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    lpxC UDP-3-O-acyl-N-acetylglucosamine deacetylase [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 944816, updated on 3-Dec-2024

    Summary

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    Official Symbol
    lpxC
    Official Full Name
    UDP-3-O-acyl-N-acetylglucosamine deacetylase
    Primary source
    ECOCYC:EG10265
    Locus tag
    b0096
    See related
    ASAP:ABE-0000336
    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
    asmB; ECK0097; envA
    Summary
    LpxC regulated degradation is facilitated by FtsH. [More information is available at EcoGene: EG10265]. UDP-3-O-acyl-N-acetylglucosamine deacetylase (LpxC) catalyzes the second reaction and the first committed step in lipid A biosynthesis. [More information is available at EcoCyc: EG10265].
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    Genomic context

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    Sequence:
    NC_000913.3 (106557..107474)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene cell division protein FtsQ Neighboring gene cell division protein FtsA Neighboring gene cell division protein FtsZ Neighboring gene SecA translation regulator Neighboring gene protein translocation ATPase

    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. Site-directed mutagenesis of the bacterial metalloamidase UDP-(3-O-acyl)-N-acetylglucosamine deacetylase (LpxC). Identification of the zinc binding site. Jackman JE, et al. Biochemistry, 2001 Jan 16. PMID 11148046
    2. A slow, tight-binding inhibitor of the zinc-dependent deacetylase LpxC of lipid A biosynthesis with antibiotic activity comparable to ciprofloxacin. McClerren AL, et al. Biochemistry, 2005 Dec 20. PMID 16342948, Free PMC Article
    3. UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase functions through a general acid-base catalyst pair mechanism. Hernick M, et al. J Biol Chem, 2005 Apr 29. PMID 15705580
    4. Kinetic analysis of the zinc-dependent deacetylase in the lipid A biosynthetic pathway. McClerren AL, et al. Biochemistry, 2005 Feb 1. PMID 15667204
    5. Structure of the LpxC deacetylase with a bound substrate-analog inhibitor. Coggins BE, et al. Nat Struct Biol, 2003 Aug. PMID 12833153, Free PMC Article

    See all (66) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. A New Factor LapD Is Required for the Regulation of LpxC Amounts and Lipopolysaccharide Trafficking.
      Title: A New Factor LapD Is Required for the Regulation of LpxC Amounts and Lipopolysaccharide Trafficking.
    2. The inner membrane protein LapB is required for adaptation to cold stress in an LpxC-independent manner.
      Title: The inner membrane protein LapB is required for adaptation to cold stress in an LpxC-independent manner.
    3. An Essential Membrane Protein Modulates the Proteolysis of LpxC to Control Lipopolysaccharide Synthesis in Escherichia coli.
      Title: An Essential Membrane Protein Modulates the Proteolysis of LpxC to Control Lipopolysaccharide Synthesis in Escherichia coli.
    4. YejM Controls LpxC Levels by Regulating Protease Activity of the FtsH/YciM Complex of Escherichia coli.
      Title: YejM Controls LpxC Levels by Regulating Protease Activity of the FtsH/YciM Complex of Escherichia coli.
    5. analysis of mutants resistant to LpxC inhibitors by rebalancing cellular homeostasis
      Title: Mutants resistant to LpxC inhibitors by rebalancing cellular homeostasis.
    6. the active site metal ion in UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase (LpxC) switches between Fe(II) and Zn(II) depending on cellular conditions
      Title: Active site metal ion in UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase (LpxC) switches between Fe(II) and Zn(II) depending on cellular conditions.
    7. Functions of LpxC active site residues have been classified on the basis of changes in steady-state turnover and product binding affinity; side chains are identified that enhance and destabilize product affinity as well as enhance catalytic efficiency.
      Title: Catalytic mechanism and molecular recognition of E. coli UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase probed by mutagenesis.
    8. N-terminus verified by Edman degradation on complete protein
      Title: The envA permeability/cell division gene of Escherichia coli encodes the second enzyme of lipid A biosynthesis. UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase.
    9. A C-terminal tail of about 20 amino acids length is required for proteolysis of LpxC by FtsH
      Title: Sequence and length recognition of the C-terminal turnover element of LpxC, a soluble substrate of the membrane-bound FtsH protease.
    10. The C-terminus of LpxC contains a signal sequence necessary for FtsH-dependent degradation.
      Title: The C-terminal end of LpxC is required for degradation by the FtsH protease.
    Submit: New GeneRIF Correction See all GeneRIFs (11)

    Interactions

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    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

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    Homology

    Gene Ontology Provided by EcoCyc

    Function Evidence Code Pubs
    enables UDP-3-O-acyl-N-acetylglucosamine deacetylase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables deacetylase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables hydrolase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables iron ion binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables metal ion binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables zinc ion binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    Process Evidence Code Pubs
    involved_in carbohydrate derivative metabolic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in lipid A biosynthetic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    acts_upstream_of_or_within lipid A biosynthetic process IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in organophosphate metabolic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in phosphate-containing compound metabolic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    Component Evidence Code Pubs
    located_in cytoplasm IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in membrane IEA
    Inferred from Electronic Annotation
    more info
    		  

    General protein information

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    Preferred Names
    UDP-3-O-acyl-N-acetylglucosamine deacetylase
    NP_414638.1

    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
      106557..107474
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_414638.1 UDP-3-O-acyl-N-acetylglucosamine deacetylase [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_414638.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A5B9AML4
      Conserved Domains (1) summary
      PRK13186
      Location:1 → 299
      lpxC; UDP-3-O-acyl-N-acetylglucosamine deacetylase
    Nucleotide Protein
    Heading Accession and Version

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