P10946 · SPAS_BACIU
- ProteinLantibiotic subtilin
- GenespaS
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids
- Protein existenceEvidence at protein level
- Annotation score4/5
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 annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Molecular Function | signaling receptor binding | |
Biological Process | defense response to bacterium | |
Biological Process | killing of cells of another organism |
Keywords
- Molecular function
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameLantibiotic subtilin
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Bacillota > Bacilli > Bacillales > Bacillaceae > Bacillus
Accessions
- Primary accessionP10946
Subcellular Location
UniProt Annotation
GO Annotation
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 29 | Devoid of antimicrobial activity; keeps full lysis capacity. | ||||
Sequence: S → A |
PTM/Processing
Features
Showing features for propeptide, modified residue, peptide, cross-link.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Propeptide | PRO_0000017142 | 1-24 | ||||
Sequence: MSKFDDFDLDVVKVSKQDSKITPQ | ||||||
Modified residue | 25 | N2-succinyltryptophan; partial | ||||
Sequence: W | ||||||
Peptide | PRO_0000017143 | 25-56 | Lantibiotic subtilin | |||
Sequence: WKSESLCTPGCVTGALQTCFLQTLTCNCKISK | ||||||
Cross-link | 27↔31 | Lanthionine (Ser-Cys) | ||||
Sequence: SESLC | ||||||
Modified residue | 29 | 2,3-didehydroalanine (Ser) | ||||
Sequence: S | ||||||
Cross-link | 32↔35 | Beta-methyllanthionine (Thr-Cys) | ||||
Sequence: TPGC | ||||||
Cross-link | 37↔43 | Beta-methyllanthionine (Thr-Cys) | ||||
Sequence: TGALQTC | ||||||
Modified residue | 42 | (Z)-2,3-didehydrobutyrine | ||||
Sequence: T | ||||||
Cross-link | 47↔50 | Beta-methyllanthionine (Thr-Cys) | ||||
Sequence: TLTC | ||||||
Cross-link | 49↔52 | Beta-methyllanthionine (Thr-Cys) | ||||
Sequence: TCNC | ||||||
Modified residue | 55 | 2,3-didehydroalanine (Ser) | ||||
Sequence: S |
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
- PTM
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length56
- Mass (Da)6,218
- Last updated1989-07-01 v1
- ChecksumDA9707FBF8A1EBBA
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |