Bacteriocin: Subtilosin-A
Accession: BAC054
Classification
Class: Unclassified
Genetics
Gene: sboA; Synonyms=sbo; OrderedLocusNames=BSU37350
Producer and target organisms
Producer Organism: Bacillus subtilis [Gram-positive]
Taxonomy: Bacteria
FirmicutesBacillalesBacillaceaeBacillus
Target organismssome Gram-positive bacteria such as Listeria -
some species of Bacillus - Enterococcus faecium
Description
Mode of action:
end of vegetative growth and finishes before spore formation. and is under dual and independent control of spo0A-abrB and resDE.
Post-translational modification:
This peptide undergoes unique processing steps that include proteolytic cleavage after Glu-8, and covalent linkage of the alpha-amino of Asn-9 with the carboxyl of Gly-43 to form a cyclopeptide. Thioether cross-links are formed between cysteines and the alpha-carbons of other amino acids, Cys-12 to Phe-39, Cys- 15 to Thr-36, and Cys-21 to Phe-30. In forming these cross-links, Thr-36 and Phe-39 are converted to D-amino-acids. and 39 probably due to their modification, and reports a cyclic permutation of the peptide sequence.
end of vegetative growth and finishes before spore formation. and is under dual and independent control of spo0A-abrB and resDE.
Post-translational modification:
This peptide undergoes unique processing steps that include proteolytic cleavage after Glu-8, and covalent linkage of the alpha-amino of Asn-9 with the carboxyl of Gly-43 to form a cyclopeptide. Thioether cross-links are formed between cysteines and the alpha-carbons of other amino acids, Cys-12 to Phe-39, Cys- 15 to Thr-36, and Cys-21 to Phe-30. In forming these cross-links, Thr-36 and Phe-39 are converted to D-amino-acids. and 39 probably due to their modification, and reports a cyclic permutation of the peptide sequence.
Uniprot and PDB links
UniProt Entry: O07623
PDB Entry1PXQ resolved by NMR
[Ref. 1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], STRAIN=ATCC 6633 / PCI 219
Stein T., Duesterhus S., Entian K.-D.
"Subtilosin A biosynthesis is conserved among two different classes of Bacillus subtilis strains.", Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
Stein T., Duesterhus S., Entian K.-D.
"Subtilosin A biosynthesis is conserved among two different classes of Bacillus subtilis strains.", Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
NUCLEOTIDE SEQUENCE [GENOMIC DNA], STRAIN=168
MEDLINE=98015417;PubMed=9353933;
Presecan E., Moszer I., Boursier L., Cruz Ramos H., De La Fuente V., Hullo M.-F., Lelong C., Schleich S., Sekowska A., Song B.H., Villani G., Kunst F., Danchin A., Glaser P.
"The Bacillus subtilis genome from gerBC (311 degrees) to licR (334 degrees).", Microbiology 143:3313-3328(1997).
MEDLINE=98015417;PubMed=9353933;
Presecan E., Moszer I., Boursier L., Cruz Ramos H., De La Fuente V., Hullo M.-F., Lelong C., Schleich S., Sekowska A., Song B.H., Villani G., Kunst F., Danchin A., Glaser P.
"The Bacillus subtilis genome from gerBC (311 degrees) to licR (334 degrees).", Microbiology 143:3313-3328(1997).
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], STRAIN=168
MEDLINE=98044033;PubMed=9384377;DOI=10.1038/36786
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter
"?",
MEDLINE=98044033;PubMed=9384377;DOI=10.1038/36786
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter
"?",
PROTEIN SEQUENCE OF 9-43, CHARACTERIZATION, AND MASS SPECTROMETRY, STRAIN=168
MEDLINE=86111663;PubMed=3936839;
Babasaki K., Takao T., Shimonishi Y., Kurahashi K.
"Subtilosin A, a new antibiotic peptide produced by Bacillus subtilis 168: isolation, structural analysis, and biogenesis.", J. Biochem. 98:585-603(1985).
