ArticleBMC genomics2008
Phylogenetic distribution and membrane topology of the LytR-CpsA-Psr protein family.
Article in BMC genomics, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.
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Who cites it
48 citing papers in PubMed, 83 citations in OpenAlex.
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- Rv3839-Rv3840 links the endogenous heme biosynthesis pathway withbioRxiv : the preprint server for biology · 2026Article
- Naturally occurring dinactin targets cpsA protein and kills Mycobacterium tuberculosis by disrupting the proton motive force.Communications biology · 2026Article
- Impairment of two non-essential LytR-cpsA-psr (Lcp) cell wall ligases decelerate cell wall assembly in Mycolicibacterium smegmatis.BMC microbiology · 2026Article
- ACA kills Mycobacterium tuberculosis and M. bovis by targeting cell wall core assembling protein CpsA.Communications biology · 2025Article
- Evidence that glycopolymer transferases promote peptidoglycan hydrolysis inbioRxiv : the preprint server for biology · 2025Article
- Article
- Structural insights of an LCP protein-LytR-fromFrontiers in chemistry · 2024Article
- Encapsulation of the septal cell wall protects Streptococcus pneumoniae from its major peptidoglycan hydrolase and host defenses.PLoS pathogens · 2022Article
- The LCP Family Protein, Psr, Is Required for Cell Wall Integrity and Virulence inMicroorganisms · 2022Article
- LytR-CpsA-Psr Glycopolymer Transferases: Essential Bricks in Gram-Positive Bacterial Cell Wall Assembly.International journal of molecular sciences · 2021Review
- LcpB Is a Pyrophosphatase Responsible for Wall Teichoic Acid Synthesis and Virulence inFrontiers in microbiology · 2021Article
- TheMicroorganisms · 2020Review
- Genetic Determinants Enabling Medium-Dependent Adaptation to Nafcillin in Methicillin-Resistant Staphylococcus aureus.mSystems · 2020Article
- Crystallographic analysis ofThe Journal of biological chemistry · 2020Article
- Chitin Attenuates Expression ofFrontiers in microbiology · 2020Article
- Impairment of the Cell Wall Ligase, LytR-CpsA-Psr Protein (LcpC), in Methicillin ResistantFrontiers in microbiology · 2020Article
- Group B Streptococcus Biofilm Regulatory Protein A Contributes to Bacterial Physiology and Innate Immune Resistance.The Journal of infectious diseases · 2018Article
- Deficiency of BrpA in Streptococcus mutans reduces virulence in rat caries model.Molecular oral microbiology · 2018Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundThe bacterial cell wall is the target of many antibiotics and cell envelope constituents are critical to host-pathogen interactions. To combat resistance development and virulence, a detailed knowledge of the individual factors involved is essential. Members of the LytR-CpsA-Psr family of cell envelope-associated attenuators are relevant for beta-lactam resistance, biofilm formation, and stress tolerance, and they are suggested to play a role in cell wall maintenance. However, their precise function is still unknown. This study addresses the occurrence as well as sequence-based characteristics of the LytR-CpsA-Psr proteins.
resultsA comprehensive list of LytR-CpsA-Psr proteins was established, and their phylogenetic distribution and clustering into subgroups was determined. LytR-CpsA-Psr proteins were present in all Gram-positive organisms, except for the cell wall-deficient Mollicutes and one strain of the Clostridiales. In contrast, the majority of Gram-negatives did not contain LytR-CpsA-Psr family members. Despite high sequence divergence, the LytR-CpsA-Psr domains of different subclusters shared a highly similar, predicted mixed a/beta-structure, and conserved charged residues. PhoA fusion experiments, using MsrR of Staphylococcus aureus, confirmed membrane topology predictions and extracellular location of its LytR-CpsA-Psr domain.
conclusionThe LytR-CpsA-Psr domain is unique to bacteria. The presence of diverse subgroups within the LytR-CpsA-Psr family might indicate functional differences, and could explain variations in phenotypes of respective mutants reported. The identified conserved structural elements and amino acids are likely to be important for the function of the domain and will help to guide future studies of the LytR-CpsA-Psr proteins.
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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.