and periplasmic domain for protein-protein interactions Escherichia coli

Protein Variants

Protein Variants Comment Organism
D115A decreased catalytic activity, 6.4% of wild-type activity on N-deacetylation of poly-beta-1,6-N-acetyl-D-glucosamine-adhesin Escherichia coli
H184A mutant, deficient in biofilm formation Escherichia coli
PgaB271 DUF187 domain truncation mutant, amino acids 1-271, deficient in biofilm formation and poly-beta-1,6-N-acetyl-D-glucosamine secretion, 4.1% of wild-type activity on N-deacetylation of poly-beta-1,6-N-acetyl-D-glucosamine-adhesin Escherichia coli
PgaB410 DUF187 domain truncation mutant, amino acids 1-410, proteolytic cleavage during overexpression Escherichia coli
PgaB516 DUF187 domain truncation mutant, amino acids 1-516, deficient in biofilm formation and poly-beta-1,6-N-acetyl-D-glucosamine secretion, 5% of wild-type activity on N-deacetylation of poly-beta-1,6-N-acetyl-D-glucosamine-adhesin, proteolytic cleavage during overexpression Escherichia coli

General Stability

General Stability Organism
proteolytic cleavage of DUF187 domain truncation mutants PgaB516 and PgaB410 during overexpression in Escherichia coli Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
outer membrane predicted beta-barrel porin of PgaA that forms outer membrane secretin for poly-beta-1,6-N-acetyl-D-glucosamine (PGA) and promotes its export from periplasm in response to N-deacetylation by PgaB, defective PGA secretion in PgaA-deficient mutant strain Escherichia coli 19867
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outer membrane predicted, N-deacetylation of poly-beta-1,6-N-acetyl-D-glucosamine (PGA) by PgaB promotes its export from periplasma by PgaA, defective PGA secretion in PgaB-deficient mutant strain Escherichia coli 19867
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Escherichia coli deacetylase domain necessary but not suffficient for normal catalytic activity, requires also the enzyme’s C-terminus: DUF187 domain putatively binds unmodified poly-beta-1,6-N-acetyl-D-glucosamine and assists catalysis ?
-
 ?
additional information Escherichia coli K-12 MG1655 deacetylase domain necessary but not suffficient for normal catalytic activity, requires also the enzyme’s C-terminus: DUF187 domain putatively binds unmodified poly-beta-1,6-N-acetyl-D-glucosamine and assists catalysis ?
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli P69434
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Escherichia coli P75906
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Escherichia coli K-12 MG1655 P69434
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Escherichia coli K-12 MG1655 P75906
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information deacetylase domain necessary but not suffficient for normal catalytic activity, requires also the enzyme’s C-terminus: DUF187 domain putatively binds unmodified poly-beta-1,6-N-acetyl-D-glucosamine and assists catalysis Escherichia coli ?
-
 ?
additional information involved in export of poly-beta-1,6-N-acetyl-D-glucosamine (beta-1,6-GlcNAc, PGA) from periplasma after its deacetylation Escherichia coli ?
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 ?
additional information involved in export of poly-beta-1,6-N-acetyl-D-glucosamine (beta-1,6-GlcNAc, PGA) from periplasma after its deacetylation Escherichia coli K-12 MG1655 ?
-
 ?
additional information deacetylase domain necessary but not suffficient for normal catalytic activity, requires also the enzyme’s C-terminus: DUF187 domain putatively binds unmodified poly-beta-1,6-N-acetyl-D-glucosamine and assists catalysis Escherichia coli K-12 MG1655 ?
-
 ?
poly-beta-1,6-N-acetyl-D-glucosamine-adhesin + H2O beta-1,6-GlcNAc (PGA) also called polysaccharide intracellular adhesin (PIA) Escherichia coli acetate + ?
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 ?
poly-beta-1,6-N-acetyl-D-glucosamine-adhesin + H2O beta-1,6-GlcNAc (PGA) also called polysaccharide intracellular adhesin (PIA) Escherichia coli K-12 MG1655 acetate + ?
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 ?

Synonyms

Synonyms Comment Organism
PgaA encoded within pgaABCD operon, BLAST analyses: not related to a protein of known function Escherichia coli
PgaB encoded within pgaABCD operon, BLAST analyses: contains polysaccharide N-deacetylase domain of carbohydrate esterase 4 (CE4) family Escherichia coli

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
37
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 increased temperature might improve poly-beta-1,6-N-acetyl-D-glucosamine export in absence of deacetylation by PgaB Escherichia coli