{"metadata":{"accession":"PF10090","entry_id":null,"type":"domain","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR018762","hierarchy":null,"name":{"name":"Histidine phosphotransferase C-terminal domain","short":"HPTransfase"},"description":[{"text":"<p>HPTransfase is a family of essential histidine phosphotransferases. It controls the activity of the master bacterial cell-cycle regulator CtrA through phosphorylation.  It behaves as a homodimer by adopting the domain architecture of the intracellular part of class I histidine kinases. Each subunit consists of two distinct domains: an N-terminal helical hairpin domain and a C-terminal [alpha]/[beta] domain. The two N-terminal domains are adjacent within the dimer, forming a four-helix bundle. The C-terminal domain adopts an atypical Bergerat ATP-binding fold [[cite:PUB00075663]].</p>","llm":false,"checked":false,"updated":false}],"wikipedia":[{"title":"Histidine_phosphotransfer_domain","extract":"<p><b>Histidine phosphotransfer domains</b> and <b>histidine phosphotransferases</b> are protein domains involved in the \"phosphorelay\" form of two-component regulatory systems. These proteins possess a phosphorylatable histidine residue and are responsible for transferring a phosphoryl group from an aspartate residue on an intermediate \"receiver\" domain, typically part of a hybrid histidine kinase, to an aspartate on a final response regulator.</p>","thumbnail":null}],"literature":{"PUB00075663":{"PMID":22949187,"ISBN":null,"volume":"68","issue":"Pt 9","year":2012,"title":"Structural insights into ChpT, an essential dimeric histidine phosphotransferase regulating the cell cycle in Caulobacter crescentus.","URL":null,"raw_pages":"1025-9","medline_journal":"Acta Crystallogr Sect F Struct Biol Cryst Commun","ISO_journal":"Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun.","authors":["Fioravanti A","Clantin B","Dewitte F","Lens Z","Verger A","Biondi EG","Villeret V."],"DOI_URL":"http://dx.doi.org/10.1107/S1744309112033064"}},"set_info":{"accession":"CL0025","name":"His_Kinase_A"},"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":1,"interactions":0,"matches":2320,"pathways":0,"proteins":2320,"proteomes":2317,"sets":1,"structural_models":{"alphafold":1567},"structures":4,"taxa":3145},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":45,"alignment:full":1368},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":{"accession":"4qpk","name":"1.7 Angstrom Structure of a Bacterial Phosphotransferase"}}}