View bacteriocin : subtilin Bookmark and Share

Accession BAC045
Name subtilin
Gene spaS; Synonyms=sub
Class Lantibiotic
Producer Organism Bacillus subtilis [Gram-positive]
Taxonomy BacteriaFirmicutesBacillalesBacillaceaeBacillus
Target organisms active on Gram-positive bacteria
Swiss-Prot Entry P10946
PDB Entry Unknown
Other databases EMBL J03767EMBL M86869EMBL M83944EMBL M99263EMBL U09819

PIR A28112InterPro IPR006079InterPro IPR000446Pfam PF02052PRINTS PR00324
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.
[Ref. 1] | View abstract | Export citation
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).

[Ref. 2] | View abstract | Export citation
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).

[Ref. 3] | View abstract | Export citation
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).

[Ref. 4] | View abstract | Export citation
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).

[Ref. 5] | View abstract | Export citation
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).

[Ref. 6] | View abstract | Export citation
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).

[Ref. 7] | View abstract | Export citation
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).

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Sequence
........10........20........30........40
| | | |
WKSESLCTPGCVTGALQTCFLQTLTCNCKISK
Wheel representation
Composition
AA N° %

AA N° %

AA N° %
Ala 1 3.13%

Ile 1 3.13%

Arg 0 .00%
Cys 5 15.63%

Lys 3 9.38%

Ser 3 9.38%
Asp 0 .00%

Leu 4 12.50%

Thr 5 15.63%
Glu 1 3.13%

Met 0 .00%

Val 1 3.13%
Phe 1 3.13%

Asn 1 3.13%

Trp 1 3.13%
Gly 2 6.25%

Pro 1 3.13%

Tyr 0 .00%
His 0 .00%

Gln 2 6.25%
Total 32
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
Red solid plot : values according to the hydrophobicity scale of Kyte and Doolittle (reference paper).


Yellow dashed plot : Experimentally determined hydrophobicity scale for proteins at membrane interfaces(reference paper).


Green dotted-dashed plot : prediction of transmembrane helices (reference paper). In this scale (unlike the others), more negative values reflect greater hydrophobicity.

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