"accession"	"counters"	"cross_references"	"description"	"entry_id"	"go_terms"	"hierarchy"	"integrated"	"is_llm"	"is_reviewed_llm"	"is_updated_llm"	"literature"	"member_databases"	"name"	"overlaps_with"	"representative_structure"	"set_info"	"source_database"	"type"	"wikipedia"
"IPR032899"	"{'subfamilies': 0, 'domain_architectures': 0, 'interactions': 0, 'matches': 1444, 'pathways': 0, 'proteins': 1444, 'proteomes': 416, 'sets': 0, 'structural_models': {'alphafold': 1253, 'bfvd': 0}, 'structures': 0, 'taxa': 991}"	"{}"	"[{'text': '<p>This entry represents the cell division protein DamX from Enterobacteriaceae. DamX is an inner membrane protein that contributes to the cell constriction process during bacterial cytokinesis. It contains a C-terminal SPOR domain that may act as autonomous septal targeting determinant [[cite:PUB00077003], [cite:PUB00077005]]. DamX localises to the septal ring, but it is non-essential for cell division, and it inhibits cell division when overproduced [[cite:PUB00077032]]. It has been suggested that it may contribute to cell envelope biogenesis or integrity in other ways distinct from its role in cell division [[cite:PUB00065333]].</p>', 'llm': False, 'checked': False, 'updated': False}]"	""	"[{'identifier': 'GO:0032506', 'name': 'cytokinetic process', 'category': {'code': 'P', 'name': 'biological_process'}}, {'identifier': 'GO:0030428', 'name': 'cell septum', 'category': {'code': 'C', 'name': 'cellular_component'}}]"	"{'accession': 'IPR032899', 'name': 'Cell division protein DamX', 'type': 'Family', 'children': []}"	""	False	False	False	"{'PUB00077003': {'PMID': 19684127, 'ISBN': None, 'volume': '191', 'issue': '24', 'year': 2009, 'title': 'Self-enhanced accumulation of FtsN at Division Sites and Roles for Other Proteins with a SPOR domain (DamX, DedD, and RlpA) in Escherichia coli cell constriction.', 'URL': None, 'raw_pages': '7383-401', 'medline_journal': 'J Bacteriol', 'ISO_journal': 'J. Bacteriol.', 'authors': ['Gerding MA', 'Liu B', 'Bendezu FO', 'Hale CA', 'Bernhardt TG', 'de Boer PA.'], 'DOI_URL': 'http://dx.doi.org/10.1128/JB.00811-09'}, 'PUB00065333': {'PMID': 23290046, 'ISBN': None, 'volume': '52', 'issue': '4', 'year': 2013, 'title': 'Nuclear magnetic resonance solution structure of the peptidoglycan-binding SPOR domain from Escherichia coli DamX: insights into septal localization.', 'URL': None, 'raw_pages': '627-39', 'medline_journal': 'Biochemistry', 'ISO_journal': 'Biochemistry', 'authors': ['Williams KB', 'Yahashiri A', 'Arends SJ', 'Popham DL', 'Fowler CA', 'Weiss DS.'], 'DOI_URL': 'http://dx.doi.org/10.1021/bi301609e'}, 'PUB00077032': {'PMID': 7603433, 'ISBN': None, 'volume': '247', 'issue': '5', 'year': 1995, 'title': 'Characterization of three genes in the dam-containing operon of Escherichia coli.', 'URL': None, 'raw_pages': '546-54', 'medline_journal': 'Mol Gen Genet', 'ISO_journal': 'Mol. Gen. Genet.', 'authors': ['Lyngstadaas A', 'Lobner-Olesen A', 'Boye E.'], 'DOI_URL': 'http://dx.doi.org/10.1007/BF00290345'}, 'PUB00077005': {'PMID': 19880599, 'ISBN': None, 'volume': '192', 'issue': '1', 'year': 2010, 'title': 'Discovery and characterization of three new Escherichia coli septal ring proteins that contain a SPOR domain: DamX, DedD, and RlpA.', 'URL': None, 'raw_pages': '242-55', 'medline_journal': 'J Bacteriol', 'ISO_journal': 'J. Bacteriol.', 'authors': ['Arends SJ', 'Williams K', 'Scott RJ', 'Rolong S', 'Popham DL', 'Weiss DS.'], 'DOI_URL': 'http://dx.doi.org/10.1128/JB.01244-09'}}"	"{'hamap': {'MF_02021': 'Cell division protein DamX [damX]'}}"	"{'name': 'Cell division protein DamX', 'short': 'DamX'}"	""	""	""	"interpro"	"family"	""