W9T9W7 · W9T9W7_9PSED

  • Protein
    Multifunctional fusion protein
  • Gene
    lon
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Evidence at transcript level
  • Annotation score
    4/5

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.
ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP.

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.

112681002003004005006007008009001,0001,1001,200
TypeIDPosition(s)Description
Binding site16Zn2+ (UniProtKB | ChEBI)
Binding site19Zn2+ (UniProtKB | ChEBI)
Binding site38Zn2+ (UniProtKB | ChEBI)
Binding site41Zn2+ (UniProtKB | ChEBI)
Binding site121-128ATP (UniProtKB | ChEBI)
Binding site822-829ATP (UniProtKB | ChEBI)
Active site1144
Active site1187

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular FunctionATP binding
Molecular FunctionATP hydrolysis activity
Molecular FunctionATP-dependent peptidase activity
Molecular FunctionATP-dependent protein folding chaperone
Molecular Functionprotein dimerization activity
Molecular Functionsequence-specific DNA binding
Molecular Functionserine-type endopeptidase activity
Molecular Functionunfolded protein binding
Molecular Functionzinc ion binding
Biological Processcellular response to heat
Biological Processprotein quality control for misfolded or incompletely synthesized proteins

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Multifunctional fusion protein

Including 2 domains:

  • Recommended name
    Lon protease
  • EC number
  • Alternative names
    • ATP-dependent protease La
  • Recommended name
    ATP-dependent Clp protease ATP-binding subunit ClpX

Gene names

    • Name
      lon
    • Synonyms
      clpX
    • ORF names
      BAY1663_00266

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • BAY1663
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Pseudomonadales > Pseudomonadaceae > Pseudomonas

Accessions

  • Primary accession
    W9T9W7

Proteomes

Subcellular Location

Keywords

Expression

Induction

By heat shock.

Interaction

Subunit

Component of the ClpX-ClpP complex. Forms a hexameric ring that, in the presence of ATP, binds to fourteen ClpP subunits assembled into a disk-like structure with a central cavity, resembling the structure of eukaryotic proteasomes.
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
Domain4-57ClpX-type ZB
Domain477-670Lon N-terminal
Domain1057-1238Lon proteolytic
Region1246-1268Disordered
Compositional bias1248-1268Basic and acidic residues

Sequence similarities

Belongs to the ClpX chaperone family.
Belongs to the peptidase S16 family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,268
  • Mass (Da)
    140,527
  • Last updated
    2014-05-14 v1
  • Checksum
    4CB8354A6B187992
MTDTRNGEDSGKLLYCSFCGKSQHEVRKLIAGPSVFICDECVDLCNDIIREEVQEAQAESSAHKLPAPKEISGILDQYVIGQERAKKILAVAVYNHYKRLNQRDKKEEVELGKSNILLIGPTGSGKTLLAETLARLLNVPFTIADATTLTEAGYVGEDVENIIQKLLQKCDYDVEKAQMGIVYIDEIDKISRKSDNPSITRDVSGEGVQQALLKLIEGTVASVPPQGGRKHPQQEFLQVDTRNILFICGGAFAGLEKVIQGRSTQGGIGFNAEVRSKDPGKKIGEALRSVEPDDLVKFGLIPEFVGRLPVIATLDELDEAALIQILTEPKNALTKQYAKLFELEGVDLEFRPDALKAVAQRALERKTGARGLRSILEGVLLDTMYDIPSQKDVSKVVIDESVIEGTSQPLLIYENSEPPAKLRLRRDRTKGPAGPFVFVPSPCFLQGMPSSLQQGYSVRLPPYGRRRAEFMKTTIELPLLPLRDVVVYPHMVIPLFVGREKSIEALESAMAGDKQILLLAQKNPADDDPVEDALYRVGTVATVLQLLKLPDGTVKVLVEGEQRGVIERFLEVDDHCRAEVALIEESEVEARESEVFTRSLLSQFEQYVQLGKKVPAEVLSSLSSIDEPARLVDTMAAHMALKIEQKQEILEITELPARVEHVLALLDAEIDLLQVEKRIRGRVKKQMERSQREYYLNEQMKAIQKELGDIDEGHNEIDDLKKRIENAGLSKDAYAKAQAELNKLKQMSPMSAEATVVRTYIDWLVNVPWKAASKVRLDLGKAEEVLDADHYGLEEVKDRILEYLAVQKRVKKLKGPVLCLVGPPGVGKTSLAESIARSTNRKFVRMALGGVRDEAEIRGHRRTYIGSMPGRLIQKMTKVGVRNPLFLLDEIDKMGSDMRGDPASALLEVLDPEQNHNFNDHYLEVDYDLSDVMFLCTANSMNIPAPLLDRMEVIRLPGYTEDEKVNIATRYLAPKQIQANGLKKGEVEFEEAAIRDIIRYYTREAGVRSLERQLAKVCRKVVKEHAAQKRFQVTVGADSLEHFLGVRKFRYGLAELQDQVGQVTGLAWTQVGGELLTIEAAVVPGKGRLTKTGSLGEVMGESITAALTVVRSRATSLGIAVDFHEKQDIHIHVPEGATPKDGPSAGIGMCTALVSALTQIPVRADVAMTGEITLRGQVLAIGGLKEKLLAAHRGGIKTVIIPEENQRDLKEIPENIKQDLQIKPVKWIDEVLQIALQYAPEPLPDAAPEIVAKDDKREPDSKERISTH

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias1248-1268Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AZSV01000002
EMBL· GenBank· DDBJ
EXF47248.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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