{"metadata":{"accession":"PF06295","entry_id":null,"type":"family","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR009386","hierarchy":null,"name":{"name":"Z-ring associated protein G-like","short":"ZapG-like"},"description":[{"text":"<p>This family includes Z-ring associated protein G from Escherichia coli (ZapG) and similar proteins predominantly found in gammaproteobacteria. ZapG is involved in cell division, cell envelope biogenesis and cell shape maintenance. It is a key regulator of cell envelope growth, playing a crucial role in coordinating cell width, elongation and division to maintain cell envelope integrity. It plays an important role in the lipopolysaccharide (LPS) assembly/transport [[cite:PUB00151520],[cite:PUB00104752],[cite:PUB00151522],[cite:PUB00151523]]. This protein adopts an alpha helical configuration.</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00151522":{"PMID":34941903,"ISBN":null,"volume":"17","issue":"12","year":2021,"title":"Loss of YhcB results in dysregulation of coordinated peptidoglycan, LPS and phospholipid synthesis during Escherichia coli cell growth.","URL":null,"raw_pages":"e1009586","medline_journal":"PLoS Genet","ISO_journal":"PLoS Genet","authors":["Goodall ECA","Isom GL","Rooke JL","Pullela K","Icke C","Yang Z","Boelter G","Jones A","Warner I","Da Costa R","Zhang B","Rae J","Tan WB","Winkle M","Delhaye A","Heinz E","Collet JF","Cunningham AF","Blaskovich MA","Parton RG","Cole JA","Banzhaf M","Chng SS","Vollmer W","Bryant JA","Henderson IR."],"DOI_URL":"https://doi.org/10.1371/journal.pgen.1009586"},"PUB00104752":{"PMID":33895137,"ISBN":null,"volume":"296","issue":null,"year":2021,"title":"ZapG (YhcB/DUF1043), a novel cell division protein in gamma-proteobacteria linking the Z-ring to septal peptidoglycan synthesis.","URL":null,"raw_pages":"100700","medline_journal":"J Biol Chem","ISO_journal":"J Biol Chem","authors":["Mehla J","Liechti G","Morgenstein RM","Caufield JH","Hosseinnia A","Gagarinova A","Phanse S","Goodacre N","Brockett M","Sakhawalkar N","Babu M","Xiao R","Montelione GT","Vorobiev S","den Blaauwen T","Hunt JF","Uetz P."],"DOI_URL":null},"PUB00151520":{"PMID":27335665,"ISBN":null,"volume":"2012","issue":null,"year":2012,"title":"Inner Membrane Protein YhcB Interacts with RodZ Involved in Cell Shape Maintenance in Escherichia coli.","URL":null,"raw_pages":"304021","medline_journal":"ISRN Mol Biol","ISO_journal":"ISRN Mol Biol","authors":["Li G","Hamamoto K","Kitakawa M."],"DOI_URL":"https://doi.org/10.5402/2012/304021"},"PUB00151523":{"PMID":36077106,"ISBN":null,"volume":"23","issue":"17","year":2022,"title":"A New Factor LapD Is Required for the Regulation of LpxC Amounts and Lipopolysaccharide Trafficking.","URL":null,"raw_pages":"9706","medline_journal":"Int J Mol Sci","ISO_journal":"Int J Mol Sci","authors":["Wieczorek A","Sendobra A","Maniyeri A","Sugalska M","Klein G","Raina S."],"DOI_URL":"https://doi.org/10.3390/ijms23179706"}},"set_info":null,"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":1,"interactions":0,"matches":2165,"pathways":0,"proteins":2165,"proteomes":2155,"sets":0,"structural_models":{"alphafold":1391},"structures":1,"taxa":2906},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":19,"alignment:full":726},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":null}}