A0A1L7NI82 · A0A1L7NI82_PSEPU

Function

function

Functions as both a chaperone and a metalloprotease. Maintains the integrity of the outer membrane by promoting either the assembly or the elimination of outer membrane proteins, depending on their folding state.

Cofactor

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 1 zinc ion per subunit.

Features

Showing features for binding site, active site.

147850100150200250300350400450
TypeIDPosition(s)Description
Binding site127Zn2+ (UniProtKB | ChEBI); catalytic
Active site128
Binding site131Zn2+ (UniProtKB | ChEBI); catalytic
Binding site193Zn2+ (UniProtKB | ChEBI); catalytic
Active site197Proton donor

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 Componentmembrane
Cellular Componentperiplasmic space
Molecular Functionmetalloendopeptidase activity
Molecular Functionzinc ion binding
Biological Processchaperone-mediated protein folding
Biological Processproteolysis involved in protein catabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Putative beta-barrel assembly-enhancing protease
  • EC number

Gene names

    • ORF names
      I5S84_28440
      , KF715C_ch45610

Organism names

Accessions

  • Primary accession
    A0A1L7NI82

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for signal, chain.

TypeIDPosition(s)Description
Signal1-21
ChainPRO_503455996122-478Putative beta-barrel assembly-enhancing protease

Family & Domains

Features

Showing features for domain, coiled coil.

TypeIDPosition(s)Description
Domain62-251Peptidase M48
Coiled coil335-362

Sequence similarities

Belongs to the peptidase M48 family. BepA subfamily.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    478
  • Mass (Da)
    53,202
  • Last updated
    2017-03-15 v1
  • Checksum
    97AF4C0ABEB598FE
MNLLRPTLLTLACLMALPGHADDLPSLGDASSAIVSPQQEHQLGRAWLSLLRGQVNQLNDPQLKDYVETTVYRLAETSQLQDRRLEFILIDSRELNAFAAPGGIVGVNGGLFLNARTEGEYASVLAHELAHLSQRHFARGVEAQQRMQLPMMAALLAGIVLAAGGAGDAGIGMIAGTQAAAIQEQRRFSRQNEQEADRIGIQNLEKAGYDPRNMPTMFERLAQQYRYGAKPPEFLLTHPVTESRIADTRNRAEQAPKGGVEDSMRYQLIRARVALTYEGTPGLAAKRFRAQLDEDPKMDAARYGLALAQIKGGQLNEARELLKPLLAKAPNDITYNLAQIDLDITNNRLADAQQRAERMQGLYPGNYPLKQVRADLLVKQNKPAEAEKVLNELIKSRPDDPDVWYDMAEVRGLSGNTIGLHRARAEYFTLVGDFDQAIQQLDYAKRRAGGNFPLASQIDQRQREILEQQRMVREMMGR

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AP015029
EMBL· GenBank· DDBJ
BAW25134.1
EMBL· GenBank· DDBJ
Genomic DNA
JADUCP010000065
EMBL· GenBank· DDBJ
MBH3452742.1
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