U.S. flag

An official website of the United States government

Format

Send to:

Choose Destination

Links from GEO Profiles

    • Showing Current items.

    mpaA murein tripeptide amidase A [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 945969, updated on 17-Dec-2024

    Summary

    Go to the top of the page Help
    Official Symbol
    mpaA
    Official Full Name
    murein tripeptide amidase A
    Primary source
    ECOCYC:G6662
    Locus tag
    b1326
    See related
    ASAP:ABE-0004450
    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
    ECK1322; ycjI
    Summary
    MpaA is a murein peptide amidase that may act with YcjG in murein recycling . [More information is available at EcoCyc: G6662].
    NEW
    Try the new Gene table
    Try the new Transcript table

    Genomic context

    Go to the top of the page Help
    Sequence:
    NC_000913.3 (1389870..1390598, complement)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene DNA-binding transcriptional dual regulator TyrR Neighboring gene lipid hydroperoxide peroxidase Neighboring gene L-Ala-D/L-Glu epimerase Neighboring gene putative uncharacterized protein YmjC Neighboring gene uncharacterized protein YmjD Neighboring gene putative hydrolase YcjY

    Genomic regions, transcripts, and products

    Go to the top of the page Help
    Genomic Sequence:
    NC_000913.3

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

    Go to the top of the pageHelp

    Related articles in PubMed

    1. MpaA is a murein-tripeptide-specific zinc carboxypeptidase that functions as part of a catabolic pathway for peptidoglycan-derived peptides in γ-proteobacteria. Maqbool A, et al. Biochem J, 2012 Dec 15. PMID 22970852
    2. Identification of MpaA, an amidase in Escherichia coli that hydrolyzes the gamma-D-glutamyl-meso-diaminopimelate bond in murein peptides. Uehara T, et al. J Bacteriol, 2003 Jan. PMID 12511517, Free PMC Article
    3. Thioredoxin-linked "thiol peroxidase" from periplasmic space of Escherichia coli. Cha MK, et al. J Biol Chem, 1995 Dec 1. PMID 7499381
    4. MEROPS: the peptidase database. Rawlings ND, et al. Nucleic Acids Res, 2006 Jan 1. PMID 16381862, Free PMC Article
    5. Evolution of enzymatic activities in the enolase superfamily: identification of the general acid catalyst in the active site of D-glucarate dehydratase from Escherichia coli. Gulick AM, et al. Biochemistry, 2001 Aug 28. PMID 11513584

    See all (10) citations in PubMed

    GeneRIFs: Gene References Into Functions

    General gene information

    Go to the top of the page Help

    Homology

    Gene Ontology Provided by EcoCyc

    Function Evidence Code Pubs
    enables amidase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables amidase activity IGI
    Inferred from Genetic Interaction
    more info
    		 PubMed 
    enables carboxypeptidase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables metal ion binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables metallocarboxypeptidase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables metallopeptidase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables murein tripeptide carboxypeptidase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables murein tripeptide carboxypeptidase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables protein homodimerization activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables zinc ion binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables zinc ion binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    Process Evidence Code Pubs
    involved_in cell wall macromolecule catabolic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in cell wall organization IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in glycopeptide catabolic process IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in peptidoglycan catabolic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    acts_upstream_of_or_within peptidoglycan catabolic process IGI
    Inferred from Genetic Interaction
    more info
    		 PubMed 
    involved_in peptidoglycan catabolic process IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in proteolysis IEA
    Inferred from Electronic Annotation
    more info
    		  
    Component Evidence Code Pubs
    located_in cytoplasm IEA
    Inferred from Electronic Annotation
    more info
    		  

    General protein information

    Go to the top of the page Help
    Preferred Names
    murein tripeptide amidase A

    NCBI Reference Sequences (RefSeq)

    Go to the top of the page Help

    NEW Try the new Transcript table

    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
      1389870..1390598 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_415842.2 murein tripeptide amidase A [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_415842.2

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A775UVR7, A0A8S7TAP7
      Conserved Domains (1) summary
      PRK10602
      Location:1 → 237
      PRK10602; murein tripeptide amidase MpaA
    Nucleotide Protein
    Heading Accession and Version

    Gene LinkOut

    The following LinkOut resources are supplied by external providers. These providers are responsible for maintaining the links.