Q9A4S2 · Q9A4S2_CAUVC

Function

function

Might be efficient in the degradation of transiently denatured and unfolded proteins which accumulate in the periplasm following stress conditions.

Catalytic activity

  • Acts on substrates that are at least partially unfolded. The cleavage site P1 residue is normally between a pair of hydrophobic residues, such as Val-|-Val.
    EC:3.4.21.107 (UniProtKB | ENZYME | Rhea)

Features

Showing features for active site.

153050100150200250300350400450500
TypeIDPosition(s)Description
Active site146Charge relay system
Active site176Charge relay system
Active site256Charge relay system

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Molecular Functionserine-type endopeptidase activity
Biological Processproteolysis

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Probable periplasmic serine endoprotease DegP-like
  • EC number
  • Alternative names
    • Protease Do

Gene names

    • Ordered locus names
      CC_2758

Organism names

Accessions

  • Primary accession
    Q9A4S2

Proteomes

PTM/Processing

Features

Showing features for signal, chain.

TypeIDPosition(s)Description
Signal1-21
ChainPRO_503891473322-530Probable periplasmic serine endoprotease DegP-like

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region, compositional bias, domain.

TypeIDPosition(s)Description
Region95-129Disordered
Compositional bias105-129Polar residues
Domain300-391PDZ
Region396-430Disordered
Domain408-518PDZ

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    530
  • Mass (Da)
    54,455
  • Last updated
    2001-06-01 v1
  • Checksum
    55E1775CA2636102
MTARKSGFIVGAVAGASVACAALAGMGMRMGTADAAQAPVVRVSTASAPTFAPPPGAPMSFADIFEKVSPAVVQINVTSKAQAPSLRIPGLEGFDIVPRGQRRPGQPGQQGQQQEDDGDTPATPKQQSAGSGFFISADGYIVTNNHVVADADDIQVVLKDGRELKATLVGRDESTDLAVIKVVDPKAKGKDFTFVNFENQAKPRVGDWVITIGNPFGLGGTATAGIISAYDRNLNDTTSSFVPYIQIDAPINRGNSGGPSFDIYGRVIGVNSAIYSPSGGSVGIGFAIPAEVAEGVAKQLIENGKVVRGYIGVSIMAFNAEMAEALGMSDVKGAIVASVVPGGPAAKAGLLPDDILVAVNGVKISDSSELTREVSKARPGETIKVSIIRDGKPRIVDVKSGTRPSESSLAVTDDEQGQDGAAPTPDKPASQKVDALGLTLGPIDAASRQTYKIEPDIKGLLIIGVKGDSDAGEKGLAKGDVLSNINGAPVTSVADVTSAVETAKKAGRASVLVKIVRQNRPVFIPLKIAP

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias105-129Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AE005673
EMBL· GenBank· DDBJ
AAK24722.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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