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    ptrB oligopeptidase B [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 946358, updated on 17-Dec-2024

    Summary

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    Official Symbol
    ptrB
    Official Full Name
    oligopeptidase B
    Primary source
    ECOCYC:EG11004
    Locus tag
    b1845
    See related
    ASAP:ABE-0006133
    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
    ECK1846; tlp
    Summary
    Cleaves after Arg and Lys. [More information is available at EcoGene: EG11004]. Protease II is a serine protease that hydrolyzes peptide bonds following arginines and lysines. [More information is available at EcoCyc: EG11004].
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    Genomic context

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    Sequence:
    NC_000913.3 (1926779..1928839, complement)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene DNA polymerase III subunit theta Neighboring gene putative carbon-nitrogen hydrolase family protein YobB Neighboring gene exonuclease X Neighboring gene DUF533 domain-containing inner membrane protein YebE Neighboring gene secreted protein YebF

    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. Proteolytic activity of Escherichia coli oligopeptidase B against proline-rich antimicrobial peptides. Mattiuzzo M, et al. J Microbiol Biotechnol, 2014 Feb 28. PMID 24225368
    2. Novel Translation Initiation Regulation Mechanism in Escherichia coli ptrB Mediated by a 5'-Terminal AUG. Beck HJ, et al. J Bacteriol, 2017 Jul 15. PMID 28484048, Free PMC Article
    3. Protease II from Escherichia coli. Substrate specificity and kinetic properties. Pacaud M. Eur J Biochem, 1978 Jan 16. PMID 342237
    4. The study of Escherichia coli proteases. Intracellular serine protease of E. coli-an analogue of bacillus proteases. Strongin AY, et al. J Gen Microbiol, 1979 Feb. PMID 374683
    5. Purification of protease II from Escherichia coli by affinity chromatography and separation of two enzyme species from cells harvested at late log phase. Pacaud M. Eur J Biochem, 1976 Apr 15. PMID 776612

    See all (18) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. results suggest that translation initiation of ptrB mRNA is controlled via its 5'-terminal AUG which, in cooperation with the ptrB 5'-UTR, represents a novel form of regulation that can act as an autonomous control element independent of gene context
      Title: Novel Translation Initiation Regulation Mechanism in Escherichia coli ptrB Mediated by a 5'-Terminal AUG.
    2. Two consecutive basic residues are a preferred cleavage site for the peptidase.
      Title: Proteolytic activity of Escherichia coli oligopeptidase B against proline-rich antimicrobial peptides.
    3. Site-directed mutagenesis of staphylokinase(SAK) His43 and SAKTyr44 demonstrated the crucial requirement of a positively charged and an aromatic residue, respectively, at these positions for optimal functioning of SAK-plasmin activator complex.
      Title: Intermolecular interactions in staphylokinase-plasmin(ogen) bimolecular complex: function of His43 and Tyr44.
    4. N-terminus verified by Edman degradation on complete protein
      Title: Protease II from Escherichia coli: sequencing and expression of the enzyme gene and characterization of the expressed enzyme.
    Submit: New GeneRIF Correction

    General gene information

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    Homology

    Gene Ontology Provided by EcoCyc

    Function Evidence Code Pubs
    enables oligopeptidase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables serine-type endopeptidase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables serine-type endopeptidase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables serine-type peptidase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    Process Evidence Code Pubs
    involved_in proteolysis IEA
    Inferred from Electronic Annotation
    more info
    		  
    Component Evidence Code Pubs
    located_in cytoplasm IDA
    Inferred from Direct Assay
    more info
    		 PubMed 

    General protein information

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    Preferred Names
    oligopeptidase B
    NP_416359.1

    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
      1926779..1928839 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_416359.1 oligopeptidase B [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_416359.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A6N8NE27
      Conserved Domains (1) summary
      PRK10115
      Location:1 → 686
      PRK10115; protease 2; Provisional
    Nucleotide Protein
    Heading Accession and Version

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