Bacteriocin: subtilin
Accession: BAC045
Classification
Class: Lantibiotic
Genetics
Gene: spaS; Synonyms=sub
Producer and target organisms
Producer Organism: Bacillus subtilis [Gram-positive]
Taxonomy: Bacteria
FirmicutesBacillalesBacillaceaeBacillus
Target organismsactive on Gram-positive bacteria
Description
Mode of action:
Lanthionine-containing peptide antibiotic (lantibiotic). The bactericidal activity of lantibiotics is based on depolarization of energized bacterial cytoplasmic membranes, initiated by the formation of aqueous transmembrane pores.
Post-translational modification:
Maturation of lantibiotics involves the enzymic 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. phase, but not during exponential growth.
Lanthionine-containing peptide antibiotic (lantibiotic). The bactericidal activity of lantibiotics is based on depolarization of energized bacterial cytoplasmic membranes, initiated by the formation of aqueous transmembrane pores.
Post-translational modification:
Maturation of lantibiotics involves the enzymic 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. phase, but not during exponential growth.
Uniprot and PDB links
UniProt Entry: P10946
PDB EntryUnknown
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
MEDLINE=88243844;PubMed=2837490;
Banerjee S., Hansen J.N.
"Structure and expression of a gene encoding the precursor of subtilin, a small protein antibiotic.", J. Biol. Chem. 263:9508-9514(1988).
MEDLINE=88243844;PubMed=2837490;
Banerjee S., Hansen J.N.
"Structure and expression of a gene encoding the precursor of subtilin, a small protein antibiotic.", J. Biol. Chem. 263:9508-9514(1988).
NUCLEOTIDE SEQUENCE [GENOMIC DNA], STRAIN=ATCC 6633 / PCI 219
MEDLINE=92138640;PubMed=1735728;
Chung Y.J., Steen M.T., Hansen J.N.
"The subtilin gene of Bacillus subtilis ATCC 6633 is encoded in an operon that contains a homolog of the hemolysin B transport protein.", J. Bacteriol. 174:1417-1422(1992).
MEDLINE=92138640;PubMed=1735728;
Chung Y.J., Steen M.T., Hansen J.N.
"The subtilin gene of Bacillus subtilis ATCC 6633 is encoded in an operon that contains a homolog of the hemolysin B transport protein.", J. Bacteriol. 174:1417-1422(1992).
NUCLEOTIDE SEQUENCE [GENOMIC DNA], STRAIN=ATCC 6633 / PCI 219
MEDLINE=92171481;PubMed=1539969;
Klein C., Kaletta C., Schnell N., Entian K.-D.
"Analysis of genes involved in biosynthesis of the lantibiotic subtilin.", Appl. Environ. Microbiol. 58:132-142(1992).
MEDLINE=92171481;PubMed=1539969;
Klein C., Kaletta C., Schnell N., Entian K.-D.
"Analysis of genes involved in biosynthesis of the lantibiotic subtilin.", Appl. Environ. Microbiol. 58:132-142(1992).
PROTEIN SEQUENCE OF 25-56.
MEDLINE=75040028;PubMed=4154277;
Gross E., Kiltz H.H., Nebelin E.
"Subtilin, VI: the structure of subtilin.", Hoppe-Seyler's Z. Physiol. Chem. 354:810-812(1973).
MEDLINE=75040028;PubMed=4154277;
Gross E., Kiltz H.H., Nebelin E.
"Subtilin, VI: the structure of subtilin.", Hoppe-Seyler's Z. Physiol. Chem. 354:810-812(1973).
MODE OF ACTION.
MEDLINE=89276381;PubMed=2471644;
Schueller F., Benz R., Sahl H.-G.
"The peptide antibiotic subtilin acts by formation of voltage- dependent multi-state pores in bacterial and artificial membranes.", Eur. J. Biochem. 182:181-186(1989).
MEDLINE=89276381;PubMed=2471644;
Schueller F., Benz R., Sahl H.-G.
"The peptide antibiotic subtilin acts by formation of voltage- dependent multi-state pores in bacterial and artificial membranes.", Eur. J. Biochem. 182:181-186(1989).
STRUCTURE BY NMR, STRAIN=ATCC 6633 / PCI 219
MEDLINE=92192284;PubMed=1547888;DOI=10.1016/0014-5793(92)80163-B
Chan W.C., Bycroft B.W., Leylands M.L., Lian L.-Y., Yang J.C., Roberts G.C.K.
