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secA [Fri Dec 30 2016 17:42:22 GMT+0100 (CET)]
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secA [Fri Dec 30 2016 17:42:22 GMT+0100 (CET)]

preprotein translocase subunit (ATPase), required for membrane targeting of DivIVA, motor protein that drives preprotein translocation through the SecY-SecE-SecG channel
locus
BSU35300
pI
5.00
mw
95.00 kDa
function
protein secretion
product
preprotein translocase subunit (ATPase)
essential
yes
synonyms
div, div-341, ts-341
Outlinks
KEGGBsubCycSubtiListUniProtExpression Browser

Genomic Context

      

categories

  • [category|SW 3|Information processing] → [category|SW 3.3|Protein synthesis, modification and degradation] → [category|SW 3.3.5|Protein secretion]
  • [category|SW 6|Groups of genes] → [category|SW 6.1|Essential genes]
  • [category|SW 6|Groups of genes] → [category|SW 6.2|Membrane proteins]

    • [SW|Categories] containing this gene/protein

  • [SW|protein secretion], [SW|essential genes], [SW|membrane proteins]

    • Gene

    Coordinates on the chromosome (coding sequence)
    3,628,310 -> 3,630,835

    Phenotypes of a mutant

  • essential [Pubmed|12682299]
  • terminal phenotype of CRISPRi knockdown mutant is moderate bending and a cessation of growth [Pubmed|27238023]

    • The protein

    Catalyzed reaction/ biological activity

  • ATP -> ADP Pi preprotein translocation
  • required for membrane targeting of [SW|DivIVA] [Pubmed|24592260]

    • Protein family

  • SecA family (according to Swiss-Prot)

    • Paralogous protein(s)

  • none in Bacillus, some species have a paralogous secA gene named secA2 that has an altered substrate range

    • [SW|Domains]

  • nucleotide binding domain, preprotein binding domain, IRA2 domain, scaffold domain, wing domain, IRA1 domain, C-terminal domain

    • [SW|Cofactors]

  • Mg

    • Effectors of protein activity

  • anionic phospholipids, preprotein, [protein|search|SecY], signal peptides (even when added in trans) [Pubmed|19924216]

    • Structure

  • [PDB|1TF5] (open structure), [PDB|2IBM], [PDB|3DL8] (structure of the ([protein|search|SecY]-[protein|search|SecE]-[protein|search|SecG])-[protein|search|SecA] complex [Pubmed|18923516]

    • [SW|Localization]

  • cell membrane (according to Swiss-Prot)

    • [SW|Interactions]

  • ([protein|search|SecY]-[protein|search|SecE]-[protein|search|SecG])2-[protein|search|SecA]2 [Pubmed|18923516]
  • [protein|search|SecA]-[protein|search|Ffh] [Pubmed|9880811]
  • [protein|search|CsaA]-[protein|search|SecA] [Pubmed|10816431]
  • [SW|DivIVA]-[protein|search|SecA] [Pubmed|24592260]

    • Additional information

  • subject to Clp-dependent proteolysis upon glucose starvation [PubMed|17981983]

    • Expression and Regulation

    Operon

  • ''[protein|search|secA]-[protein|search|prfB]'' [Pubmed|9882663]

    • [SW|Sigma factor]

  • [protein|search|SigA] [Pubmed|9882663]

    • Additional information

  • subject to Clp-dependent proteolysis upon glucose starvation [PubMed|17981983]

    • Biological materials

    Mutant

  • BEC35300, a CRISPRi knockdown mutant, is available from the [http://bgsc.org/ Bacillus Genetic Stock Center]

    • References

    Reviews

  • 25212246,27890920,27799326

    • Original publications

  • 19933328,19924216,18923516,12873133,12242434,1385592,10816431,19850053,9880811,12218047,17981983,9882663,23484952,20574771,23167435,23794293,23852076,24592260,24786965,11021932,7851746,7894702,10074074,8497195,8440733,7706219,7642557,27336478,27238023,27795329