Annotations: 4YPM

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	Lon	e4ypmA3	A: alpha arrays	X: Histone-like	H: Histone-related	T: AAA+ ATPase lid domain	F: Lon	ECOD (1.6)
A	Lon_C_N	e4ypmA1	A: a+b two layers	X: Ribosomal protein S5 domain 2-like (From Topology)	H: Ribosomal protein S5 domain 2-like (From Topology)	T: Ribosomal protein S5 domain 2-like	F: Lon_C_N	ECOD (1.6)
A	Lon_C_C	e4ypmA2	A: a/b three-layered sandwiches	X: C-terminal subdomain in Lon-related proteases catalytic domains (From Topology)	H: C-terminal subdomain in Lon-related proteases catalytic domains (From Topology)	T: C-terminal subdomain in Lon-related proteases catalytic domains	F: Lon_C_C	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF05362	Lon protease (S16) C-terminal proteolytic domain (Lon_C)	Lon protease (S16) C-terminal proteolytic domain	The Lon serine proteases must hydrolyse ATP to degrade protein substrates. In Escherichia coli, these proteases are involved in turnover of intracellular proteins, including abnormal proteins following heat-shock. The active site for protease activit ...	The Lon serine proteases must hydrolyse ATP to degrade protein substrates. In Escherichia coli, these proteases are involved in turnover of intracellular proteins, including abnormal proteins following heat-shock. The active site for protease activity resides in a C-terminal domain. The Lon proteases are classified as family S16 in Merops.	Domain
A	PF22667	Lon protease AAA+ ATPase lid domain (Lon_lid)	Lon protease AAA+ ATPase lid domain	This entry represents the AAA+ ATPase lid domain of Lon proteases [1-5].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	Lon protease	binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding small molecule binding pyrophosphatase activity ATP hydrolysis activity ribonucleoside triphosphate phosphatase activity hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides hydrolase activity hydrolase activity, acting on acid anhydrides catalytic activity ATP-dependent activity peptidase activity catalytic activity, acting on a protein serine hydrolase activity serine-type peptidase activity serine-type endopeptidase activity endopeptidase activity ATP-dependent peptidase activity sequence-specific DNA binding DNA binding nucleic acid binding cation binding metal ion binding identical protein binding protein binding	cellular response to stimulus cellular response to heat response to stimulus cellular response to stress response to stress response to heat response to abiotic stimulus cellular process response to temperature stimulus catabolic process proteolysis involved in protein catabolic process primary metabolic process protein catabolic process macromolecule catabolic process cellular response to stimulus cellular response to heat response to stimulus cellular response to stress response to stress response to heat response to abiotic stimulus cellular process response to temperature stimulus catabolic process proteolysis involved in protein catabolic process primary metabolic process protein catabolic process macromolecule catabolic process proteolysis metabolic process protein metabolic process macromolecule metabolic process protein quality control for misfolded or incompletely synthesized proteins	cellular anatomical structure intracellular anatomical structure cytoplasm

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR027543	Lon protease, bacterial	Family
A	IPR015947	PUA-like superfamily	Homologous Superfamily
A	IPR046336	Lon protease, N-terminal domain superfamily	Homologous Superfamily
A	IPR003111	Lon protease, N-terminal domain	Domain
A	IPR004815	Lon protease, bacterial/eukaryotic-type	Family
A	IPR054594	Lon protease, AAA+ ATPase lid domain	Domain
A	IPR003593	AAA+ ATPase domain	Domain
A	IPR008269	Peptidase S16, Lon proteolytic domain	Domain
A	IPR027065	Lon protease	Family
A	IPR008268	Peptidase S16, active site	Active Site
A	IPR003959	ATPase, AAA-type, core	Domain
A	IPR020568	Ribosomal protein uS5 domain 2-type superfamily	Homologous Superfamily
A	IPR027417	P-loop containing nucleoside triphosphate hydrolase	Homologous Superfamily
A	IPR014721	Small ribosomal subunit protein uS5 domain 2-type fold, subgroup	Homologous Superfamily

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM157729.