Home  |  Contact
Annotation rule MF_01973
Send feedback

General rule information [?]

Accession MF_01973
Dates 18-JUN-2010 (Created)
19-NOV-2019 (Last updated, Version 12)
Name lon_bact
Scope
Bacteria
Archaea
Templates P0A9M0 (LON_ECOLI); P37945 (LON1_BACSU): [Recover all]

Propagated annotation [?]


Identifier, protein and gene names [?]

Identifier
LON
Protein name
RecName: Full=Lon protease;
EC 3.4.21.53;
AltName: Full=ATP-dependent protease La;
Gene name
lon

Comments [?]

case <OC:Escherichia> or <OC:Shigella>
Function ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner. Endogenous substrates include the regulatory proteins RcsA and SulA, the transcriptional activator SoxS, and UmuD. Its overproduction specifically inhibits translation through at least two different pathways, one of them being the YoeB-YefM toxin-antitoxin system.
else
Function ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner.
end case
Catalytic activity Reaction=Hydrolysis of proteins in presence of ATP.; EC=3.4.21.53;
case <OC:Escherichia> or <OC:Shigella>
Activity regulation Contains an allosteric site (distinct from its active site), whose occupancy by an unfolded polypeptide leads to enzyme activation.
end case
case <OC:Escherichia> or <OC:Shigella>
Subunit Homohexamer. Organized in a ring with a central cavity. ATP binding and hydrolysis do not affect the oligomeric state of the enzyme.
else
Subunit Homohexamer. Organized in a ring with a central cavity.
end case
Subcellular location Cytoplasm.
case <OC:Escherichia> or <OC:Shigella>
Induction By accumulation of abnormal proteins, such as at high temperatures. Under stress conditions.
else
Induction By heat shock.
end case
Similarity Belongs to the peptidase S16 family.

Keywords [?]

case <FTTag:ATP>
end case

Gene Ontology [?]

GO:0005737; Cellular component: cytoplasm.
GO:0005524; Molecular function: ATP binding.
GO:0016887; Molecular function: ATPase activity.
GO:0004176; Molecular function: ATP-dependent peptidase activity.
GO:0004252; Molecular function: serine-type endopeptidase activity.
GO:0043565; Molecular function: sequence-specific DNA binding.
GO:0034605; Biological process: cellular response to heat.
GO:0006515; Biological process: protein quality control for misfolded or incompletely synthesized proteins.

Cross-references [?]

PROSITE PS51787; LON_N; 1; trigger=PRU01123;
PS51786; LON_PROTEOLYTIC; 1; trigger=PRU01122;
PS01046; LON_SER; 1;
Pfam PF00004; AAA; 1;
PF02190; LON; 1;
PRINTS PR00830; ENDOLAPTASE; 1;
TIGRFAMs TIGR00763; lon; 1;

Features [?]

case <OC:Escherichia> or <OC:Shigella>
From: LON_ECOLI (P0A9M0)
Key     From     To       Description   Tag   Condition   FTGroup
INIT_MET     Nter     Nter       Removed        
end case
NP_BIND     356     363       ATP   ATP   G-[AP]-P-G-[ITV]-G-K-[ST]  
ACT_SITE     679     679             S  
ACT_SITE     722     722             K  

Additional information [?]

Size range 768-996 amino acids
Related rules MF_03120 (LONM); MF_03121 (LONP2)
Fusion None