Bacteriocin: subtilin

Default view

Bacteriocin: subtilin

Accession: BAC045

Classification
Class: Lantibiotic
Genetics
Gene: spaS; Synonyms=sub
Producer and target organisms
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.
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).
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).
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).
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).
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).
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).
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).
Loading...
End Note
Reference Manager
BibTeX
Gene structure
genome of subtilin

Gene idNameDescriptionLocation
BACGene153spaBSpaB495..3587
BACGene154spaTSpaT3578..5422
BACGene155spaCSpaC5395..6720
BACGene156spaSSpaS lantibiotic subtilin6795..6965
BACGene157spaiSpaI immunity7548..8045
BACGene158spaFSpaF immunity8032..8775
BACGene159spaESpaE immunity8772..9527
BACGene160spaGSpaG immunity9688..10299
BACGene161spaRSpaR response regulator10317..10979
BACGene162spaKSpaK kinase10970..12349
BACGene163spaKOrf1 putative protein similar to hypothetical protein YvaPcomplement(12559..12885)
BACGene164spaKOrf2 putative protein similar to hypothetical protein YvaOcomplement(12976..13395)
BACGene165yvanYvan hypotheticalcomplement(13424..13831)
spaBspaTspaCspaSspaispaFspaEspaGspaRspaKspaKspaKyvan
Protein sequence
 ........10 ........20 ........30 ........40 
          |          |          |          | 
 WKSESLCTPG CVTGALQTCF LQTLTCNCKI SK

Wheel representation
wheel representation of subtilin
Protein sequence annotations
Features of subtilin

WSTS
FeaturePosition(s)LengthDescription
PEPTIDE1↔3232
Lantibiotic subtilin.
Feature identifier = PRO_0000017143.
Modified residue1N2-succinyltryptophan; partial.
Modified residue52,3-didehydroalanine (Ser).
Modified residue18(Z)-2,3-didehydrobutyrine.
Modified residue312,3-didehydroalanine (Ser).
Cross-link3↔75Lanthionine (Ser-Cys).
Cross-link8↔114Beta-methyllanthionine (Thr-Cys).
Cross-link13↔197Beta-methyllanthionine (Thr-Cys).
Cross-link23↔264Beta-methyllanthionine (Thr-Cys).
Cross-link25↔284Beta-methyllanthionine (Thr-Cys).
MUTAGEN5S->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

Users comments for subtilin

No comments found

Login or register to submit a comment for subtilin.