MEDLINE=86111663;PubMed=3936839;
Babasaki K., Takao T., Shimonishi Y., Kurahashi K.
"Subtilosin A, a new antibiotic peptide produced by Bacillus subtilis 168: isolation, structural analysis, and biogenesis.", J. Biochem. 98:585-603(1985).
TRANSCRIPTIONAL REGULATION, STRAIN=168 / JH642
MEDLINE=20270160;PubMed=10809710;DOI=10.1128/JB.182.11.3274-3277.2000
Nakano M.M., Zheng G., Zuber P.
"Dual control of sbo-alb operon expression by the Spo0 and ResDE systems of signal transduction under anaerobic conditions in Bacillus subtilis.", J. Bacteriol. 182:3274-3277(2000).
MEDLINE=20270160;PubMed=10809710;DOI=10.1128/JB.182.11.3274-3277.2000
Nakano M.M., Zheng G., Zuber P.
"Dual control of sbo-alb operon expression by the Spo0 and ResDE systems of signal transduction under anaerobic conditions in Bacillus subtilis.", J. Bacteriol. 182:3274-3277(2000).
STRUCTURE BY NMR, AND CYS-PHE AND CYS-THR INTRACHAIN CROSS-LINKS.
MEDLINE=22583854;PubMed=12696888;DOI=10.1021/ja029654t
Kawulka K., Sprules T., McKay R.T., Mercier P., Diaper C.M., Zuber P., Vederas J.C.
"Structure of subtilosin A, an antimicrobial peptide from Bacillus subtilis with unusual posttranslational modifications linking cysteine sulfurs to alpha-carbons of phenylalanine and threonine.", J. Am. Chem. Soc. 125:4726-4727(2003).
MEDLINE=22583854;PubMed=12696888;DOI=10.1021/ja029654t
Kawulka K., Sprules T., McKay R.T., Mercier P., Diaper C.M., Zuber P., Vederas J.C.
"Structure of subtilosin A, an antimicrobial peptide from Bacillus subtilis with unusual posttranslational modifications linking cysteine sulfurs to alpha-carbons of phenylalanine and threonine.", J. Am. Chem. Soc. 125:4726-4727(2003).
[Ref. 8]
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Protein sequence
| ........10 ........20 ........30 ........40 | | | | NKGCATCSIG AACLVDGPIP DFEIAGATGL FGLWG |
Wheel representation
3D Structure
Protein sequence annotations
| Feature | Position(s) | Length | Description |
| PEPTIDE | 1↔35 | 35 | Subtilosin-A. Feature identifier = PRO_0000002781. |
| Cross-link | 1↔35 | 35 | Cyclopeptide (Asn-Gly). |
| Cross-link | 4↔31 | 28 | 2-cysteinyl-D-phenylalanine (Cys-Phe). |
| Cross-link | 7↔28 | 22 | 2-cysteinyl-D-allo-threonine (Cys-Thr). |
| Cross-link | 13↔22 | 10 | 2-cysteinyl-L-phenylalanine (Cys-Phe). |
| TURN | 4↔7 | 4 | |
| TURN | 15↔18 | 4 | |
| HELIX | 29↔34 | 6 |
Composition
Hydrophobicity
Composition
| Formula | C152
H234
N38
O46
S3 |
| Absent amino acids | HMQRY |
| Common amino acids | G |
| Mass (Da) | 3444.56 |
| Net charge | -2 |
| Isoelectric point | 3.88 |
| Basic residues | 1 |
| Acidic residues | 3 |
| Hydrophobic residues | 15 |
| Polar residues | 14 |
| Aliphatic residues | 7 |
| Tiny residues | 13 |
| Boman Index | 16.34 |
| Hydropathy Index | 0.69 |
| Aliphatic Index | 89.43 |
| Instability Index | 24.71 (stable) |
| Half Life |
Mammalian : 1.4 hour Yeast : 3 min E. coli : >10 hour |
| Extinction Coefficient | 5625 M-1 cm-1 |
| Absorbance 280nm | 165.44 |
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