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Literature summary for 7.4.2.5 extracted from

  • Morita, K.; Tokuda, H.; Nishiyama, K.
    Multiple SecA molecules drive protein translocation across a single translocon with SecG inversion (2012), J. Biol. Chem., 287, 455-464.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 7.4.2.5

Protein Variants

Protein Variants Comment Organism
D209A a dominant-negative mutant, binds ATP but is unable to hydrolyze it and is inactive in proOmpA translocation. Mutant generates a translocation intermediate of 18 kDa. Further addition of wild-type SecA causes its translocation into either mature OmpA or another intermediate of 28 kDa that can be translocated into mature by a proton motive force. The addition of excess D209N SecA during translocation causes a topology inversion of SecG Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane inner membrane Escherichia coli 16020
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Organism

Organism UniProt Comment Textmining
Escherichia coli
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General Information

General Information Comment Organism
physiological function multiple SecA molecules drive translocation across a single translocon with SecG inversion. Model of proOmpA translocation suggests that a single catalytic cycle of SecA causes translocation of 10–13 kDa with ATP binding and hydrolysis, and SecG inversion is required when the next SecA cycle begins with additional ATP hydrolysis Escherichia coli