ArticleInfection and immunity2011
Identification of an ATPase, MsmK, which energizes multiple carbohydrate ABC transporters in Streptococcus pneumoniae.
Article in Infection and immunity, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
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Who cites it
46 citing papers in PubMed, 74 citations in OpenAlex.
- Structural studies and functional engineering of NanX: an anhydro-sialic acid transporter from Escherichia coli.FEBS open bio · 2026Article
- Ligand-binding properties of substrate binding proteins of a maltose uptake system inMicrobiology (Reading, England) · 2026Article
- Characterisation of anhydro-sialic acid transporters from mucosa-associated bacteria.Microbiology (Reading, England) · 2024Article
- Article
- A multiomics analysis of direct interkingdom dynamics between influenza A virus and Streptococcus pneumoniae uncovers host-independent changes to bacterial virulence fitness.PLoS pathogens · 2022Article
- ATP-Binding Cassette Transporters: Snap-on Complexes?Sub-cellular biochemistry · 2022Article
- Comparison of carbohydrate ABC importers from Mycobacterium tuberculosis.BMC genomics · 2021Article
- Transcriptional Regulation of Plant Biomass Degradation and Carbohydrate Utilization Genes in the Extreme ThermophilemSystems · 2021Article
- Multiple evolutionary origins reflect the importance of sialic acid transporters in the colonization potential of bacterial pathogens and commensals.Microbial genomics · 2021Article
- Streptococcus suis MsmK: Novel Cell Division Protein Interacting with FtsZ and Maintaining Cell Shape.mSphere · 2021Article
- The repertoire of ABC proteins inComputational and structural biotechnology journal · 2021Article
- Structural characterization of two solute-binding proteins forJournal of structural biology: X · 2021Article
- Multitask ATPases (NBDs) of bacterial ABC importers type I and their interspecies exchangeability.Scientific reports · 2020Article
- Involvement of Various Enzymes in the Physiology and Pathogenesis ofVeterinary sciences · 2020Review
- Host-glycan metabolism is regulated by a species-conserved two-component system in Streptococcus pneumoniae.PLoS pathogens · 2020Article
- Molecular analysis of an enigmaticThe Journal of biological chemistry · 2019Article
- An Uncharacterized Member of the Gls24 Protein Superfamily Is a Putative Sensor of Essential Amino Acid Availability in Streptococcus pneumoniae.Microbial ecology · 2019Article
- Article
- Characterization of a Signaling System in Streptococcus mitis That Mediates Interspecies Communication with Streptococcus pneumoniae.Applied and environmental microbiology · 2019Article
- "Just a spoonful of sugar...": import of sialic acid across bacterial cell membranes.Biophysical reviews · 2018Review
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Streptococcus pneumoniae is the leading cause of community-acquired pneumonia and results in over 1 million deaths each year worldwide. Asymptomatic colonization of the airway precedes disease, and acquisition of carbohydrates from the host environment is necessary for bacterial survival. We previously demonstrated that S. pneumoniae cleaves sialic acid from human glycoconjugates to be used as a carbohydrate source. The satABC genes are required for growth and import of sialic acid. The satABC genes are predicted to encode components of an ABC transporter but not the ATPases essential to energize transport. As this subunit is essential, an ATPase must be encoded elsewhere in the genome. We identified msmK as a candidate based on similarity to other known carbohydrate ATPases. Recombinant MsmK hydrolyzed ATP, revealing that MsmK is an ATPase. An msmK mutant was reduced in growth on and transport of sialic acid, demonstrating that MsmK is the ATPase energizing the sialic acid transporter. In addition to satABC, S. pneumoniae contains five other loci that are predicted to encode CUT1 family carbohydrate ABC transporter components; each of these lacks a predicted ATPase. Data indicate that msmK is also required for growth on raffinose and maltotetraose, which are the substrates of two other characterized carbohydrate ABC transporters. Furthermore, an msmK mutant was reduced in airway colonization. Together, these data imply that in vivo, MsmK energizes multiple carbohydrate transporters in S. pneumoniae. This is the first demonstration of a shared ATPase in a pathogenic bacterium.
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