An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. This entry stands for a family of bacterial enzymes that are dedicated to the secretion of one or several closely related proteins belonging to the toxin, protease and lipase families. Examples from Gram-negative bacteria include alpha-hemolysin, cyclolysin, colicin V and siderophores, while examples from Gram-positive bacteria include bacteriocin, subtilin, competence factor and pediocin.
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SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (ABC-type, peptide-exporting)
An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. This entry stands for a family of bacterial enzymes that are dedicated to the secretion of one or several closely related proteins belonging to the toxin, protease and lipase families. Examples from Gram-negative bacteria include alpha-hemolysin, cyclolysin, colicin V and siderophores, while examples from Gram-positive bacteria include bacteriocin, subtilin, competence factor and pediocin.
SecA2 plays a role in Mycobacterium tuberculosis inhibition of the immune response, which is likely important for survival in the host and pathogenesis
SecA2 plays a role in Mycobacterium tuberculosis inhibition of the immune response, which is likely important for survival in the host and pathogenesis
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
subunit SecA1 forms homodimers with an apparent dimer dissociation constant of 65 nM at 30 mM KCl, microscale thermophoresis technique. No binding is observed at 300 mM KCl. Heterodimerization of subunit SecA1 and SecA2 is observed with an apparent Kd of 378 nM while the experiment in high salt buffer shows no interaction. SecA1/SecA2 heterodimers have a significantly lower affinity than the SecA1 or SecA2 homodimer
subunit SecA1 forms homodimers with an apparent dimer dissociation constant of Kd of 161 nM at 30 mM KCl, and a Kd of 618 nM at 150 mM KCl, microscale thermophoresis technique. No binding is observed at 300 mM KCl. Heterodimerization of subunit SecA1 and SecA2 is observed with an apparent Kd of 378 nM while the experiment in high salt buffer shows no interaction. SecA1/SecA2 heterodimers have a significantly lower affinity than the SecA1 or SecA2 homodimer
Label-free quantitative proteomics reveals a role for the Mycobacterium tuberculosis SecA2 pathway in exporting solute binding proteins and Mce transporters to the cell wall