O84348 · LON_CHLTR

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.

1819100200300400500600700800
Type
IDPosition(s)Description
Binding site392-399ATP (UniProtKB | ChEBI)
Active site724
Active site767

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
    • Ordered locus names
      CT_344

Organism names

Accessions

  • Primary accession
    O84348

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00000761321-819Lon protease

Expression

Induction

By heat shock.

Interaction

Subunit

Homohexamer. Organized in a ring with a central cavity.

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for compositional bias, region, domain.

Type
IDPosition(s)Description
Compositional bias1-16Polar residues
Region1-40Disordered
Compositional bias18-38Basic and acidic residues
Domain42-239Lon N-terminal
Domain634-818Lon proteolytic

Sequence similarities

Belongs to the peptidase S16 family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    819
  • Mass (Da)
    91,965
  • Last updated
    1998-11-01 v1
  • Checksum
    FEA7802A5441557C
MNSTNNTDSQNLDPNASEVEKLLDESAEAEEKVDDHTPPSELFILPLNKRPFFPGMAAPLLIEAGPHYEVLTLLAKSSQKHIGLVLTKKEDANTLKVGFNQLHRVGVSARILRIMPIEGGSAQVLLSIEDRIRIVKPIQDKYLKAKVSYHKENKELTEELKAYSISIVSIIKDLLKLNPLFKEELQIFLGHSDFTEPGKLADFSVALTTATREELQEILETTDMHDRIDKALVLLKKELDLSRLQSSINQKIEATITKSQKEFFLKEQLKTIKKELGLEKDDHAVDLEKFMERFNKRDVPQYAMDVIQDEMDKLQTLETSSAEYAVCRNYLDWLTIVPWGIQTKEYHDLKKAESILNKDHYGLEDIKQRILELISVGKLANGMKGSIICLVGPPGVGKTSIGRSIAKVLHRKFFRFSVGGMRDEAEIKGHRRTYIGAMPGKLVQALKQSQIMNPVIMIDEVDKIGSSYHGDPASALLEVLDPEQNKDFLDHYLDVRVDLSNVLFILTANVLDSIPDPLLDRMEVLRLSGYILEEKLQIATKYLVPRARKEMGLSAQNVTFQPEALKHMINNYAREAGVRTLNENIKKVLRKVALKIVQNQEKNLSKKSRFTITPKNLQDYLGKPVFSSDRFYEKTPVGVATGLAWTSLGGATLYIESVQVPSSSGKADMHLTGQAGDVMKESSQIAWTYLHSALERYAPGQPFFEKSQVHIHIPEGATPKDGPSAGITMVTSLLSLLLDVPVLNNLGMTGELTLTGRVLGIGGIREKLIAARRSKLNILIFPEDNRRDYDELPAYLKKGLKVHFVTHYDDVFKIAFPGV

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias1-16Polar residues
Compositional bias18-38Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AE001273
EMBL· GenBank· DDBJ
AAC67939.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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