A0A9D2KMR3 · A0A9D2KMR3_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.

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.

1925100200300400500600700800900
TypeIDPosition(s)Description
Binding site469-476ATP (UniProtKB | ChEBI)
Active site792
Active site835

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
      H9962_06515

Organism names

Accessions

  • Primary accession
    A0A9D2KMR3

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 region, compositional bias, domain.

TypeIDPosition(s)Description
Region1-110Disordered
Compositional bias52-66Acidic residues
Compositional bias67-86Basic and acidic residues
Domain122-317Lon N-terminal
Region354-385Disordered
Domain705-886Lon proteolytic
Region890-925Disordered

Sequence similarities

Belongs to the peptidase S16 family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    925
  • Mass (Da)
    101,040
  • Last updated
    2023-05-03 v1
  • Checksum
    8C5B2FF9860C9E17
MTDAAFLPDGGLSEPSLAVSGPSYKDPAEGRLDASFDDAIPLPAADVPAPESPDGEVEENESGEGERSDDGSEANDTPEERDMPNRPRRRRIRRPSAVTVTPERPGGADNTQQILAEIPSTLPVVPLRDSVVFNSMIVPLYEGREKSILAVDTALGSNRFLLLCTQKDASVDDPGPGDLYEVGSVVMILRMLKMPDGQVKILVQGLARAQIKSFVATEPFLAARMELLQEKEAGPRDVRQEALIRSAREQSEKILNLRGIPTGDIMGVLMAVDDPGRLADLIAANMRLRVTDAQALLESLDPVERLQMVNDHLSREVEVADMQARIQNMAREGMDKAQKDYFLREQMKAIRRELGDNADQEEELEELTKSLDKAGLPSDARKEADKQLRRLSSMHGDSAEATVIRTYLDWLAELPWKKLSRDRLDIVKAKEILDADHFGLGRVKDRILEYLSVRKLNPDSKGPILCFVGPPGVGKTSLGRSIARAMGRKFQRISLGGMRDEAEIRGHRRTYIGAMPGRIIQAVKQAGTRNPVIVLDEIDKLGSDFRGDPSSALLEVLDPEQNSHFSDHYLNLEFDLSKVLFLCTANQLDTIPSALLDRMEVISLPGYTEQEKLAIAKKYLIPRQLEANGLKDGDITMRDGAIARIVREYTREAGLRNLERQLGTVCRKLARRKAEGEKGPFVVAAAQVPKLLGAPRFLDEERENALMPGVALGLAWTQAGGEVLHVEVTTMKGKGHLTLTGQLGDVMKESAQAAMSYARSHAGELGLDPDFTDKVDIHVHVPAGATPKDGPSAGVTLVTALVSALTCRPARNDTCMTGEITLRGRVLPVGGIKEKILGAVARGLEHAVIPSQNVKDLEDIPADLRRKIDIKSVDSIDQLLPLVLTPEVDDTCKRPAPAKKGRTSSVKEQPAKPGAKRPGRAAAAR

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias52-66Acidic residues
Compositional bias67-86Basic and acidic residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
DXAN01000022
EMBL· GenBank· DDBJ
HJA08823.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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