B7FSL4 · LONM_PHATC

Function

function

ATP-dependent serine protease that mediates the selective degradation of misfolded, unassembled or oxidatively damaged polypeptides as well as certain short-lived regulatory proteins in the mitochondrial matrix. May also have a chaperone function in the assembly of inner membrane protein complexes. Participates in the regulation of mitochondrial gene expression and in the maintenance of the integrity of the mitochondrial genome. Binds to mitochondrial DNA in a site-specific manner.

Catalytic activity

  • Hydrolysis of proteins in presence of ATP.
    EC:3.4.21.53 (UniProtKB | ENZYME | Rhea)

Features

Showing features for binding site, active site.

1882100200300400500600700800
TypeIDPosition(s)Description
Binding site435-442ATP (UniProtKB | ChEBI)
Active site784
Active site827

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentmitochondrial matrix
Molecular FunctionATP binding
Molecular FunctionATP hydrolysis activity
Molecular FunctionATP-dependent peptidase activity
Molecular Functionsequence-specific DNA binding
Molecular Functionserine-type endopeptidase activity
Molecular Functionsingle-stranded DNA binding
Biological Processcellular response to oxidative stress
Biological Processchaperone-mediated protein complex assembly
Biological Processmitochondrion organization
Biological Processoxidation-dependent protein catabolic process
Biological Processprotein quality control for misfolded or incompletely synthesized proteins

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Lon protease homolog, mitochondrial
  • EC number

Gene names

    • ORF names
      PHATRDRAFT_18202

Organism names

Accessions

  • Primary accession
    B7FSL4

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for transit peptide, chain.

TypeIDPosition(s)Description
Transit peptide1-34Mitochondrion
ChainPRO_000039577035-882Lon protease homolog, mitochondrial

Proteomic databases

Interaction

Subunit

Homohexamer or homoheptamer. Organized in a ring with a central cavity.

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain68-281Lon N-terminal
Domain687-878Lon proteolytic

Sequence similarities

Belongs to the peptidase S16 family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    882
  • Mass (Da)
    97,656
  • Last updated
    2009-02-10 v1
  • Checksum
    021DFBDCF0C019F1
MIHVLKSRSTLLTASSIVRTSVGSSSRYSQTRTYSRTHSWSKDASGGAISVLPTKLPFGEQAPRFPHTLGLPLVSRPLFPGLVTSVTLTDEATIDAMEALTKNQDQAYVSCFLRKKNPTGVSEGGVILATPEVITDPSDIYHVGTFAQIQRLTRGDETAATLILLAHRRLDLEYVDKIGPPIDVTVKHWNRSDYTGADDTIRALSNEIISTIREVAQVNMLFRENLQYFPMRVDANDPFRLADFAASISASGTPEDLQAVLEEKDAEMRLHKALVLLNREREVSKLQQEISQKVEERMTEAQRKYFLTEQLKSIKKELGMERDDKDTLIEKYRKTLSEYPHVPEEAMETIDAELEKFSTLEKNSPEYNVTRSYLDWLTSVPWGVETEENFDIQKARKTLDRDHYGLDDVKDTILEFIAIGKLRGSVQGKILCLSGPPGTGKTSIAKSVADALGRQFFRFSVGGLSDVSEIKGHRRTYIGAMPGKLIQCLKATGTTNPVVLIDEIDKLGTGFRGDPASALLEVLDPGQNSTFRDYFLDVPVDISKVLFICTANELERIPGPLLDRMEVIRLSGYDLPEKVAIAEQYLVPKSMRDSGLLGVPETLKLTIDAVRSLARWYAREAGVRNLAKYIDRITRKLALQVVAESEGATLTDKSSRKSNTWEITEDNLHEYVGKPVFTSDRLYEDGPLPHGIVMGLAYTSMGGSALYIETQSIRRGLDSEGKTRGGGTLKVTGQLGDVMKESTQIASTVARARLSDIKPESNFFDINDIHMHVPEGATPKDGPSAGVTMVTSMLSLALDRPIRNDLAMTGEVSLTGKVLAVGGIKEKIMGARRAGIKCVILPAANKRDYDEIPDYLKEDLEVHYADTFDKVYEVAFSSVDST

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CM000606
EMBL· GenBank· DDBJ
EEC50499.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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