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secB [ Escherichia coli str. K-12 substr. MG1655 ]

Gene ID: 948123, updated on 24-Aug-2024

Summary

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Official Symbol
secB
Primary source
ASAP:ABE-0011798
Locus tag
b3609
See related
ECOCYC:EG10937
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. SecB-mediated protein export need not occur via kinetic partitioning. Krishnan B, et al. J Mol Biol, 2009 Jan 30. PMID 19028503
  2. Sites of interaction of a precursor polypeptide on the export chaperone SecB mapped by site-directed spin labeling. Crane JM, et al. J Mol Biol, 2006 Oct 13. PMID 16962134, Free PMC Article
  3. SecB is a bona fide generalized chaperone in Escherichia coli. Ullers RS, et al. Proc Natl Acad Sci U S A, 2004 May 18. PMID 15128935, Free PMC Article
  4. Crystal structure of SecB from Escherichia coli. Dekker C, et al. J Struct Biol, 2003 Dec. PMID 14643199
  5. Characterisation of preYvaY export reveals differences in the substrate specificities of Bacillus subtilis and Escherichia coli leader peptidases. Linde D, et al. FEMS Microbiol Lett, 2003 Oct 10. PMID 14568161

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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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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