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    treB trehalose-specific PTS enzyme IIBC component [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 948761, updated on 3-Dec-2024

    Summary

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    Official Symbol
    treB
    Official Full Name
    trehalose-specific PTS enzyme IIBC component
    Primary source
    ECOCYC:EG12127
    Locus tag
    b4240
    See related
    ASAP:ABE-0013872
    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
    ECK4235
    Summary
    [More information is available at EcoCyc: EG12127].
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    Genomic context

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    Sequence:
    NC_000913.3 (4464759..4466180, complement)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene anaerobic ribonucleoside-triphosphate reductase Neighboring gene trehalose-6-phosphate hydrolase Neighboring gene DNA-binding transcriptional repressor TreR Neighboring gene leader peptide MgtL

    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. Characterization of TreR, the major regulator of the Escherichia coli trehalose system. Horlacher R, et al. J Biol Chem, 1997 May 16. PMID 9148912
    2. Protein:Protein interactions in the cytoplasmic membrane apparently influencing sugar transport and phosphorylation activities of the e. coli phosphotransferase system. Aboulwafa M, et al. PLoS One, 2019. PMID 31751341, Free PMC Article
    3. Trehalase of Escherichia coli. Mapping and cloning of its structural gene and identification of the enzyme as a periplasmic protein induced under high osmolarity growth conditions. Boos W, et al. J Biol Chem, 1987 Sep 25. PMID 2820965
    4. Transport and metabolism of trehalose in Escherichia coli and Salmonella typhimurium. Maréchal LR. Arch Microbiol, 1984 Jan. PMID 6370169
    5. Trehalose transport and metabolism in Escherichia coli. Boos W, et al. J Bacteriol, 1990 Jun. PMID 2160944, Free PMC Article

    See all (18) citations in PubMed

    GeneRIFs: Gene References Into Functions

    Pathways from PubChem

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    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 kinase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    enables protein-N(PI)-phosphohistidine-sugar phosphotransferase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables protein-phosphocysteine-trehalose phosphotransferase system transporter activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables protein-phosphocysteine-trehalose phosphotransferase system transporter activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables protein-phosphocysteine-trehalose phosphotransferase system transporter activity IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    enables protein-phosphocysteine-trehalose phosphotransferase system transporter activity ISM
    Inferred from Sequence Model
    more info
    		 PubMed 
    enables trehalose transmembrane transporter activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    Process Evidence Code Pubs
    involved_in phosphoenolpyruvate-dependent sugar phosphotransferase system IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    acts_upstream_of_or_within phosphoenolpyruvate-dependent sugar phosphotransferase system IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in phosphoenolpyruvate-dependent sugar phosphotransferase system IEA
    Inferred from Electronic Annotation
    more info
    		  
    acts_upstream_of_or_within phosphoenolpyruvate-dependent sugar phosphotransferase system IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    acts_upstream_of_or_within trehalose transport EXP
    Inferred from Experiment
    more info
    		 PubMed 
    involved_in trehalose transport IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    acts_upstream_of_or_within trehalose transport IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in trehalose transport IEA
    Inferred from Electronic Annotation
    more info
    		  
    Component Evidence Code Pubs
    located_in membrane IEA
    Inferred from Electronic Annotation
    more info
    		  
    is_active_in plasma membrane IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in plasma membrane IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in plasma membrane IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in plasma membrane RCA
    inferred from Reviewed Computational Analysis
    more info
    		 PubMed 

    General protein information

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    Preferred Names
    trehalose-specific PTS enzyme IIBC component
    NP_418661.1

    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
      4464759..4466180 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_418661.1 trehalose-specific PTS enzyme IIBC component [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_418661.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A5B9ALU8
      Conserved Domains (1) summary
      PRK11007
      Location:1 → 473
      PRK11007; PTS system trehalose(maltose)-specific transporter subunits IIBC; Provisional
    Nucleotide Protein
    Heading Accession and Version

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