View bacteriocin : Subtilosin-A

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Accession BAC054
Name Subtilosin-A
Related Entries subtilosin
Gene sboA; Synonyms=sbo; OrderedLocusNames=BSU37350
Class Unclassified
Producer Organism Bacillus subtilis [Gram-positive]
Taxonomy BacteriaFirmicutesBacillalesBacillaceaeBacillus
Target organisms some Gram-positive bacteria such as Listeria -

some species of Bacillus - Enterococcus faecium
Swiss-Prot Entry O07623
PDB Entry 1PXQ resolved by NMR
Other databases EMBL AJ430547EMBL Z97024EMBL Z99123PIR A69704GenomeReviews AL009126_GR

SubtiList BG12671BioCyc BSUB1423:BSU3733-MONOMER
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.
[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.

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

[Ref. 3] | View abstract | Export citation
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
"?",

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

[Ref. 5] | View abstract | Export citation
FUNCTION, STRAIN=168 / JH642, and 22a
MEDLINE=20042357;PubMed=10572140;
Zheng G., Yan L.Z., Vederas J.C., Zuber P.
"Genes of the sbo-alb locus of Bacillus subtilis are required for production of the antilisterial bacteriocin subtilosin.", J. Bacteriol. 181:7346-7355(1999).

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

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

[Ref. 8]
STEREOCHEMISTRY OF D-ALLO-THR-36.
Vederas J.C.
"", Unpublished observations (MAY-2003).

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Sequence
 ........10 ........20 ........30 ........40 
          |          |          |          | 
 NKGCATCSIG AACLVDGPIP DFEIAGATGL FGLWG
Wheel representation
Structure
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
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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