{"metadata":{"accession":"PF14092","entry_id":null,"type":"family","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR025366","hierarchy":null,"name":{"name":"BamH","short":"BamH"},"description":[{"text":"<p>This entry, previously known as DUF4270, represents BamH subunit of the beta-barrel-assembly machinery so-called BAM. BamH along with BamG are involved in forming the extracellular canopy and are both required for BAM function. They are conserved across the Bacteroidota, suggesting that they form an essential extension to the canonical BAM core in this phylum. BamH interacts with BamM to form a long canopy structure on the extracellular side of the outer membrane that extends from the rear of BamA across the BamA barrel [[cite:PUB00163537]]. BamH consists of two homologous beta-sandwich domains with a Nucleoplasmin-like jelly roll topology. One of the domains is inserted into the other resulting in a circular permutation. The N-terminal strand of one of the domains occupies the position of the C-terminal strand of the other.</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00163537":{"PMID":41034578,"ISBN":null,"volume":"647","issue":"8089","year":2025,"title":"A new paradigm for outer membrane protein biogenesis in the Bacteroidota.","URL":null,"raw_pages":"479-487","medline_journal":"Nature","ISO_journal":"Nature","authors":["Liu X","Orenday Tapia L","Deme JC","Lea SM","Berks BC."],"DOI_URL":"https://doi.org/10.1038/s41586-025-09532-8"}},"set_info":{"accession":"CL0055","name":"Nucleoplasmin"},"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":1,"interactions":0,"matches":2444,"pathways":0,"proteins":2444,"proteomes":2014,"sets":1,"structural_models":{"alphafold":1580},"structures":4,"taxa":2671},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":28,"alignment:full":1149},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":null}}