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HAMAP rule MF_01973

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General rule information [?]

Accession MF_01973
Dates 18-JUN-2010 (Created)
1-JUN-2023 (Last updated, Version 19)
Name lon_bact
Scope(s) Bacteria
Archaea
Template(s) P0A9M0 (LON_ECOLI); P37945 (LON1_BACSU); [ Recover all ]
Triggered by HAMAP; MF_01973 (Get profile general information and statistics)

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 Name=lon;

Comments [?]

case <OC:Escherichia> or <OC:Shigella>
FUNCTIONATP-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
FUNCTIONATP-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 REGULATIONContains 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>
SUBUNITHomohexamer. Organized in a ring with a central cavity. ATP binding and hydrolysis do not affect the oligomeric state of the enzyme.
else
SUBUNITHomohexamer. Organized in a ring with a central cavity.
end case
SUBCELLULAR LOCATIONCytoplasm.
case <OC:Escherichia> or <OC:Shigella>
INDUCTIONBy accumulation of abnormal proteins, such as at high temperatures. Under stress conditions.
else
INDUCTIONBy heat shock.
end case
SIMILARITYBelongs to the peptidase S16 family.

Keywords [?]


Gene Ontology [?]

GO:0005737; Cellular component:cytoplasm
GO:0005524; Molecular function:ATP binding
GO:0016887; Molecular function:ATP hydrolysis 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;
PROSITE PS51786; LON_PROTEOLYTIC; 1;
PROSITE PS01046; LON_SER; 1;
Pfam PF00004; AAA; 1;
Pfam PF02190; LON; 1;
PRINTS PR00830; ENDOLAPTASE; 1;
NCBIfam TIGR00763; lon; 1;

Features [?]

From: LON_ECOLI (P0A9M0)
Key From To Description Tag Condition FTGroup
BINDING 356 363 /ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"
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
MF_03121
Fusion Nter: None Cter: None



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