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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 3-Dec-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. 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
    2. 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
    3. 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
    4. 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
    5. 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

    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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    Homology

    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
    Heading Accession and Version

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