EC Number   |
General Information |
Reference |
|---|
   7.4.2.5 | malfunction |
enzyme ablation results in 3-5fold reduction in the in vivo rate and extent of valacyclovir absorption |
733688 |
| 7.4.2.5 | physiological function |
Both SecA and the ribosome need to interact with the translocon during membrane protein insertion. SecA and ribosome binding to the translocon is mutually exclusive, implying that during membrane protein insertion, both ligands bind the translocon in a sequential manner |
-, 720060 |
| 7.4.2.5 | physiological function |
mechanism of Sap-mediated import of antimicrobial peptides, a strategy to reduce periplasmic and inner membrane accumulation of these host defense peptides. Antimicrobial peptides localize to the bacterial cytoplasm of the wild-type strain and are susceptible to cytoplasmic peptidase activity. In bacteria lacking a functional Sap permease complex, antimicrobial peptides accumulate in the periplasm. The periplasmic binding protein SapA binds antimicrobial peptides and is required for virulence in vivo |
720880 |
| 7.4.2.5 | 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 1013 kDa with ATP binding and hydrolysis, and SecG inversion is required when the next SecA cycle begins with additional ATP hydrolysis |
720044 |
| 7.4.2.5 | physiological function |
role for the SecA2 pathway in the cell wall localization of solute binding proteins that work with ABC transporters to import solutes. Additionally, SecA2 has a profound effect on the cell wall localization of the Mce1 and Mce4 lipid transporters, which contribute to Mycobacterium tuberculosis virulence. A relationship exists between SecA2 and the hypoxia-induced DosR regulon associated with Mycobacterium tuberculosis latency. Nearly half of the transcriptionally controlled DosR regulon of cytoplasmic proteins are detected at higher levels in the secA2 mutant versus wild-type |
-, 734686 |
| 7.4.2.5 | physiological function |
SecA ATPase associates with the SecY complex to push preproteins across the bacterial membrane. One SecY copy is sufficient to bind SecA and the preprotein, but only the SecY dimer together with acidic lipids supports the activation of the SecA translocation ATPase. In nanodiscs, the dimer is predominantly arranged in a back-to-back manner and remains active even if a constituent SecY copy is defective for SecA binding. In membrane vesicles and in intact cells, the coproduction of two inactive SecYs, one for channel gating and the other for SecA binding, recreates a functional translocation unit |
720940 |
| 7.4.2.5 | physiological function |
Similarly to a SecA2 deletion mutant, a SecA2 ATPase bearing a mutated nucleotide binding site exhibits rough colonies, a bacterial chaining phenotype, an impaired protein secretion profile, and in vivo virulence in comparison to wild-type Listeria monocytogenes. Mice immunized with the SecA2 nucelotide binding site mutant are not protected against secondary infection with wild-type Listeria monocytogenes and do not develop CCL3+ memory CD8+ T cells |
719587 |
| 7.4.2.5 | physiological function |
the enzyme contributes to water absorption in the colon |
733062 |
