ReviewMicrobiology spectrum2019
The Two Distinct Types of SecA2-Dependent Export Systems.
Review in Microbiology spectrum, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
19 citing papers in PubMed, 22 citations in OpenAlex.
- Comparative genomic and functional analysis of Staphylococcus caprae clinical isolates: insights into genetic diversity and opportunistic pathogenic potential.Archives of microbiology · 2026Article
- Integrated Genomics and Phenotypic Analysis ofMicroorganisms · 2026Article
- Genetic engineering ofMicrobial genomics · 2026Article
- A structural basis for the strain-dependent UDP-sugar specificity of glycosyltransferase C from the Limosilactobacillus reuteri accessory secretion system.Acta crystallographica. Section D, Structural biology · 2025Article
- Protein trafficking across the cell envelope of gram-positive bacteria.Journal of bacteriology · 2025Review
- Optimizing a Subunit Vaccine ofIranian journal of public health · 2025Article
- Cold induced expression of a novel levansucrase gene sacB1 enhances exopolysaccharide production and stress resilience in Leuconostoc mesenteroides.Scientific reports · 2025Article
- Structure, Function, and Regulation of LytA: TheMicroorganisms · 2025Review
- Review
- Screening a library of temperature-sensitive mutants to identify secretion factors inJournal of bacteriology · 2025Article
- A conserved bacterial genetic basis for commensal-host specificity.Science (New York, N.Y.) · 2024Article
- Phylogenomic analyses of multidrug resistant Corynebacterium striatum strains isolated from patients in a tertiary care hospital in the UK.European journal of clinical microbiology & infectious diseases : official publication of the European Society of Clinical Microbiology · 2024Article
- Virulence Factors ofPathogens (Basel, Switzerland) · 2023Review
- Mycobacterium smegmatis: The Vanguard of Mycobacterial Research.Journal of bacteriology · 2023Review
- The first genomic characterization of a stable, hemin-dependent small colony variant strain ofFrontiers in microbiology · 2023Article
- Inter-species diversity and functional genomic analyses of closed genome assemblies of clinically isolated, megaplasmid-containingAccess microbiology · 2023Article
- The Type VII Secretion System ofAnnual review of microbiology · 2021Article
- Streptococcal Serine-Rich Repeat Proteins in Colonization and Disease.Frontiers in microbiology · 2020Review
- O-acetylation controls the glycosylation of bacterial serine-rich repeat glycoproteins.The Journal of biological chemistryArticle
Corrections and comments
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Authors and funding
3 authors at 3 institutions in 1 country.
Funding
Abstract
In addition to SecA of the general Sec system, many Gram-positive bacteria, including mycobacteria, express SecA2, a second, transport-associated ATPase. SecA2s can be subdivided into two mechanistically distinct types: (i) SecA2s that are part of the accessory Sec (aSec) system, a specialized transporter mediating the export of a family of serine-rich repeat (SRR) glycoproteins that function as adhesins, and (ii) SecA2s that are part of multisubstrate systems, in which SecA2 interacts with components of the general Sec system, specifically the SecYEG channel, to export multiple types of substrates. Found mainly in streptococci and staphylococci, the aSec system also contains SecY2 and novel accessory Sec proteins (Asps) that are required for optimal export. Asp2 also acetylates glucosamine residues on the SRR domains of the substrate during transport. Targeting of the SRR substrate to SecA2 and the aSec translocon is mediated by a specialized signal peptide. Multisubstrate SecA2 systems are present in mycobacteria, corynebacteria, listeriae, clostridia, and some bacillus species. Although most substrates for this SecA2 have canonical signal peptides that are required for export, targeting to SecA2 appears to depend on structural features of the mature protein. The feature of the mature domains of these proteins that renders them dependent on SecA2 for export may be their potential to fold in the cytoplasm. The discovery of aSec and multisubstrate SecA2 systems expands our appreciation of the diversity of bacterial export pathways. Here we present our current understanding of the mechanisms of each of these SecA2 systems.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.