A0A0K1PF18 · A0A0K1PF18_9BACT

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.

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.

1912100200300400500600700800900
Type
IDPosition(s)Description
Binding site477-484ATP (UniProtKB | ChEBI)
Active site801
Active site844

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
      AKJ08_2403

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • DSM 27710
  • Taxonomic lineage
    Bacteria > Myxococcota > Myxococcia > Myxococcales > Cystobacterineae > Vulgatibacteraceae > Vulgatibacter

Accessions

  • Primary accession
    A0A0K1PF18

Proteomes

Subcellular Location

Keywords

Expression

Induction

By heat shock.

Interaction

Subunit

Homohexamer. Organized in a ring with a central cavity.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain, region, compositional bias.

Type
IDPosition(s)Description
Domain1-195Lon N-terminal
Region335-380Disordered
Compositional bias406-454Basic and acidic residues
Region406-461Disordered
Domain713-895Lon proteolytic

Sequence similarities

Belongs to the peptidase S16 family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    912
  • Mass (Da)
    99,225
  • Last updated
    2015-11-11 v1
  • MD5 Checksum
    4360332A148A902ABEE670FEDE2D0638
MPVLPIRGAVVFPLAVVPISVGQERSIQLAEEVMHTDRLIAIVAQQNEDASPAEPDDLYRVGTSAVVRQFHRTDAGTIQLVVQGLGRIRIDDYVSTEPYMVAKVSDAPEEGGAGKTELEALTRTAQDLFSQLAQHTPELPDELALAMRAFDDPLQVTYLLATTVPLPTPVRQDLLELDSVAVRLQHLVELIQKDLAVRELEQKIVDETKVRISDTQREYVLRERIRAIQEELGESGGEGQQLRKKIEEAGLNEEAKREADRELSRLEGIPEVSPEHGMIRTWLEWIAAMPWKKTTGGPIDLDEARMILDRDHYDLDKIKERLVDYLAVKKLRDERRVGAEPSTAREKGGEPSGKPTGKPAEKPAGKPVGKPNGTTGTVIATGAPTEGAEAAVERAAKAAMEAAKESAKGSAKEEAKAAAKEAEEKAEKKAAKEAGEEAPSDEKPGKKPAKGPEKKEGFVPTALQRPLRREPILCFVGPPGTGKTSLGQSIARALGRKFVHASLGGIHDEAEIRGHRRTYIGALPGRIVQSLRRVGVSDPVFMLDEVDKLSASFQGDPSAALLEVLDPDQNSEFVDTYLGVPVNLSRVLFICTANTTEPIPPALLDRMEVLRLAGYTEEEKVQIAVRHLLPLELRSNGLDAEEVELDDDVLRKVIREYTREAGVRNLERELATILRKSARRIGEGKPTPIAVLPDELHDFLGPRRFFDELAERVDRPGVATGLSWTPAGGQTLFVEATMMPGRKEKLILTGKLGSVLKESAQAALSWLRSNATRLGIEPDIFLRRIVHVHVPSGAIAKDGPSAGVAILAALVSLVSGVALRPDVAMTGEITLRGKVLPVGGIRDKVLAAHRAGIPVVILPRRSEGALEELPKEVRDDMHIVLVDTVDEVLAEALPAVKAEEEAEGEEAAPDLM

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias406-454Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP012332
EMBL· GenBank· DDBJ
AKU92016.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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