A0A8T7D5F4 · A0A8T7D5F4_9GAMM

Function

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.

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

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.

1810100200300400500600700800
TypeIDPosition(s)Description
Binding site364-371ATP (UniProtKB | ChEBI)
Active site687
Active site730

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular FunctionATP binding
Molecular FunctionATP hydrolysis activity
Molecular FunctionATP-dependent peptidase activity
Molecular Functionsequence-specific DNA binding
Molecular Functionserine-type endopeptidase activity
Biological Processcellular response to heat
Biological Processprotein quality control for misfolded or incompletely synthesized proteins

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Lon protease
  • EC number
  • Alternative names
    • ATP-dependent protease La

Gene names

    • Name
      lon
    • ORF names
      HKP13_10980
      , KJO08_00720

Organism names

Accessions

  • Primary accession
    A0A8T7D5F4

Proteomes

Subcellular Location

Keywords

Expression

Induction

By heat shock.

Interaction

Subunit

Homohexamer. Organized in a ring with a central cavity.

Family & Domains

Features

Showing features for domain, coiled coil, region, compositional bias.

TypeIDPosition(s)Description
Domain19-212Lon N-terminal
Coiled coil191-218
Domain600-781Lon proteolytic
Region786-810Disordered
Compositional bias787-810Basic and acidic residues

Sequence similarities

Belongs to the peptidase S16 family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    810
  • Mass (Da)
    91,016
  • Last updated
    2022-10-12 v1
  • Checksum
    FD8149CA62DF7620
MSNNDRQSSPESNPTIVSLPVLPLRDVVVYPYMVVPLFVGRAKSIVALERAMVEERKILLTAQRDASQNEPTTEDIYHTGTVSTILQLLKLPDGTVKVLVEGLYRASIERFIETDNYLFAEITKYEEQPVETKNVEALIRSTMTQFEKYVKLNRKISPEIIASLTDINDSGRLADVVAAHLFIKIDQKQELLETKDVKSRLEQLAHHLEREIDLLQVERKIHGRVKKQMEKNQREYYLNEQMKAIQKELGDMEDGTNEIERLAKKIEEAGMSKEAKEKATAEIKKLKMMSPMSSEATVVRNYVDWLLDVPWKKRTRIRHDLPKAEGVLEEDHYGLEKVKERITEYLAVQQRVKKLKGPILCLVGPPGVGKTSLGKSIARATGREFIRMSLGGVRDEAEIRGHRRTYIGALPGRIIQKLAKGGVRNPLFLLDEVDKMSMDFRGDPSSALLEVLDPEQNHTFNDHYLEVDYDLSEIMFVATANSMNIPGPLLDRMEVIRIPGYTEIEKLNIAKRYLIPKQTKDNGLKDGEINITQNAIQDIIRYYTREAGVRNVEREIAKISRKVVKQKIISGSDKQTLITPKSLEKYLGVQRFHYGRAEEEDRIGHVTGLAWTEVGGDLLTIEAAIMPGKGNLSHTGSLGDVMQESIQAAMTVVRSRSKQLGLEPEFYQKHDVHIHVPEGATPKDGPSAGVGMCTALVSTLTKIPVLSNVAMTGEITLRGEVLPIGGLKEKLLAALRGGITKVLIPRENQRDLSEIPANIKQGLDIQTVKWIDEVLELALQYTPTPTELKADREKPASVGKEGAHDALRTH

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias787-810Basic and acidic residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JAHHNN010000032
EMBL· GenBank· DDBJ
MBT8419363.1
EMBL· GenBank· DDBJ
Genomic DNA
JABDQX010000448
EMBL· GenBank· DDBJ
NNJ85435.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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