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    tatB twin arginine protein translocation system - TatB protein [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 948319, updated on 24-Dec-2024

    Summary

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    Official Symbol
    tatB
    Official Full Name
    twin arginine protein translocation system - TatB protein
    Primary source
    ECOCYC:G7808
    Locus tag
    b3838
    See related
    ASAP:ABE-0012545
    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
    ECK3831; mttA2; ysgB
    Summary
    Forms a complex with TatAC. [More information is available at EcoGene: EG14322]. TatB is a component of the TatABCE (twin-arginine translocation) complex for the export of folded proteins. [More information is available at EcoCyc: G7808].
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    Genomic context

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    Sequence:
    NC_000913.3 (4022218..4022733)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene ubiquinone biosynthesis accessory factor UbiJ Neighboring gene ncRNA Neighboring gene ubiquinone biosynthesis protein UbiB Neighboring gene twin arginine protein translocation system - TatA protein Neighboring gene twin arginine protein translocation system - TatC protein Neighboring gene 3' -> 5' ssDNA/RNA exonuclease TatD Neighboring gene transcription antiterminator RfaH

    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. Twin-arginine translocase component TatB performs folding quality control via a chaperone-like activity. Taw MN, et al. Sci Rep, 2022 Sep 1. PMID 36050356, Free PMC Article
    2. Twin-arginine translocation-arresting protein regions contact TatA and TatB. Taubert J, et al. Biol Chem, 2014 Jul. PMID 25003386
    3. Characterisation of the membrane-extrinsic domain of the TatB component of the twin arginine protein translocase. Maldonado B, et al. FEBS Lett, 2011 Feb 4. PMID 21237157
    4. TatBC, TatB, and TatC form structurally autonomous units within the twin arginine protein transport system of Escherichia coli. Orriss GL, et al. FEBS Lett, 2007 Aug 21. PMID 17686475, Free PMC Article
    5. The entire N-terminal half of TatC is involved in twin-arginine precursor binding. Holzapfel E, et al. Biochemistry, 2007 Mar 13. PMID 17300178

    See all (102) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. TatA and TatB generate a hydrophobic mismatch important for the function and assembly of the Tat translocon in Escherichia coli.
      Title: TatA and TatB generate a hydrophobic mismatch important for the function and assembly of the Tat translocon in Escherichia coli.
    2. Twin-arginine translocase component TatB performs folding quality control via a chaperone-like activity.
      Title: Twin-arginine translocase component TatB performs folding quality control via a chaperone-like activity.
    3. Hydrophobic mismatch is a key factor in protein transport across lipid bilayer membranes via the Tat pathway.
      Title: Hydrophobic mismatch is a key factor in protein transport across lipid bilayer membranes via the Tat pathway.
    4. It has been concluded that Tat signal peptides play roles in substrate targeting and in triggering assembly of the active TatABC translocase.
      Title: A signal sequence suppressor mutant that stabilizes an assembled state of the twin arginine translocase.
    5. In the TatBC receptor complex the transmembrane helix of each TatB molecule is sandwiched between two TatC molecules, with one of the inter-subunit interfaces incorporating a functionally important cluster of interacting polar residues. Unexpectedly, the authors find that TatA also associates with TatC at the polar cluster site.
      Title: Assembling the Tat protein translocase.
    6. In vitro cross-linking of residues located in the periplasmically-oriented part of the TatBC receptor to TorA[KQ]-30aa-MalE reporter variants harboring a more hydrophobic h-region in their signal peptides confirmed that unlike in TorA[KQ]-30aa-MalE with an unaltered h-region, the mutated reporters moved deep into the TatBC-binding cavity.
      Title: The h-region of twin-arginine signal peptides supports productive binding of bacterial Tat precursor proteins to the TatBC receptor complex.
    7. Twin-arginine translocation (Tat) system TatA exhibits a uniform distribution throughout the inner membrane and that altering the expression of TatBC shows a uncharacterised distribution of TatA in the inner membrane.
      Title: TatA complexes exhibit a marked change in organisation in response to expression of the TatBC complex.
    8. we confirm the evidence of interactions between TatC fragments and DmsD chaperone. Using a peptide overlapping array, it was shown that the different NarJ subfamily REMPs interact with different regions of the TatB cytoplasmic domains
      Title: Identification of protein-protein interactions between the TatB and TatC subunits of the twin-arginine translocase system and respiratory enzyme specific chaperones.
    9. Distributed TatA thus may serve to accompany membrane-interacting Tat substrates to the few TatBC spots in the cells.
      Title: TatBC-independent TatA/Tat substrate interactions contribute to transport efficiency.
    10. The data thus suggest that mature protein domains are translocated through a TatA and TaTB environment.
      Title: Twin-arginine translocation-arresting protein regions contact TatA and TatB.
    Submit: New GeneRIF Correction See all GeneRIFs (22)

    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 identical protein binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables identical protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    enables protein binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    enables protein homodimerization activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables protein transmembrane transporter activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables proton motive force dependent protein transmembrane transporter activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    Process Evidence Code Pubs
    acts_upstream_of_or_within intracellular protein transmembrane transport IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    acts_upstream_of_or_within intracellular protein transmembrane transport IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in protein transport IEA
    Inferred from Electronic Annotation
    more info
    		  
    acts_upstream_of_or_within protein transport by the Tat complex IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in protein transport by the Tat complex IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in protein transport by the Tat complex NAS
    Non-traceable Author Statement
    more info
    		 PubMed 
    Component Evidence Code Pubs
    part_of TAT protein transport complex IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    part_of TAT protein transport complex IEA
    Inferred from Electronic Annotation
    more info
    		  
    part_of TAT protein transport complex NAS
    Non-traceable Author Statement
    more info
    		 PubMed 
    located_in membrane IEA
    Inferred from Electronic Annotation
    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 ISM
    Inferred from Sequence Model
    more info
    		 PubMed 
    located_in plasma membrane NAS
    Non-traceable Author Statement
    more info
    		 PubMed 

    General protein information

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    Preferred Names
    twin arginine protein translocation system - TatB protein

    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
      4022218..4022733
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. YP_026270.1 twin arginine protein translocation system - TatB protein [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for YP_026270.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A418GQ87
      Conserved Domains (1) summary
      PRK01770
      Location:1 → 171
      PRK01770; Sec-independent protein translocase subunit TatB
    Nucleotide Protein
    Heading Accession and Version

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