{"metadata":{"accession":"PS51753","entry_id":null,"type":"domain","go_terms":null,"source_database":"profile","member_databases":null,"integrated":"IPR032255","hierarchy":null,"name":{"name":"HBM domain profile","short":"HBM"},"description":[{"text":"<p>The helical bimodular (HBM) domain is a small molecule binding domain of\naround 250 amino acids. It is found in Bacteria and Archaea but is absent from\neukaryotes and forms part of chemoreceptors and histidine\nkinases. The HBM domain is composed of two structural\nmodules, each of which recognizes a different type of ligand. The conservation\nof amino acids in the ligand binding sites of both modules suggests that HBM\nfamily members recognize similar ligands [[cite:PUB00076243]].\n\nThe HBM domain is composed of six helices linked by loops.\nTwo short helices (alpha1 and alpha2) at the membrane-proximal part of the\nstructure are followed by the long helix alpha3. This segment is followed by\nanother couple of short helices (alpha4 and alpha5) and a second long helix\nalpha6, which is predicted to continue as a transmembrane helix. The structure\ncan be understood as a duplication of a structural element made of two short\nand a long helix. The six helices of the HBM domain arrange into two modules,\neach forming a four-helix bundle. The membrane proximal module is composed of\nalpha1, alpha2, the N-terminal segment of alpha 3, and the C-terminal segment\nof alpha6. The membrane distal module is composed of the C-terminal segment of\nalpha3, helices alpha4 and alpha5, and the the N-terminal part of alpha6 [[cite:PUB00076242]].\n\nThe profile we developed covers the entire HBM domain.</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00076243":{"PMID":24347303,"ISBN":null,"volume":"23","issue":"3","year":2014,"title":"The HBM domain: introducing bimodularity to bacterial sensing.","URL":null,"raw_pages":"332-6","medline_journal":"Protein Sci","ISO_journal":"Protein Sci.","authors":["Ortega A","Krell T."],"DOI_URL":"http://dx.doi.org/10.1002/pro.2410"},"PUB00076242":{"PMID":23112148,"ISBN":null,"volume":"109","issue":"46","year":2012,"title":"Evidence for chemoreceptors with bimodular ligand-binding regions harboring two signal-binding sites.","URL":null,"raw_pages":"18926-31","medline_journal":"Proc Natl Acad Sci U S A","ISO_journal":"Proc. Natl. Acad. Sci. U.S.A.","authors":["Pineda-Molina E","Reyes-Darias JA","Lacal J","Ramos JL","Garcia-Ruiz JM","Gavira JA","Krell T."],"DOI_URL":"http://dx.doi.org/10.1073/pnas.1201400109"}},"set_info":null,"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":0,"interactions":0,"matches":4949,"pathways":0,"proteins":4945,"proteomes":1158,"sets":0,"structural_models":{"alphafold":3793,"bfvd":0},"structures":2,"taxa":2049},"entry_annotations":{},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":{"accession":"2yfa","name":"X-ray structure of McpS ligand binding domain in complex with malate"}}}