A0A7X7NVJ1 · A0A7X7NVJ1_9MOLU

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.

1771100200300400500600700
TypeIDPosition(s)Description
Binding site354-361ATP (UniProtKB | ChEBI)
Active site677
Active site720

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
      GX546_02000

Organism names

  • Taxonomic identifier
  • Strain
    • AS06rmzACSIP_177
  • Taxonomic lineage
    Bacteria > Mycoplasmatota > Mollicutes > Acholeplasmatales > Acholeplasmataceae

Accessions

  • Primary accession
    A0A7X7NVJ1

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.

TypeIDPosition(s)Description
Domain8-202Lon N-terminal
Domain590-771Lon proteolytic

Sequence similarities

Belongs to the peptidase S16 family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    771
  • Mass (Da)
    87,136
  • Last updated
    2021-06-02 v1
  • Checksum
    88C376FAE8ED2206
MMPSKKILPALVTRGVVPLPNNDFRIEIGRPFSLKALDEAEEKFDKYLVLLIQKNPLIDVPTVEDVEDFGVLAKLAMKIKLPNDTYKVKFNIIKRIKVVEYTKTIDSFEIEYDELEEVFEGDIQEVITTVKMITTEIAKNPTQLLDSQLVLEKIEGETTPDKIADIIAYNLKINEMEKYKYIAETDVLKRLKFILMDINQQKMIVELEAKINEEVKKAIDENQKEYYLRERMKAIQNELGDRAKREEDMERLRKAIGEAGMPKNIEKHALSELSRLQSTSSFMAEANVIQNYLEFIVKLPWYKTSEDRNDLNEVKKILDANHYGLDKVKDRIIEYLSVKIKTQKNPQTILCLVGPPGVGKTSLGISIAEALGRRFVKHSLGGVKDESEIRGHRRTYVGAMPGRILKSMELAQTINPVFLLDEIDKLSSDYKGDPASAMLEVLDPEQNSKFSDHYLEVPYDLSQVLFITTANYLENIPAPLRDRMEIVQLSSYTELEKQQIARNHLLKEQLDAHGITEAEFSITDEAILEIIQYYTREAGVRELARHLGSLIRKAIKKILLEKVEKVEITKANLEEYLGKHKFIHNLADKKAQVGVVTGLAYTAYGGDTLPVEVTYYKGKGNLVLTGKLGDVMKESAQTALSYIKSKAEEYKIDPNLFLENDFHIHVPEGAIPKDGPSAGITIATALYSAVTNKLVRNDVGMTGEVTLRGLVLPIGGLKEKSIAADRSGIKTIVIPKENESDIDEIPEEVKEKLDIILVSEVNEVFKIAIKA

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JAAYXR010000065
EMBL· GenBank· DDBJ
NLG31324.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp