{"metadata":{"accession":"PF07338","entry_id":null,"type":"domain","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR010854","hierarchy":null,"name":{"name":"YdgH/BhsA/McbA-like domain","short":"YdgH_BhsA-like"},"description":[{"text":"<p>This domain is found in several Enterobacterial proteins of around 90 residues in length, including E. coli YdgH, YhcN, BhsA and McbA, which play a role in stress response, biofilm formation and pathogenesis [[cite:PUB00097758],[cite:PUB00097759]]. BhsA (also known as ComC) reduces the permeability of the outer  membrane to copper and may decrease biofilm formation by repressing cell-cell interaction and cell surface interaction [[cite:PUB00097760]]. Members of this entry have one copy of this domain with the exception of YdgH, which has three copies. The function of this domain is unknown, however, it is suggested to be directly involved in host-pathogen interaction [[cite:PUB00097759]].</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00097759":{"PMID":25010333,"ISBN":null,"volume":"9","issue":"7","year":2014,"title":"Structural and functional characterization of DUF1471 domains of Salmonella proteins SrfN, YdgH/SssB, and YahO.","URL":null,"raw_pages":"e101787","medline_journal":"PLoS One","ISO_journal":"PLoS One","authors":["Eletsky A","Michalska K","Houliston S","Zhang Q","Daily MD","Xu X","Cui H","Yee A","Lemak A","Wu B","Garcia M","Burnet MC","Meyer KM","Aryal UK","Sanchez O","Ansong C","Xiao R","Acton TB","Adkins JN","Montelione GT","Joachimiak A","Arrowsmith CH","Savchenko A","Szyperski T","Cort JR."],"DOI_URL":null},"PUB00097758":{"PMID":31534833,"ISBN":null,"volume":"7","issue":null,"year":2019,"title":"Proteomics and bioinformatics analysis reveal potential roles of cadmium-binding proteins in cadmium tolerance and accumulation of <i>Enterobacter cloacae</i>.","URL":null,"raw_pages":"e6904","medline_journal":"PeerJ","ISO_journal":"PeerJ","authors":["Chuanboon K","Na Nakorn P","Pannengpetch S","Laengsri V","Nuchnoi P","Isarankura-Na-Ayudhya C","Isarankura-Na-Ayudhya P."],"DOI_URL":null},"PUB00097760":{"PMID":22089859,"ISBN":null,"volume":"25","issue":"1","year":2012,"title":"The copper-inducible ComR (YcfQ) repressor regulates expression of ComC (YcfR), which affects copper permeability of the outer membrane of Escherichia coli.","URL":null,"raw_pages":"33-43","medline_journal":"Biometals","ISO_journal":"Biometals","authors":["Mermod M","Magnani D","Solioz M","Stoyanov JV."],"DOI_URL":null}},"set_info":null,"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":3,"interactions":0,"matches":5637,"pathways":0,"proteins":4596,"proteomes":538,"sets":0,"structural_models":{"alphafold":2805},"structures":6,"taxa":823},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":61,"alignment:full":1343},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":{"accession":"4evu","name":"Crystal structure of C-terminal domain of putative periplasmic protein ydgH from S. enterica"}}}