"Sequence-specific resonance assignment and conformational analysis of subtilin by 2D NMR.", FEBS Lett. 300:56-62(1992).
MEDLINE=92192284;PubMed=1547888;DOI=10.1016/0014-5793(92)80163-B
Chan W.C., Bycroft B.W., Leylands M.L., Lian L.-Y., Yang J.C., Roberts G.C.K.
"Sequence-specific resonance assignment and conformational analysis of subtilin by 2D NMR.", FEBS Lett. 300:56-62(1992).
MUTAGENESIS OF SER-29.
MEDLINE=93167833;PubMed=8434932;
Liu W., Hansen J.N.
"The antimicrobial effect of a structural variant of subtilin against outgrowing Bacillus cereus T spores and vegetative cells occurs by different mechanisms.", Appl. Environ. Microbiol. 59:648-651(1993).
MEDLINE=93167833;PubMed=8434932;
Liu W., Hansen J.N.
"The antimicrobial effect of a structural variant of subtilin against outgrowing Bacillus cereus T spores and vegetative cells occurs by different mechanisms.", Appl. Environ. Microbiol. 59:648-651(1993).
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Gene structure
| Gene id | Name | Description | Location |
| BACGene153 | spaB | SpaB | 495..3587 |
| BACGene154 | spaT | SpaT | 3578..5422 |
| BACGene155 | spaC | SpaC | 5395..6720 |
| BACGene156 | spaS | SpaS lantibiotic subtilin | 6795..6965 |
| BACGene157 | spai | SpaI immunity | 7548..8045 |
| BACGene158 | spaF | SpaF immunity | 8032..8775 |
| BACGene159 | spaE | SpaE immunity | 8772..9527 |
| BACGene160 | spaG | SpaG immunity | 9688..10299 |
| BACGene161 | spaR | SpaR response regulator | 10317..10979 |
| BACGene162 | spaK | SpaK kinase | 10970..12349 |
| BACGene163 | spaK | Orf1 putative protein similar to hypothetical protein YvaP | complement(12559..12885) |
| BACGene164 | spaK | Orf2 putative protein similar to hypothetical protein YvaO | complement(12976..13395) |
| BACGene165 | yvan | Yvan hypothetical | complement(13424..13831) |
Protein sequence
| ........10 ........20 ........30 ........40 | | | | WKSESLCTPG CVTGALQTCF LQTLTCNCKI SK |
Wheel representation
Protein sequence annotations
| Feature | Position(s) | Length | Description |
| PEPTIDE | 1↔32 | 32 | Lantibiotic subtilin. Feature identifier = PRO_0000017143. |
| Modified residue | 1 | N2-succinyltryptophan; partial. | |
| Modified residue | 5 | 2,3-didehydroalanine (Ser). | |
| Modified residue | 18 | (Z)-2,3-didehydrobutyrine. | |
| Modified residue | 31 | 2,3-didehydroalanine (Ser). | |
| Cross-link | 3↔7 | 5 | Lanthionine (Ser-Cys). |
| Cross-link | 8↔11 | 4 | Beta-methyllanthionine (Thr-Cys). |
| Cross-link | 13↔19 | 7 | Beta-methyllanthionine (Thr-Cys). |
| Cross-link | 23↔26 | 4 | Beta-methyllanthionine (Thr-Cys). |
| Cross-link | 25↔28 | 4 | Beta-methyllanthionine (Thr-Cys). |
| MUTAGEN | 5 | S->A: Devoid of antimicrobial activity; |
Composition
Hydrophobicity
Composition
| Formula | C148
H243
N39
O46
S5 |
| Absent amino acids | DHMRY |
| Common amino acids | CT |
| Mass (Da) | 3483.63 |
| Net charge | +2 |
| Isoelectric point | 8.21 |
| Basic residues | 3 |
| Acidic residues | 1 |
| Hydrophobic residues | 9 |
| Polar residues | 16 |
| Aliphatic residues | 6 |
| Tiny residues | 6 |
| Boman Index | -20.19 |
| Hydropathy Index | 0.19 |
| Aliphatic Index | 73.13 |
| Instability Index | 38.42 (stable) |
| Half Life |
Mammalian : 2.8 hour Yeast : 3 min E. coli : 2 min |
| Extinction Coefficient | 5750 M-1 cm-1 |
| Absorbance 280nm | 185.48 |
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