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pgaB poly-beta-1,6-N-acetyl-D-glucosamine N-deacetylase and beta-1,6 glycoside hydrolase [ Escherichia coli str. K-12 substr. MG1655 ]

Gene ID: 945604, updated on 19-Sep-2024

Summary

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Official Symbol
pgaB
Official Full Name
poly-beta-1,6-N-acetyl-D-glucosamine N-deacetylase and beta-1,6 glycoside hydrolase
Primary source
ECOCYC:G6530
Locus tag
b1023
See related
ASAP:ABE-0003467
Gene type
protein coding
RefSeq status
PROVISIONAL
Organism
Escherichia coli str. K-12 substr. MG1655 (strain: K-12, substrain: MG1655)
Lineage
Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia
Also known as
ECK1013; hmsF; ycdR
Summary
PGA is a biofilm adhesin polysaccharide. [More information is available at EcoGene: EG13864]. The pgaABCD locus is required for the synthesis of a cell-bound hexosamine-rich polysaccharide, which was identified as a linear polymer of beta-1,6-N-acetylglucosamine residues (PGA), an adhesin essential in biofilm formation . [More information is available at EcoCyc: G6530].
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Genomic context

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Sequence:
NC_000913.3 (1087839..1089857, complement)

NC_000913.3Genomic Context describing neighboring genes Neighboring gene ATP-binding protein PhoH Neighboring gene poly-N-acetyl-D-glucosamine synthase subunit PgaD Neighboring gene poly-N-acetyl-D-glucosamine synthase subunit PgaC Neighboring gene partially deacetylated poly-beta-1,6-N-acetyl-D-glucosamine export outer membrane porin Neighboring gene putative diguanylate cyclase DgcT

Genomic regions, transcripts, and products

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Genomic Sequence:
NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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Related articles in PubMed

  1. PgaB orthologues contain a glycoside hydrolase domain that cleaves deacetylated poly-β(1,6)-N-acetylglucosamine and can disrupt bacterial biofilms. Little DJ, et al. PLoS Pathog, 2018 Apr. PMID 29684093, Free PMC Article
  2. Structural Basis for Translocation of a Biofilm-supporting Exopolysaccharide across the Bacterial Outer Membrane. Wang Y, et al. J Biol Chem, 2016 May 6. PMID 26957546, Free PMC Article
  3. The structure of the deacetylase domain of Escherichia coli PgaB, an enzyme required for biofilm formation: a circularly permuted member of the carbohydrate esterase 4 family. Nishiyama T, et al. Acta Crystallogr D Biol Crystallogr, 2013 Jan. PMID 23275162
  4. The structure- and metal-dependent activity of Escherichia coli PgaB provides insight into the partial de-N-acetylation of poly-β-1,6-N-acetyl-D-glucosamine. Little DJ, et al. J Biol Chem, 2012 Sep 7. PMID 22810235, Free PMC Article
  5. Combining in situ proteolysis and mass spectrometry to crystallize Escherichia coli PgaB. Little DJ, et al. Acta Crystallogr Sect F Struct Biol Cryst Commun, 2012 Jul 1. PMID 22750880, Free PMC Article

See all (19) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. The crystal structure of the N-terminal domain of PgaB, which has deacetylase activity, is described and compared with models of other deacetylases.
    Title: The structure of the deacetylase domain of Escherichia coli PgaB, an enzyme required for biofilm formation: a circularly permuted member of the carbohydrate esterase 4 family.
  2. Crystals of the selenomethionine-incorporated PgaB exhibited the symmetry of space group P2(1)2(1)2(1) and diffracted to 2.1 A resolution
    Title: Combining in situ proteolysis and mass spectrometry to crystallize Escherichia coli PgaB.
Submit: New GeneRIF Correction

General gene information

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Gene Ontology Provided by EcoCyc

Function Evidence Code Pubs
enables hydrolase activity IEA
Inferred from Electronic Annotation
more info
  
enables hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds IDA
Inferred from Direct Assay
more info
 PubMed 
enables hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds IEA
Inferred from Electronic Annotation
more info
  
enables hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds IMP
Inferred from Mutant Phenotype
more info
 PubMed 
enables hydrolase activity, hydrolyzing O-glycosyl compounds IDA
Inferred from Direct Assay
more info
 PubMed 
enables protein binding IPI
Inferred from Physical Interaction
more info
 PubMed 
Process Evidence Code Pubs
involved_in carbohydrate metabolic process IEA
Inferred from Electronic Annotation
more info
  
involved_in cell adhesion involved in biofilm formation IEA
Inferred from Electronic Annotation
more info
  
acts_upstream_of_or_within macromolecule deacylation IDA
Inferred from Direct Assay
more info
 PubMed 
acts_upstream_of_or_within macromolecule deacylation IMP
Inferred from Mutant Phenotype
more info
 PubMed 
acts_upstream_of_or_within single-species biofilm formation IMP
Inferred from Mutant Phenotype
more info
 PubMed 
Component Evidence Code Pubs
located_in cell outer membrane IEA
Inferred from Electronic Annotation
more info
  

General protein information

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Preferred Names
poly-beta-1,6-N-acetyl-D-glucosamine N-deacetylase and beta-1,6 glycoside hydrolase

NCBI Reference Sequences (RefSeq)

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

  1. NC_000913.3 Reference assembly

    Range
    1087839..1089857 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_415542.1 poly-beta-1,6-N-acetyl-D-glucosamine N-deacetylase and beta-1,6 glycoside hydrolase [Escherichia coli str. K-12 substr. MG1655]

    See identical proteins and their annotated locations for NP_415542.1

    Status: PROVISIONAL

    UniProtKB/TrEMBL
    A0A2H4TN66
    Conserved Domains (1) summary
    PRK14582
    Location:1 → 672
    pgaB; poly-beta-1,6-N-acetyl-D-glucosamine N-deacetylase PgaB
Nucleotide Protein
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