P10946 · SPAS_BACIU

  • Protein
    Lantibiotic subtilin
  • Gene
    spaS
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    4/5

Function

function

Lanthionine-containing peptide antibiotic (lantibiotic) active on Gram-positive bacteria. The bactericidal activity of lantibiotics is based on depolarization of energized bacterial cytoplasmic membranes, initiated by the formation of aqueous transmembrane pores.

Miscellaneous

Subtilin activity is observed during stationary phase, but not during exponential growth.

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 region
Molecular Functionsignaling receptor binding
Biological Processdefense response to bacterium
Biological Processkilling of cells of another organism

Keywords

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Lantibiotic subtilin

Gene names

    • Name
      spaS
    • Synonyms
      sub

Organism names

  • Taxonomic identifier
  • Strain
    • ATCC 6633 / PCI 219 / NRS 231
  • Taxonomic lineage
    Bacteria > Bacillota > Bacilli > Bacillales > Bacillaceae > Bacillus

Accessions

  • Primary accession
    P10946

Subcellular Location

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis29Devoid of antimicrobial activity; keeps full lysis capacity.

PTM/Processing

Features

Showing features for propeptide, modified residue, peptide, cross-link.

TypeIDPosition(s)Description
PropeptidePRO_00000171421-24
Modified residue25N2-succinyltryptophan; partial
PeptidePRO_000001714325-56Lantibiotic subtilin
Cross-link27↔31Lanthionine (Ser-Cys)
Modified residue292,3-didehydroalanine (Ser)
Cross-link32↔35Beta-methyllanthionine (Thr-Cys)
Cross-link37↔43Beta-methyllanthionine (Thr-Cys)
Modified residue42(Z)-2,3-didehydrobutyrine
Cross-link47↔50Beta-methyllanthionine (Thr-Cys)
Cross-link49↔52Beta-methyllanthionine (Thr-Cys)
Modified residue552,3-didehydroalanine (Ser)

Post-translational modification

Maturation of lantibiotics involves the enzymatic conversion of Thr, and Ser into dehydrated AA and the formation of thioether bonds with cysteine. This is followed by membrane translocation and cleavage of the modified precursor.
Succinylated subtilin is 10-20 times less active than subtilin. The ratio subtilin/succinylated subtilin is about 1:2 after 24 hours growth.
The 2,3-didehydrobutyrine is determined to be the Z-isomer.

Keywords

Structure

Family & Domains

Sequence similarities

Belongs to the type A lantibiotic family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    56
  • Mass (Da)
    6,218
  • Last updated
    1989-07-01 v1
  • Checksum
    DA9707FBF8A1EBBA
MSKFDDFDLDVVKVSKQDSKITPQWKSESLCTPGCVTGALQTCFLQTLTCNCKISK

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
J03767
EMBL· GenBank· DDBJ
AAA22841.1
EMBL· GenBank· DDBJ
Genomic DNA
M83944
EMBL· GenBank· DDBJ
AAA22772.1
EMBL· GenBank· DDBJ
Genomic DNA
M86869
EMBL· GenBank· DDBJ
AAA22840.1
EMBL· GenBank· DDBJ
Genomic DNA
M99263
EMBL· GenBank· DDBJ
AAA22778.1
EMBL· GenBank· DDBJ
Genomic DNA
U09819
EMBL· GenBank· DDBJ
AAB91589.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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