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    mepS peptidoglycan endopeptidase/peptidoglycan L,D-carboxypeptidase [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 946686, updated on 3-Dec-2024

    Summary

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    Official Symbol
    mepS
    Official Full Name
    peptidoglycan endopeptidase/peptidoglycan L,D-carboxypeptidase
    Primary source
    ECOCYC:G7147
    Locus tag
    b2175
    See related
    ASAP:ABE-0007200
    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
    ECK2169; spr; yeiV
    Summary
    prc deletions are TS at low salt, suppressible by spr mutations; spr prc+ strains are also TS at low salt, which is suppressible by multicopy expression of PBP7 (PbpG). [More information is available at EcoGene: EG14076]. spr is believed to encode a lipoprotein. spr deletion mutants are thermosensitive for growth at low osmolarity, but they suppress the thermosensitivity of prc deletion mutants when the two are combined . nlpI mutations suppress the thermosensitivity of spr mutations . [More information is available at EcoCyc: G7147].
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    Genomic context

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    Sequence:
    NC_000913.3 (2269979..2270545)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene zinc-binding GTPase YeiR Neighboring gene lipid A-core phosphotransferase Neighboring gene putative c-di-GMP phosphodiesterase PdeN Neighboring gene putative oligopeptide ABC transporter periplasmic binding protein YejA

    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. Regulated proteolysis of a cross-link-specific peptidoglycan hydrolase contributes to bacterial morphogenesis. Singh SK, et al. Proc Natl Acad Sci U S A, 2015 Sep 1. PMID 26283368, Free PMC Article
    2. Cell division is antagonized by the activity of peptidoglycan endopeptidases that promote cell elongation. Truong TT, et al. Mol Microbiol, 2020 Dec. PMID 32866331, Free PMC Article
    3. Salinity-dependent impacts of ProQ, Prc, and Spr deficiencies on Escherichia coli cell structure. Kerr CH, et al. J Bacteriol, 2014 Mar. PMID 24443528, Free PMC Article
    4. Overproduction of penicillin-binding protein 7 suppresses thermosensitive growth defect at low osmolarity due to an spr mutation of Escherichia coli. Hara H, et al. Microb Drug Resist, 1996 Spring. PMID 9158724
    5. Interaction of the Escherichia coli lipoprotein NlpI with periplasmic Prc (Tsp) protease. Tadokoro A, et al. J Biochem, 2004 Feb. PMID 15047720

    See all (17) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Cell division is antagonized by the activity of peptidoglycan endopeptidases that promote cell elongation.
      Title: Cell division is antagonized by the activity of peptidoglycan endopeptidases that promote cell elongation.
    2. Prc deficiency may alter bacterial morphology by impairing control of Spr activity at high salinity.
      Title: Salinity-dependent impacts of ProQ, Prc, and Spr deficiencies on Escherichia coli cell structure.
    3. The solution NMR structure of the C-terminal NlpC/P60 domain of E. coli Spr described here reveals that the protein adopts a papain-like alpha+beta fold and identifies a substrate-binding cleft featuring several highly conserved residues.
      Title: Solution NMR structure of the NlpC/P60 domain of lipoprotein Spr from Escherichia coli: structural evidence for a novel cysteine peptidase catalytic triad.
    Submit: New GeneRIF Correction

    General gene information

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    Homology

    Gene Ontology Provided by EcoCyc

    Function Evidence Code Pubs
    enables cysteine-type peptidase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables endopeptidase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables endopeptidase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables endopeptidase activity RCA
    inferred from Reviewed Computational Analysis
    more info
    		 PubMed 
    enables muramoyltetrapeptide carboxypeptidase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    Process Evidence Code Pubs
    involved_in capsule polysaccharide biosynthetic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in cell wall organization IEA
    Inferred from Electronic Annotation
    more info
    		  
    acts_upstream_of_or_within peptidoglycan metabolic process IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in peptidoglycan turnover IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in peptidoglycan turnover IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in proteolysis IEA
    Inferred from Electronic Annotation
    more info
    		  
    Component Evidence Code Pubs
    located_in cell outer membrane IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in cell outer membrane RCA
    inferred from Reviewed Computational Analysis
    more info
    		 PubMed 

    General protein information

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    Preferred Names
    peptidoglycan endopeptidase/peptidoglycan L,D-carboxypeptidase

    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
      2269979..2270545
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_416680.1 peptidoglycan endopeptidase/peptidoglycan L,D-carboxypeptidase [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_416680.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A376W966, A0A5B9AIC5
      Conserved Domains (1) summary
      PRK10838
      Location:2 → 188
      spr; bifunctional murein DD-endopeptidase/murein LD-carboxypeptidase
    Nucleotide Protein
    Heading Accession and Version

    Gene LinkOut

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