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    patZ peptidyl-lysine N-acetyltransferase [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 947056, updated on 17-Dec-2024

    Summary

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    Official Symbol
    patZ
    Official Full Name
    peptidyl-lysine N-acetyltransferase
    Primary source
    ECOCYC:G7350
    Locus tag
    b2584
    See related
    ASAP:ABE-0008506
    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
    ECK2582; pka; yfiQ
    Summary
    Acs is the only known substrate for Pat (S.t.) and YfiQ(Pat) has not been characterized in Escherichia coli so a role in general protein lysine acetylation is speculative. yfiQ was named pat for protein acetyltransferase in Salmonella where it inhibits acetyl CoA synthase Acs by acetylating residue K609; yfiQ(pat) is assumed to have the same function in Escherichia coli (Starai, 2004). [More information is available at EcoGene: EG14224]. Deletion of yfiQ does not eliminate acetylation of a heterologous protein produced in Escherichia coli . [More information is available at EcoCyc: G7350].
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    Genomic context

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    Sequence:
    NC_000913.3 (2719953..2722613)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene reduced thioredoxin 2 Neighboring gene tRNA 3-amino-3-carboxypropyltransferase Neighboring gene protein PssL Neighboring gene phosphatidylserine synthase Neighboring gene DUF2279 domain-containing protein YfiM Neighboring gene alpha-ketoglutarate:H(+) symporter

    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. cAMP-CRP co-ordinates the expression of the protein acetylation pathway with central metabolism in Escherichia coli. Castaño-Cerezo S, et al. Mol Microbiol, 2011 Dec. PMID 22059728
    2. Protein acetylation in prokaryotes increases stress resistance. Ma Q, et al. Biochem Biophys Res Commun, 2011 Jul 15. PMID 21703240, Free PMC Article
    3. Time- and temperature-dependent acetylation of the chemokine RANTES produced in recombinant Escherichia coli. d'Alayer J, et al. Protein Expr Purif, 2007 Sep. PMID 17574862
    4. The Protein Acetyltransferase PatZ from Escherichia coli Is Regulated by Autoacetylation-induced Oligomerization. de Diego Puente T, et al. J Biol Chem, 2015 Sep 18. PMID 26251518, Free PMC Article
    5. Post-translational modification of RNase R is regulated by stress-dependent reduction in the acetylating enzyme Pka (YfiQ). Liang W, et al. RNA, 2012 Jan. PMID 22124017, Free PMC Article

    See all (19) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. The authors present evidence that the transcription of the Gcn5-like acetyltransferase YfiQ of Escherichia coli (proposed name: PatZ) is regulated by cAMP-CRP and its implications on acetate metabolism regulation.
      Title: cAMP-CRP co-ordinates the expression of the protein acetylation pathway with central metabolism in Escherichia coli.
    2. We determined that K298 of RNA polymerase alpha is acetylated in a glucose and YfiQ-dependent manner.
      Title: Involvement of protein acetylation in glucose-induced transcription of a stress-responsive promoter.
    3. These data indicate that RNase R stability depends on Pka, which itself is regulated under stress conditions.
      Title: Post-translational modification of RNase R is regulated by stress-dependent reduction in the acetylating enzyme Pka (YfiQ).
    Submit: New GeneRIF Correction

    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 ATP binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables acyltransferase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables acyltransferase activity, transferring groups other than amino-acyl groups IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables catalytic activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables identical protein binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables metal ion binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables peptide-lysine-N-acetyltransferase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables peptide-lysine-N-acetyltransferase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables peptide-lysine-N-acetyltransferase activity IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    enables protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    Process Evidence Code Pubs
    acts_upstream_of_or_within response to heat IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    acts_upstream_of_or_within response to oxidative stress IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    Component Evidence Code Pubs
    part_of protein-containing complex IDA
    Inferred from Direct Assay
    more info
    		 PubMed 

    General protein information

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    Preferred Names
    peptidyl-lysine N-acetyltransferase

    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
      2719953..2722613
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_417079.1 peptidyl-lysine N-acetyltransferase [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_417079.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A2X1PRB8, A0A8S7EHZ9
      Conserved Domains (2) summary
      COG1042
      Location:3 → 625
      ACCS; Acyl-CoA synthetase (NDP forming) [Energy production and conversion]
      pfam00583
      Location:750 → 863
      Acetyltransf_1; Acetyltransferase (GNAT) family
    Nucleotide Protein
    Heading Accession and Version

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