AC   MF_03120;
DC   Protein; auto
TR   HAMAP; MF_03120; -; 1; level=0
XX
Names: lonm_euk
XX
ID   LONM
case <OC:Mammalia>
DE   RecName: Full=Lon protease homolog, mitochondrial;
DE            EC=3.4.21.53;
DE   AltName: Full=Lon protease-like protein;
DE            Short=LONP;
DE   AltName: Full=Mitochondrial ATP-dependent protease Lon;
DE   AltName: Full=Serine protease 15;
DE   Flags: Precursor;
else case <OC:Saccharomyces>
DE   RecName: Full=Lon protease homolog, mitochondrial;
DE            EC=3.4.21.53;
DE   Flags: Precursor;
else
DE   RecName: Full=Lon protease homolog, mitochondrial;
DE            EC=3.4.21.53;
end case
case <OC:Vertebrata>
GN   Name=LONP1;
else case <OC:Fungi>
GN   Name=PIM1;
end case
XX
case <OC:Mammalia>
CC   -!- FUNCTION: ATP-dependent serine protease that mediates the selective
CC       degradation of misfolded, unassembled or oxidatively damaged
CC       polypeptides as well as certain short-lived regulatory proteins in the
CC       mitochondrial matrix. May also have a chaperone function in the
CC       assembly of inner membrane protein complexes. Participates in the
CC       regulation of mitochondrial gene expression and in the maintenance of
CC       the integrity of the mitochondrial genome. Binds to mitochondrial
CC       promoters and RNA in a single-stranded, site-specific, and strand-
CC       specific manner. May regulate mitochondrial DNA replication and/or gene
CC       expression using site-specific, single-stranded DNA binding to target
CC       the degradation of regulatory proteins binding to adjacent sites in
CC       mitochondrial promoters.
else
CC   -!- FUNCTION: ATP-dependent serine protease that mediates the selective
CC       degradation of misfolded, unassembled or oxidatively damaged
CC       polypeptides as well as certain short-lived regulatory proteins in the
CC       mitochondrial matrix. May also have a chaperone function in the
CC       assembly of inner membrane protein complexes. Participates in the
CC       regulation of mitochondrial gene expression and in the maintenance of
CC       the integrity of the mitochondrial genome. Binds to mitochondrial DNA
CC       in a site-specific manner.
end case
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of proteins in presence of ATP.; EC=3.4.21.53;
case <OC:Mammalia>
CC   -!- SUBUNIT: Homohexamer. Organized in a ring with a central cavity. The
CC       ATP-binding and proteolytic domains (AP-domain) form a hexameric
CC       chamber, while the N-terminal domain is arranged as a trimer of dimers.
CC       DNA and RNA binding is stimulated by substrate and inhibited by ATP
CC       binding. Interacts with @gn(TWNK) and mitochondrial DNA polymerase
CC       subunit @gn(POLG).
else case <OC:Saccharomyces>
CC   -!- SUBUNIT: Homoheptamer. Organized in a ring with a central cavity.
CC       Oligomerization is independent of its proteolytic activity and the
CC       autocatalytic maturation of its subunits.
else
CC   -!- SUBUNIT: Homohexamer or homoheptamer. Organized in a ring with a
CC       central cavity.
end case
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
case not <OC:Mammalia> and not <OC:Saccharomyces> and not <AnyFeature:TransitM>
CC   -!- MISCELLANEOUS: This protein may be expected to contain an N-terminal
CC       transit peptide but none has been predicted.
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   Pfam; PF03357; Snf7; 1; trigger=no
DR   PRINTS; PR00830; ENDOLAPTASE; 1; trigger=no
DR   NCBIfam; TIGR00763; lon; 1; trigger=no
case not <OC:Mammalia> and not <OC:Saccharomyces>
DR   General; TransitM; -; 0-1; trigger=yes
end case
XX
case <FTTag:ATP>
KW   ATP-binding
KW   Nucleotide-binding
end case
KW   DNA-binding
KW   Hydrolase
KW   Mitochondrion
KW   Protease
KW   Serine protease
case <OC:Mammalia> or <OC:Saccharomyces>
KW   Transit peptide
end case
XX
GO   GO:0005759; C:mitochondrial matrix
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:0034599; P:cellular response to oxidative stress
GO   GO:0070407; P:oxidation-dependent protein catabolic process
GO   GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins
GO   GO:0051131; P:chaperone-mediated protein complex assembly
XX
FT   From: LONM_BOVIN (Q59HJ6)
case <OC:Mammalia>
FT   TRANSIT         Nter..67
FT                   /note="Mitochondrion"
FT   CHAIN           68..Cter
FT                   /note="Lon protease homolog, mitochondrial"
end case
FT   From: LONM_YEAST (P36775)
case <OC:Saccharomyces>
FT   TRANSIT         Nter..37
FT                   /note="Mitochondrion"
FT   PROPEP          38..98
FT                   /note="Removed in mature form; by autocatalysis"
FT   CHAIN           99..Cter
FT                   /note="Lon protease homolog, mitochondrial"
end case
FT   From: LONM_HUMAN (P36776)
FT   BINDING         523..530
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Tag: ATP; Condition: G-P-[PT]-G-[TV]-G-K-T
FT   ACT_SITE        855
FT   Condition: S
FT   ACT_SITE        898
FT   Condition: K
XX
Size: 836-1177;
Related: MF_03121; MF_01973;
Template: P36776; Q59HJ6; P36775;
Scope:
 Eukaryota
Fusion:
 Nter: None
 Cter: None
Duplicate: in ARATH, DICDI
Plasmid: None
Comments: None
XX
# Revision 1.17 2023/06/01
//