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    secA protein translocation ATPase [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 944821, updated on 17-Dec-2024

    Summary

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    Official Symbol
    secA
    Official Full Name
    protein translocation ATPase
    Primary source
    ECOCYC:EG10936
    Locus tag
    b0098
    See related
    ASAP:ABE-0000343
    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
    azi; ECK0099; pea; prlD
    Summary
    Helicase activity is dispensable for both functions. [More information is available at EcoGene: EG10936]. SecA is an inner membrane component of the Sec Protein secretion system and is peripherally associated with the multi-subunit translocation apparatus SecYEG. [More information is available at EcoCyc: EG10936].
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    Genomic context

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    Sequence:
    NC_000913.3 (108279..110984)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene UDP-3-O-acyl-N-acetylglucosamine deacetylase Neighboring gene SecA translation regulator Neighboring gene 8-oxo-dGTP diphosphatase Neighboring gene DNA gyrase inhibitor YacG

    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. Integration of SecA protein into the Escherichia coli inner membrane is regulated by its amino-terminal ATP-binding domain. Rajapandi T, et al. Mol Microbiol, 1996 Apr. PMID 8861203
    2. Probing the affinity of SecA for signal peptide in different environments. Musial-Siwek M, et al. Biochemistry, 2005 Oct 25. PMID 16229488, Free PMC Article
    3. The catalytic cycle of the escherichia coli SecA ATPase comprises two distinct preprotein translocation events. van der Wolk JP, et al. EMBO J, 1997 Dec 15. PMID 9405359, Free PMC Article
    4. Identification of the preprotein binding domain of SecA. Papanikou E, et al. J Biol Chem, 2005 Dec 30. PMID 16243836
    5. The low-affinity ATP binding site of the Escherichia coli SecA dimer is localized at the subunit interface. van der Wolk JP, et al. Biochemistry, 1997 Dec 2. PMID 9398216

    See all (244) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Topology of the SecA ATPase Bound to Large Unilamellar Vesicles.
      Title: Topology of the SecA ATPase Bound to Large Unilamellar Vesicles.
    2. Unsaturated fatty acids augment protein transport via the SecA:SecYEG translocon.
      Title: Unsaturated fatty acids augment protein transport via the SecA:SecYEG translocon.
    3. Membrane Insertion of the M13 Minor Coat Protein G3p Is Dependent on YidC and the SecAYEG Translocase.
      Title: Membrane Insertion of the M13 Minor Coat Protein G3p Is Dependent on YidC and the SecAYEG Translocase.
    4. Cellular dynamics of the SecA ATPase at the single molecule level.
      Title: Cellular dynamics of the SecA ATPase at the single molecule level.
    5. Single-molecule analysis of dynamics and interactions of the SecYEG translocon.
      Title: Single-molecule analysis of dynamics and interactions of the SecYEG translocon.
    6. Iron is a ligand of SecA-like metal-binding domains in vivo.
      Title: Iron is a ligand of SecA-like metal-binding domains in vivo.
    7. The SecA ATPase motor protein binds to Escherichia coli liposomes only as monomers.
      Title: The SecA ATPase motor protein binds to Escherichia coli liposomes only as monomers.
    8. The N terminus and the helical linker domain of ATPase SecA bind to an acidic patch on the surface of the ribosomal protein uL23. both also insert deeply into the ribosomal tunnel to contact the intratunnel loop of uL23, which serves as a nascent chain sensor. This binding pattern is similar to that of signal recognition particle and indicates an identical interaction mode of the two targeting factors with ribosomes.
      Title: Molecular Mimicry of SecA and Signal Recognition Particle Binding to the Bacterial Ribosome.
    9. Starting from nearly identical initial states, SecA more readily dissociated from SecYEG when engaged with the precursor of outer membrane protein A as compared to the precursor of galactose-binding protein.
      Title: Direct visualization of the E. coli Sec translocase engaging precursor proteins in lipid bilayers.
    10. This mode of oligomerization, which depends on binding of the extreme N-terminus to the DEAD motor domains, NBD1 and NBD2, was used to model a novel parallel and flexible SecA solution dimer that agrees well with SAXS data.
      Title: An alternate mode of oligomerization for E. coli SecA.
    Submit: New GeneRIF Correction See all GeneRIFs (67)

    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 ATP binding IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables ATP binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables identical protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    enables metal ion binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables preprotein binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    enables protein-exporting ATPase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables ribonucleoprotein complex binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables ribosome binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    enables zinc ion binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    Process Evidence Code Pubs
    involved_in chaperone-mediated protein folding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in intracellular protein transmembrane transport IEA
    Inferred from Electronic Annotation
    more info
    		  
    acts_upstream_of_or_within intracellular protein transmembrane transport IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in intracellular protein transmembrane transport IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in intracellular protein transport IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in protein import IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in protein secretion IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in protein targeting IEA
    Inferred from Electronic Annotation
    more info
    		  
    acts_upstream_of_or_within protein targeting IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in protein targeting to membrane IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    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 
    involved_in protein transport by the Sec complex IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in protein transport by the Sec complex IDA
    Inferred from Direct Assay
    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
    part_of cell envelope Sec protein transport complex IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    part_of cell envelope Sec protein transport complex IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in cytoplasm IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in cytoplasm IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in cytoplasmic side of plasma membrane IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    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
    		  

    General protein information

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    Preferred Names
    protein translocation ATPase

    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
      108279..110984
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_414640.1 protein translocation ATPase [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_414640.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A8S7I0K7
      Conserved Domains (1) summary
      PRK12904
      Location:2 → 901
      PRK12904; preprotein translocase subunit SecA; Reviewed
    Nucleotide Protein
    Heading Accession and Version

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