A0A3B6VAG9 · A0A3B6VAG9_BRAHW

Function

Catalytic activity

  • Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins.
    EC:3.4.21.89 (UniProtKB | ENZYME | Rhea)

Features

Showing features for active site.

134950100150200250300
TypeIDPosition(s)Description
Active site50
Active site179

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
Molecular Functionserine-type endopeptidase activity
Biological Processsignal peptide processing

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Signal peptidase I
  • EC number

Gene names

    • Name
      lepB
    • Ordered locus names
      BHWA1_02481

Organism names

Accessions

  • Primary accession
    A0A3B6VAG9

Proteomes

Subcellular Location

Membrane
; Single-pass type II membrane protein

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain21-205Peptidase S26
Domain256-328Peptidase S26

Sequence similarities

Belongs to the peptidase S26 family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    349
  • Mass (Da)
    40,648
  • Last updated
    2018-12-05 v1
  • Checksum
    A1AC0D6E65625EEA
MENPIKNITETIIGECRNFKHTLKEILYAIVIVLLINTFLIQNYQIPTGSMIPVIMPGDRLFANRFVYGVKLPFTDGLLGYRLPKIKSPQRGDLVVFRAPPSASWQCESAMPYYEPSPLVQMLKLPVMIFSLTPFTWDPRFLLADYIGEKLTGGTHMAPVPLFLGLKTVDLDPRKEFVKRVIATAGETVEIRNKKIIINGNEIEDKWGYFFYGNDREFVPRIDIYGPIYVPKKGDVIIFKKLVDRDDYYNDFSSFEVYINDKVVSDDIKLSYWMNIYVPNAKDRPDEYIYNVPEDYFFVMGDNRDQSCDSRMWGLVPYRHIKGQPMIAWIQSKRPDDVEQGFFKYFIIK

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP001357
EMBL· GenBank· DDBJ
ACN84935.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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