AC   MF_01973;
DC   Protein; auto
TR   HAMAP; MF_01973; -; 1; level=0
XX
Names: lon_bact
XX
ID   LON
DE   RecName: Full=Lon protease;
DE            EC=3.4.21.53;
DE   AltName: Full=ATP-dependent protease La;
GN   Name=lon;
XX
case <OC:Escherichia> or <OC:Shigella>
CC   -!- FUNCTION: ATP-dependent serine protease that mediates the selective
CC       degradation of mutant and abnormal proteins as well as certain short-
CC       lived regulatory proteins. Required for cellular homeostasis and for
CC       survival from DNA damage and developmental changes induced by stress.
CC       Degrades polypeptides processively to yield small peptide fragments
CC       that are 5 to 10 amino acids long. Binds to DNA in a double-stranded,
CC       site-specific manner. Endogenous substrates include the regulatory
CC       proteins RcsA and SulA, the transcriptional activator SoxS, and UmuD.
CC       Its overproduction specifically inhibits translation through at least
CC       two different pathways, one of them being the YoeB-YefM toxin-antitoxin
CC       system.
else
CC   -!- FUNCTION: ATP-dependent serine protease that mediates the selective
CC       degradation of mutant and abnormal proteins as well as certain short-
CC       lived regulatory proteins. Required for cellular homeostasis and for
CC       survival from DNA damage and developmental changes induced by stress.
CC       Degrades polypeptides processively to yield small peptide fragments
CC       that are 5 to 10 amino acids long. Binds to DNA in a double-stranded,
CC       site-specific manner.
end case
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of proteins in presence of ATP.; EC=3.4.21.53;
case <OC:Escherichia> or <OC:Shigella>
CC   -!- ACTIVITY REGULATION: Contains an allosteric site (distinct from its
CC       active site), whose occupancy by an unfolded polypeptide leads to
CC       enzyme activation.
end case
case <OC:Escherichia> or <OC:Shigella>
CC   -!- SUBUNIT: Homohexamer. Organized in a ring with a central cavity. ATP
CC       binding and hydrolysis do not affect the oligomeric state of the
CC       enzyme.
else
CC   -!- SUBUNIT: Homohexamer. Organized in a ring with a central cavity.
end case
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
case <OC:Escherichia> or <OC:Shigella>
CC   -!- INDUCTION: By accumulation of abnormal proteins, such as at high
CC       temperatures. Under stress conditions.
else
CC   -!- INDUCTION: By heat shock.
end case
CC   -!- SIMILARITY: Belongs to the peptidase S16 family.
XX
DR   PROSITE; PS51787; LON_N; 1; trigger=yes
DR   PROSITE; PS51786; LON_PROTEOLYTIC; 1; trigger=yes
DR   PROSITE; PS01046; LON_SER; 1; trigger=no
DR   Pfam; PF00004; AAA; 1; trigger=no
DR   Pfam; PF02190; LON; 1; trigger=no
DR   PRINTS; PR00830; ENDOLAPTASE; 1; trigger=no
DR   NCBIfam; TIGR00763; lon; 1; trigger=no
XX
case <FTTag:ATP>
KW   ATP-binding
KW   Nucleotide-binding
end case
KW   Cytoplasm
KW   Hydrolase
KW   Protease
KW   Serine protease
KW   Stress response
XX
GO   GO:0005737; C:cytoplasm
GO   GO:0005524; F:ATP binding
GO   GO:0016887; F:ATP hydrolysis activity
GO   GO:0004176; F:ATP-dependent peptidase activity
GO   GO:0004252; F:serine-type endopeptidase activity
GO   GO:0043565; F:sequence-specific DNA binding
GO   GO:0034605; P:cellular response to heat
GO   GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins
XX
FT   From: LON_ECOLI (P0A9M0)
FT   BINDING         356..363
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Tag: ATP; Condition: G-[AP]-P-G-[ITV]-G-K-[ST]
FT   ACT_SITE        679
FT   Condition: S
FT   ACT_SITE        722
FT   Condition: K
XX
Size: 768-996;
Related: MF_03120; MF_03121;
Template: P0A9M0; P37945;
Scope:
 Bacteria
 Archaea
Fusion:
 Nter: None
 Cter: None
Duplicate: in BDEBA, DESPS, HERA2, SYNC1, SORC5, SYNFM, THET2, HYDCU
Plasmid: in PHEZH
Comments: None
XX
# Revision 1.19 2023/06/01
//