{"metadata":{"accession":"PF08353","entry_id":null,"type":"domain","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR013564","hierarchy":null,"name":{"name":"MurT ligase C-terminal","short":"MurT_C"},"description":[{"text":"<p>This entry represents the C-terminal domain of MurT ligase from Gram-positive bacteria. MurT is part of the bi-enzymatic complex MurT-GatD involved in the amidation of the alpha-carboxyl group of the D-isoglutamate residue in Lipid II in the peptidoglycan layer to produce D-isoglutamine. This domain contains an aspartate at position 349, the third residue in the catalytic triad GatD-C94, GatD-H189, MurT-D349. This C-terminal domain is built around a central six-stranded, predominantly parallel beta-sheet that is sandwiched between four alpha-helices on one side and two alpha-helices on the other. The MurT-GatD heterodimer adopts a boomerang-shaped conformation, with GatD packing against the C-terminal domain of MurT [[cite:PUB00094480]].</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00094480":{"PMID":30154570,"ISBN":null,"volume":"8","issue":"1","year":2018,"title":"Structural basis of cell wall peptidoglycan amidation by the GatD/MurT complex of Staphylococcus aureus.","URL":null,"raw_pages":"12953","medline_journal":"Sci Rep","ISO_journal":"Sci Rep","authors":["Noldeke ER","Muckenfuss LM","Niemann V","Muller A","Stork E","Zocher G","Schneider T","Stehle T."],"DOI_URL":null}},"set_info":{"accession":"CL0794","name":"Mur_ligase_C_sf"},"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":6,"interactions":0,"matches":4479,"pathways":0,"proteins":4479,"proteomes":4418,"sets":1,"structural_models":{"alphafold":2758},"structures":6,"taxa":6081},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":93,"alignment:full":2230},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":null}}