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    waaL O-antigen ligase [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 948148, updated on 3-Dec-2024

    Summary

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    Official Symbol
    waaL
    Official Full Name
    O-antigen ligase
    Primary source
    ECOCYC:EG11424
    Locus tag
    b3622
    See related
    ASAP:ABE-0011849
    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
    ECK3612; rfaL
    Summary
    The lipopolysaccharide of Escherichia coli K-12 consists of two major components: the hydrophobic lipid A moiety inserted into the outer membrane and the phosphorylated core oligosaccharide . [More information is available at EcoCyc: EG11424].
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    Genomic context

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    Sequence:
    NC_000913.3 (3796948..3798207)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene ADP-heptose--LPS heptosyltransferase 2 Neighboring gene ADP-heptose:LPS heptosyltransferase 1 Neighboring gene protein YibX;protein YibX-S Neighboring gene protein YibY Neighboring gene putative ADP-heptose:LPS heptosyltransferase 4 Neighboring gene lipopolysaccharide core biosynthesis protein WaaZ

    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. A mutant Escherichia coli that attaches peptidoglycan to lipopolysaccharide and displays cell wall on its surface. Grabowicz M, et al. Elife, 2014 Dec 31. PMID 25551294, Free PMC Article
    2. Functional analysis of the large periplasmic loop of the Escherichia coli K-12 WaaL O-antigen ligase. Pérez JM, et al. Mol Microbiol, 2008 Dec. PMID 19019161
    3. Modification of lipopolysaccharide with colanic acid (M-antigen) repeats in Escherichia coli. Meredith TC, et al. J Biol Chem, 2007 Mar 16. PMID 17227761
    4. Modulation of the surface architecture of gram-negative bacteria by the action of surface polymer:lipid A-core ligase and by determinants of polymer chain length. Whitfield C, et al. Mol Microbiol, 1997 Feb. PMID 9157235
    5. Variation in the complex carbohydrate biosynthesis loci of Acinetobacter baumannii genomes. Kenyon JJ, et al. PLoS One, 2013. PMID 23614028, Free PMC Article

    See all (25) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Both E. coli and P. aeruginosa WaaL proteins share similar membrane topology. P. aeruginosa WaaL shares similar functional properties with E. coli WaaL and E. coli WaaL may adopt a functional dimer conformation.
      Title: Escherichia coli and Pseudomonas aeruginosa lipopolysaccharide O-antigen ligases share similar membrane topology and biochemical properties.
    2. A point-mutation has been found in the gene for O-antigen ligase (WaaL) in Escherichia coli that causes LPS to be modified with peptidoglycan subunits thus conferring vancomycin resistance.
      Title: A mutant Escherichia coli that attaches peptidoglycan to lipopolysaccharide and displays cell wall on its surface.
    3. The periplasmic location of a large (EL5) and small (EL4) adjacent loops in the Escherichia coli K-12 WaaL was determined.
      Title: Functional analysis of the large periplasmic loop of the Escherichia coli K-12 WaaL O-antigen ligase.
    4. In a mouse model of urinary tract infection, NU14 DeltaampG, NU14 DeltawaaL, and NU14 Deltaalr were attenuated compared to wild-type NU14 and showed reduced fitness in competition experiments.
      Title: Molecular basis of uropathogenic Escherichia coli evasion of the innate immune response in the bladder.
    Submit: New GeneRIF Correction

    Pathways from PubChem

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    General gene information

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    Homology

    Gene Ontology Provided by EcoCyc

    Function Evidence Code Pubs
    enables glycosyltransferase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables glycosyltransferase activity IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    Process Evidence Code Pubs
    involved_in lipopolysaccharide biosynthetic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in lipopolysaccharide core region biosynthetic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    Component Evidence Code Pubs
    located_in plasma membrane IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in plasma membrane IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in plasma membrane ISM
    Inferred from Sequence Model
    more info
    		 PubMed 

    General protein information

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    Preferred Names
    O-antigen ligase

    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
      3796948..3798207
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_418079.1 O-antigen ligase [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_418079.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A7H4YQL2
      Conserved Domains (1) summary
      COG3307
      Location:1 → 393
      RfaL; O-antigen ligase [Cell wall/membrane/envelope biogenesis]
    Nucleotide Protein
    Heading Accession and Version

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