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

    Gene ID: 948328, updated on 24-Dec-2024

    Summary

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    Official Symbol
    tatC
    Official Full Name
    twin arginine protein translocation system - TatC protein
    Primary source
    ECOCYC:EG11479
    Locus tag
    b3839
    See related
    ASAP:ABE-0012547
    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
    ECK3832; mttB; yigU; yigV
    Summary
    Topology mapped using protein fusions. [More information is available at EcoGene: EG11479]. TatC is a subunit of the TatABCE (twin-arginine translocation) complex for the export of folded proteins across the cytoplasmic membrane. [More information is available at EcoCyc: EG11479].
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    Genomic context

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    Sequence:
    NC_000913.3 (4022736..4023512)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene twin arginine protein translocation system - TatA protein Neighboring gene twin arginine protein translocation system - TatB protein Neighboring gene 3' -> 5' ssDNA/RNA exonuclease TatD Neighboring gene transcription antiterminator RfaH Neighboring gene 3-octaprenyl-4-hydroxybenzoate decarboxylase

    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. Genetic evidence for a TatC dimer at the core of the Escherichia coli twin arginine (Tat) protein translocase. Maldonado B, et al. J Mol Microbiol Biotechnol, 2011. PMID 21709427
    2. Cysteine scanning mutagenesis and topological mapping of the Escherichia coli twin-arginine translocase TatC Component. Punginelli C, et al. J Bacteriol, 2007 Aug. PMID 17545291, Free PMC Article
    3. Escherichia coli tatC mutations that suppress defective twin-arginine transporter signal peptides. Strauch EM, et al. J Mol Biol, 2007 Nov 23. PMID 17936785, Free PMC Article
    4. The TatC component of the twin-arginine protein translocase functions as an obligate oligomer. Cléon F, et al. Mol Microbiol, 2015 Oct. PMID 26112072, Free PMC Article
    5. A Link between Integral Membrane Protein Expression and Simulated Integration Efficiency. Marshall SS, et al. Cell Rep, 2016 Aug 23. PMID 27524616, Free PMC Article

    See all (111) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. 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.
    2. A link between integral membrane protein TatC expression and simulated integration efficiency has been presented.
      Title: A Link between Integral Membrane Protein Expression and Simulated Integration Efficiency.
    3. 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.
    4. 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.
    5. 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.
    6. Findings show that TatC functions as an obligate oligomer
      Title: The TatC component of the twin-arginine protein translocase functions as an obligate oligomer.
    7. 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.
    8. 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.
    9. While translocation of loops 1 and 2 of TatC is strictly dependent on the Sec translocase and the YidC insertase, translocation of loop 3 does not depend on the translocase or insertase.
      Title: Both YidC and SecYEG are required for translocation of the periplasmic loops 1 and 2 of the multispanning membrane protein TatC.
    10. A physical interaction between TatC helix 5 and the TatB transmembrane helix was confirmed by the formation of a site-specific disulphide bond between TatC M205C and TatB L9C variants.
      Title: Molecular dissection of TatC defines critical regions essential for protein transport and a TatB-TatC contact site.
    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 protein binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    enables protein transmembrane transporter activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables protein transmembrane transporter activity IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    enables proton motive force dependent protein transmembrane transporter activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables proton motive force dependent protein transmembrane transporter activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    Process Evidence Code Pubs
    involved_in intracellular protein transmembrane transport IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    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
    		  
    involved_in protein transport by the Tat complex IBA
    Inferred from Biological aspect of Ancestor
    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 
    acts_upstream_of_or_within response to radiation IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    Component Evidence Code Pubs
    part_of TAT protein transport complex IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    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 IDA
    Inferred from Direct Assay
    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 - TatC 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
      4022736..4023512
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_418282.1 twin arginine protein translocation system - TatC protein [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_418282.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A8S0FHD2
      Conserved Domains (1) summary
      PRK10921
      Location:1 → 258
      PRK10921; Sec-independent protein translocase subunit TatC
    Nucleotide Protein
    Heading Accession and Version

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