A0A0S1U291 · A0A0S1U291_SERLI

Function

Catalytic activity

  • Preferential cleavage of bonds with hydrophobic residues in P1'.
    EC:3.4.24.40 (UniProtKB | ENZYME | Rhea)

Cofactor

Protein has several cofactor binding sites:
Ca2+ (UniProtKB | Rhea| CHEBI:29108 )

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 1 zinc ion per subunit.

Features

Showing features for binding site, active site.

148650100150200250300350400450
TypeIDPosition(s)Description
Binding site192Zn2+ (UniProtKB | ChEBI); catalytic
Active site193
Binding site196Zn2+ (UniProtKB | ChEBI); catalytic
Binding site202Zn2+ (UniProtKB | ChEBI); catalytic

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
Cellular Componentextracellular matrix
Cellular Componentextracellular space
Molecular Functioncalcium ion binding
Molecular Functionmetalloendopeptidase activity
Molecular Functionzinc ion binding
Biological Processproteolysis

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    serralysin
  • EC number

Gene names

    • Name
      ser2

Organism names

  • Taxonomic identifier
  • Organism
  • Strains
    • DSM 30066
    • LMG26065
    • LMG26066
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Yersiniaceae > Serratia

Accessions

  • Primary accession
    A0A0S1U291
  • Secondary accessions
    • A0A379Z805

Subcellular Location

PTM/Processing

Keywords

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain48-247Peptidase metallopeptidase

Sequence similarities

Belongs to the peptidase M10B family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    486
  • Mass (Da)
    51,842
  • Last updated
    2016-02-17 v1
  • Checksum
    068AE3CD51F98D90
MDNSLNGKTNGWDNVNDLLNYHNRGNGLTINNKPSFDVAAAGKQIARSEQTWNGTHVLGQGATVTYSFPDWDYNQSNLNGRFASQDTGLSAFTADQKAQAKLSLQSWADVANLNFVEVAPGQKSNITFGNYEGDGQAYAIKPFTGAGTDYRGHNTDGQSWFNINYDYADPRDGVYANLHPELGNYGRLSITHELGHTLGLDHPGVYNAGQSPSYAKATYAEDTRQFSVMSYWDESVTGGDHGGYYSAAPLVDDIAAIQYLYGANTTTRTGDTVYGFNSNSGRDFYTATDSSQKLIFSVWDAGGNDTLDFSGYSQDQRINLTEGSFSDVGGLKGNISIAVGAVIENAIGGSGNDVIVGNDAANILQGGAGNDVIYGGGGQDQLSGGSGSDIFVFSAVSDSPFKSPDKILDFETGIDKIDLSFFNQGDNGTDFIHFVDSFSGQAGEATLTYNSQSDFSELALNINGHATPDFLVNIVGQANTATDFIV

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
KR935795
EMBL· GenBank· DDBJ
ALM31047.1
EMBL· GenBank· DDBJ
Genomic DNA
KR935798
EMBL· GenBank· DDBJ
ALM31050.1
EMBL· GenBank· DDBJ
Genomic DNA
KR935799
EMBL· GenBank· DDBJ
ALM31051.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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