W9VCB4 · W9VCB4_9GAMM

  • Protein
    Lon protease
  • Gene
    lon
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Evidence at transcript level
  • Annotation score
    3/5

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.

1819100200300400500600700800
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
      D779_3437

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • AK35
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Chromatiales > Chromatiaceae > Imhoffiella

Accessions

  • Primary accession
    W9VCB4

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.

TypeIDPosition(s)Description
Domain18-212Lon N-terminal
Domain600-781Lon proteolytic
Region786-819Disordered
Compositional bias799-819Basic and acidic residues

Sequence similarities

Belongs to the peptidase S16 family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    819
  • Mass (Da)
    91,384
  • Last updated
    2014-05-14 v1
  • Checksum
    D2C2C2594C79B553
MAQHDTASATDFPSSQEVPVLPLRDVVVYPHMVIPLFVGRDKSIRALDGAMASDKQILLIAQKSADVDDPAVKDLHEIGTLANILQLLKLPDGTVKVLVEGNQRAHIERFLTTEEAFSAVIQPLEETLEVDEREQEVLMRSAMSLFDQYVKLNKKVPPEVLSSLASIDDAGRLADTMAAHMSLKLDEKQHVLEMVDVQARLEHLMGLMESENDILQMEKRIRGRVKRQMEKNQREYYLNEQMKAIQKELGELEDAPNEIEDLANRIEAAGMPREAKNKAQGELNKLKLMSPMSAEATVVRNYIDTLVNVPWKKRTRIRNDIKVAEGVLDKDHYGLERVKERILEYLAVQQRVRKLKGPILCLVGPPGVGKTSLGQSIARATNRKFVRMSLGGVRDEAEIRGHRRTYIGALPGKIIQNLSKAGSRNAFFLLDEIDKMAMDFRGDPASALLEVLDPEQNHTFADHYLEVDFDLSEVMFVGTANTLNIPPPLLDRMEVIRLSGYTEDEKVAIAERYLVPKQVKNNGLKSGELVIREAALRDIIRHYTREAGVRNLEREISKICRKVVKEVLLKKRDAPTVVTSKALEKYLGVQRYRYGRADEHDQIGQVTGLAWTEVGGELLRIESALVPGKGKFTYTGQLGDVMQESIQAAMTVVRARADALGVPEDFHNKFDAHIHVPEGATPKDGPSAGVAMCTALVSALTRIPVRATVAMTGEITLRGEVLPIGGLKEKLLAAHRGGIETVIIPLENERDLTEIPKNIKQHLKIHPVRWIDEVLELALVERPEPKAANIDGGESMAEEEEARDAGVDASRDQNARLHH

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias799-819Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AONC01000061
EMBL· GenBank· DDBJ
EXJ13682.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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