<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>35(4)</volume><submitter>Fiedler SM</submitter><pubmed_abstract>The bacterial cell wall is a meshwork of crosslinked peptidoglycan strands, with a thickness of up to 50 nm in Firmicutes. Little is known about how proteins move through the cell wall to find sites of enzymatic activity. Cell wall synthesis for cell elongation involves the integration of new peptidoglycan strands by integral membrane proteins, as well as the degradation of existing strands by so-called autolysins, soluble proteins that are secreted through the cell membrane. Autolysins comprise different classes of proteases and glucanases and mostly contain cell-wall binding domains in addition to their catalytic domain. We have studied dynamics of &lt;i>Bacillus subtilis&lt;/i> autolysins LytC, a major endopeptidase required for lateral cell wall growth, and LytF, a peptidase acting at the ne</pubmed_abstract><journal>Molecular biology of the cell</journal><pagination>ar55</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC11064672</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Dynamics of cell wall-binding proteins at a single molecule level: &lt;i>B. subtilis&lt;/i> autolysins show different kinds of motion.</pubmed_title><pmcid>PMC11064672</pmcid><pubmed_authors>Fiedler SM</pubmed_authors><pubmed_authors>Graumann PL</pubmed_authors></additional><is_claimable>false</is_claimable><name>Dynamics of cell wall-binding proteins at a single molecule level: &lt;i>B. subtilis&lt;/i> autolysins show different kinds of motion.</name><description>The bacterial cell wall is a meshwork of crosslinked peptidoglycan strands, with a thickness of up to 50 nm in Firmicutes. Little is known about how proteins move through the cell wall to find sites of enzymatic activity. Cell wall synthesis for cell elongation involves the integration of new peptidoglycan strands by integral membrane proteins, as well as the degradation of existing strands by so-called autolysins, soluble proteins that are secreted through the cell membrane. Autolysins comprise different classes of proteases and glucanases and mostly contain cell-wall binding domains in addition to their catalytic domain. We have studied dynamics of &lt;i>Bacillus subtilis&lt;/i> autolysins LytC, a major endopeptidase required for lateral cell wall growth, and LytF, a peptidase acting at the ne</description><dates><release>2024-01-01T00:00:00Z</release><publication>2024 Apr</publication><modification>2026-04-12T19:23:57.772Z</modification><creation>2026-04-07T13:17:24.573Z</creation></dates><accession>S-EPMC11064672</accession><cross_references><pubmed>38381561</pubmed><doi>10.1091/mbc.E23-10-0387</doi></cross_references></HashMap>