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    secB protein export chaperone SecB [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 948123, updated on 19-Sep-2024

    Summary

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    Official Symbol
    secB
    Official Full Name
    protein export chaperone SecB
    Primary source
    ECOCYC:EG10937
    Locus tag
    b3609
    See related
    ASAP:ABE-0011798
    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
    ECK3599
    Summary
    Penultimate Ser residue missing from purified protein could be a proteolytic artifact. [More information is available at EcoGene: EG10937]. SecB is a cytoplasmic protein involved in the Sec secretion pathway and is believed to function in conjunction with SecA/E/G/Y to chaperone proteins in their unfolded state to the inner membrane secretion complex. [More information is available at EcoCyc: EG10937].
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    Genomic context

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    Sequence:
    NC_000913.3 (3783661..3784128, complement)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene tRNA (cytidine/uridine-2'-O)-ribose methyltransferase Neighboring gene serine acetyltransferase Neighboring gene glycerol-3-phosphate dehydrogenase Neighboring gene reduced glutaredoxin 3 Neighboring gene putative sulfurtransferase YibN

    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. Mutational alterations in the homotetrameric chaperone SecB that implicate the structure as dimer of dimers. Murén EM, et al. J Biol Chem, 1999 Jul 2. PMID 10383453
    2. Crystallization of the chaperone protein SecB. Vrielink A, et al. Protein Sci, 1995 Aug. PMID 8520492, Free PMC Article
    3. Electrospray mass spectrometric investigation of the chaperone SecB. Smith VF, et al. Protein Sci, 1996 Mar. PMID 8868485, Free PMC Article
    4. Identification of a sequence motif that confers SecB dependence on a SecB-independent secretory protein in vivo. Kim J, et al. J Bacteriol, 1998 Mar. PMID 9515905, Free PMC Article
    5. SecB: a chaperone from Escherichia coli. Randall LL, et al. Methods Enzymol, 1998. PMID 9534181

    See all (103) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. The model of interactions presented suggests a way that binding between SecA and SecB might decrease the affinity of precursor polypeptides for SecB and facilitate the transfer to SecA.
      Title: The basis of asymmetry in the SecA:SecB complex.
    2. Demonstrated directly an interaction between the N-terminal residues 2 through 11 of SecA and the C-terminal 13 residues of SecB by isothermal titration calorimetry and analytical sedimentation velocity centrifugation.
      Title: Direct identification of the site of binding on the chaperone SecB for the amino terminus of the translocon motor SecA.
    3. the structure of the SecB/OmpA complex was visualized by electron microscopy. The binding pattern between SecB tetramer and OmpA is asymmetric.
      Title: The structure of SecB/OmpA as visualized by electron microscopy: The mature region of the precursor protein binds asymmetrically to SecB.
    4. SecB exhibits the remarkable ability to bind a diverse group of ligands recognizing them by virtue of the fact that they have non-native structure.
      Title: Export chaperone SecB uses one surface of interaction for diverse unfolded polypeptide ligands.
    5. Variants of SecA and of SecB that populate complexes were used to examine both the hydrolysis of ATP and the translocation of polypeptides.
      Title: Maximal efficiency of coupling between ATP hydrolysis and translocation of polypeptides mediated by SecB requires two protomers of SecA.
    6. effect of chaperone SecB on folding & unfolding pathways of maltose binding protein at the single-molecule level; interactions with SecB prevent stable tertiary contacts in core structure but have no detectable effect on folding of external alpha helices
      Title: Direct observation of chaperone-induced changes in a protein folding pathway.
    7. N-terminus verified by Edman degradation on mature peptide
      Title: Purification of the Escherichia coli secB gene product and demonstration of its activity in an in vitro protein translocation system.
    8. structural details of SecA on lipid layers; the pore structure is altered after transferring crystals to the SecB solution, indicating that the lipid-specific SecA structure has the SecB binding activity.
      Title: The active ring-like structure of SecA revealed by electron crystallography: conformational change upon interaction with SecB.
    9. SecB and SecA display twofold symmetry and yet the complex between the two is stabilized by contacts that are distributed asymmetrically, we identify a third distinct region of their interaction
      Title: Characterization of three areas of interactions stabilizing complexes between SecA and SecB, two proteins involved in protein export.
    10. binding between the two symmetric molecules is asymmetric and that the C-terminal alpha-helices of SecB bind in the interfacial region of the SecA dimer
      Title: Asymmetric binding between SecA and SecB two symmetric proteins: implications for function in export.
    Submit: New GeneRIF Correction See all GeneRIFs (12)

    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 preprotein binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    enables unfolded protein binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables unfolded protein binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables unfolded protein binding IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    Process Evidence Code Pubs
    involved_in maintenance of unfolded protein IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in maintenance of unfolded protein IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in protein folding IEA
    Inferred from Electronic Annotation
    more info
    		  
    acts_upstream_of_or_within protein localization IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    acts_upstream_of_or_within protein targeting IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in protein tetramerization IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in protein transport IEA
    Inferred from Electronic Annotation
    more info
    		  
    acts_upstream_of_or_within protein transport IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    acts_upstream_of_or_within protein transport by the Sec complex IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    Component Evidence Code Pubs
    located_in cytoplasm IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in cytosol IDA
    Inferred from Direct Assay
    more info
    		 PubMed 

    General protein information

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    Preferred Names
    protein export chaperone SecB

    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
      3783661..3784128 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_418066.1 protein export chaperone SecB [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_418066.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A5B9APM8, A0A775TGS4
      Conserved Domains (1) summary
      PRK05751
      Location:1 → 151
      PRK05751; preprotein translocase subunit SecB; Validated
    Nucleotide Protein
    Heading Accession and Version

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