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

Gene ID: 944821, updated on 10-Oct-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, A0AAQ2R8J3
    Conserved Domains (1) summary
    PRK12904
    Location:2 → 901
    PRK12904; preprotein translocase subunit SecA; Reviewed
Nucleotide Protein
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