<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Estevan-Morio E</submitter><funding>Spanish Ministry of Science and Innovation (MICINN)</funding><funding>Consejo Superior de Investigaciones Científicas</funding><funding>Government of Catalonia</funding><funding>Ministerio de Ciencia, Innovación y Universidades</funding><funding>JAE-Intro fellowship</funding><funding>Consolidated Research Group (SGR) project of the Generalitat de Catalunya</funding><pagination>1604</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC11674741</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>14(12)</volume><pubmed_abstract>Cytophaga is a genus of Gram-negative bacteria occurring in soil and the gut microbiome. It is closely related to pathogenic &lt;i>Flavobacterium&lt;/i> spp. that cause severe diseases in fish. Cytophaga strain L43-1 secretes cytophagalysin (CPL1), a 137 kDa peptidase with reported collagenolytic and gelatinolytic activity. We performed highly-confident structure prediction calculations for CPL1, which identified 11 segments and domains, including a signal peptide for secretion, a prosegment (PS) for latency, a metallopeptidase (MP)-like catalytic domain (CD), and eight immunoglobulin (Ig)-like domains (D3-D10). In addition, two short linkers were found at the D8-D9 and D9-D10 junctions, and the structure would be crosslinked by four disulfide bonds. The CPL1 CD was found closest to ulilysin fro</pubmed_abstract><journal>Biomolecules</journal><pubmed_title>Dissecting Cytophagalysin: Structural and Biochemical Studies of a Bacterial Pappalysin-Family Metallopeptidase.</pubmed_title><pmcid>PMC11674741</pmcid><funding_grant_id>RYC2020-029773-I</funding_grant_id><funding_grant_id>PRE2020-096731</funding_grant_id><funding_grant_id>2021SGR00423</funding_grant_id><funding_grant_id>JAEINT_22_02654</funding_grant_id><funding_grant_id>PID2021-128682OA-I00</funding_grant_id><pubmed_authors>Bushi E</pubmed_authors><pubmed_authors>Estevan-Morio E</pubmed_authors><pubmed_authors>Ramirez-Larrota JS</pubmed_authors><pubmed_authors>Eckhard U</pubmed_authors></additional><is_claimable>false</is_claimable><name>Dissecting Cytophagalysin: Structural and Biochemical Studies of a Bacterial Pappalysin-Family Metallopeptidase.</name><description>Cytophaga is a genus of Gram-negative bacteria occurring in soil and the gut microbiome. It is closely related to pathogenic &lt;i>Flavobacterium&lt;/i> spp. that cause severe diseases in fish. Cytophaga strain L43-1 secretes cytophagalysin (CPL1), a 137 kDa peptidase with reported collagenolytic and gelatinolytic activity. We performed highly-confident structure prediction calculations for CPL1, which identified 11 segments and domains, including a signal peptide for secretion, a prosegment (PS) for latency, a metallopeptidase (MP)-like catalytic domain (CD), and eight immunoglobulin (Ig)-like domains (D3-D10). In addition, two short linkers were found at the D8-D9 and D9-D10 junctions, and the structure would be crosslinked by four disulfide bonds. The CPL1 CD was found closest to ulilysin fro</description><dates><release>2024-01-01T00:00:00Z</release><publication>2024 Dec</publication><modification>2026-05-26T20:10:17.763Z</modification><creation>2026-05-25T03:07:09.427Z</creation></dates><accession>S-EPMC11674741</accession><cross_references><pubmed>39766312</pubmed><doi>10.3390/biom14121604</doi></cross_references></HashMap>