Bacteriocin: Subtilosin-A

Default view

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: BacteriaFirmicutesBacillalesBacillaceaeBacillus

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.
Uniprot and PDB links

UniProt Entry: O07623

PDB Entry1PXQ resolved by NMR

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.
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).
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).
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).
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).
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).
STEREOCHEMISTRY OF D-ALLO-THR-36.
Vederas J.C.
"", Unpublished observations (MAY-2003).
Loading...
End Note
Reference Manager
BibTeX
Protein sequence
 ........10 ........20 ........30 ........40 
          |          |          |          | 
 NKGCATCSIG AACLVDGPIP DFEIAGATGL FGLWG

Wheel representation
wheel representation of Subtilosin-A
3D Structure
Protein sequence annotations
Features of Subtilosin-A


FeaturePosition(s)LengthDescription
PEPTIDE1↔3535
Subtilosin-A.
Feature identifier = PRO_0000002781.
Cross-link1↔3535Cyclopeptide (Asn-Gly).
Cross-link4↔31282-cysteinyl-D-phenylalanine (Cys-Phe).
Cross-link7↔28222-cysteinyl-D-allo-threonine (Cys-Thr).
Cross-link13↔22102-cysteinyl-L-phenylalanine (Cys-Phe).
TURN4↔74
TURN15↔184
HELIX29↔346
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

Users comments for Subtilosin-A

No comments found

Login or register to submit a comment for Subtilosin-A.