AMPDB_72 | Subtilosin-A

1 General Description

AMPDB ID: AMPDB_72

Protein Names: Subtilosin-A (Antilisterial bacteriocin subtilosin)

Protein Family: Bacteriocin class V family

Gene Name: sboA sbo BSU37350

Source Organism: Bacillus subtilis (strain 168)

Protein Length: 43 AA

Protein Existence: Evidence at protein level

2 Protein Sequence & Composition

MKKAVIVENKGCATCSIGAACLVDGPIPDFEIAGATGLFGLWG

FASTA format

Counts of Amino Acids

'A': 6, 'R': 0, 'N': 1, 'D': 2, 'C': 3, 'Q': 0, 'E': 2, 'G': 7, 'H': 0, 'I': 4, 'L': 3, 'K': 3, 'M': 1, 'F': 2, 'P': 2, 'S': 1, 'T': 2, 'W': 1, 'Y': 0, 'V': 3

Frequencies of Amino Acids

'A': 13.95%, 'R': 0%, 'N': 2.33%, 'D': 4.65%, 'C': 6.98%, 'Q': 0%, 'E': 4.65%, 'G': 16.28%, 'H': 0%, 'I': 9.3%, 'L': 6.98%, 'K': 6.98%, 'M': 2.33%, 'F': 4.65%, 'P': 4.65%, 'S': 2.33%, 'T': 4.65%, 'W': 2.33%, 'Y': 0%, 'V': 6.98%

Missing Amino Acid(s)

H, Q, R, Y

Most Occurring Amino Acid(s)

Less Occurring Amino Acid(s)

M, N, S, W

Hydrophobic Amino Acid(s) Count

Hydrophilic Amino Acid(s) Count

Basic Amino Acid(s) Count

Acidic Amino Acid(s) Count

Modified Amino Acid(s) Count

Modified Amino Acid(s) Frequencies

Computed by biopython (version 1.79) & proteinAnalysis (version 1)

3 Physicochemical Properties

Sl. No.	Properties	Values	Reference
1.	Molecular Mass	4325.1 Da	Computed by ProtParam module (biopython 1.79)
2.	Aliphatic Index	97.674	Computed by ProtParam module (biopython 1.79)
3.	Instability Index (Half Life)	20.002	Computed by ProtParam module (biopython 1.79)
4.	Hydrophobicity (GRAVY)	0.686	Computed by ProtParam module (biopython 1.79)
5.	Hydrophobic Moment	0.295	Computed by ProtParam module (biopython 1.79)
6.	Isoelectric Point	4.544	Computed by ProtParam module (biopython 1.79)
7.	Charge (at pH 7)	-1.184	Computed by ProtParam module (biopython 1.79)
8.	Secondary Structure Fraction	0.302, 0.256, 0.279 [Helix, Turn, Sheet]	Computed by ProtParam module (biopython 1.79)
9.	Aromaticity	0.07	Computed by ProtParam module (biopython 1.79)
10.	Molar Extinction Coefficient (cysteine\|cystine)	5500, 5625	Computed by ProtParam module (biopython 1.79)

4.1 Target Organism(s)

Bacillus (Gram-positive), E.faecium (Gram-positive), Listeria (Gram-positive)

4.2 Antimicrobial Activity

Antibiotic, Antimicrobial, Bacteriocin, Anti-listeria, Anti-gram-Positive

4.3 Enzymatic Activity

4.4 Inhibitory Effect

4.5 Other Biological Activity

Hemolytic, Non-ribosomal

Activity data manually curated from Literature and UniProt

5 Database Cross-references

5.1 Literature Database

Citation 1: Presecan E, Moszer I, Boursier L, et al. The Bacillus subtilis genome from gerBC (311 degrees) to licR (334 degrees). Microbiology (Reading). 1997;143 ( Pt 10):3313-3328. Published 1997 Oct. doi:10.1099/00221287-143-10-3313

PMID: 9353933

Citation 2: Kunst F, Ogasawara N, Moszer I, et al. The complete genome sequence of the gram-positive bacterium Bacillus subtilis. Nature. 1997;390(6657):249-56. Published 1997 Nov 20. doi:10.1038/36786

PMID: 9384377

Citation 3: Babasaki K, Takao T, Shimonishi Y, et al. Subtilosin A, a new antibiotic peptide produced by Bacillus subtilis 168: isolation, structural analysis, and biogenesis. J Biochem. 1985;98(3):585-603. Published 1985 Sep. doi:10.1093/oxfordjournals.jbchem.a135315

PMID: 3936839

Citation 4: Zheng G, Yan LZ, Vederas JC, et al. Genes of the sbo-alb locus of Bacillus subtilis are required for production of the antilisterial bacteriocin subtilosin. J Bacteriol. 1999;181(23):7346-55. Published 1999 Dec. doi:10.1128/JB.181.23.7346-7355.1999

PMID: 10572140

Citation 5: Nakano MM, Zheng G, Zuber P, et al. Dual control of sbo-alb operon expression by the Spo0 and ResDE systems of signal transduction under anaerobic conditions in Bacillus subtilis. J Bacteriol. 2000;182(11):3274-7. Published 2000 Jun. doi:10.1128/JB.182.11.3274-3277.2000

PMID: 10809710

Citation 6: Huang T, Geng H, Miyyapuram VR, et al. Isolation of a variant of subtilosin A with hemolytic activity. J Bacteriol. 2009;191(18):5690-6. Published 2009 Sep. doi:10.1128/JB.00541-09

PMID: 19633086

Citation 7: FlÃ¼he L, Knappe TA, Gattner MJ, et al. The radical SAM enzyme AlbA catalyzes thioether bond formation in subtilosin A. Nat Chem Biol. 2012;8(4):350-7. Published 2012 Feb 26. doi:10.1038/nchembio.798

PMID: 22366720

Citation 8: Kawulka K, Sprules T, McKay RT, et al. 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. 2003;125(16):4726-7. Published 2003 Apr 23. doi:10.1021/ja029654t

PMID: 12696888

5.2 Protein Sequence Databases

5.3 3D Structure Databases

	Sl. no.	PDB ID	Method	Resolution	Access Links	3D View

AlphaFoldDB: O07623

5.4 Nucleotide Sequence Databases

Sl. no.	Accession(s)	Access Link(s)
1.	AJ430547	GenBank \|\| EMBL
2.	Z97024	GenBank \|\| EMBL
3.	AL009126	GenBank \|\| EMBL

5.5 Protein-Protein Interaction Databases

STRING: 224308.BSU37350

IntAct: Not found

BioGRID: Not found

5.6 Ligand Databases

BindingDB: Not found

DrugBank: Not found

ChEMBL: Not found

5.7 Family & Domain Databases

InterPro: IPR021539

PANTHER: Not found

PROSITE: Not found

5.8 Genome Annotation Databases

Ensembl: Not found

KEGG: bsu:BSU37350

5.9 Phylogenomic Databases

GeneTree: Not found

5.10 Enzyme & Pathway Databases

BRENDA: Not found

BioCyc: BSUB:BSU37350-MON

5.11 Protein-RNA Interaction Databases

RNAct: Not found

Download