AMPDB_149 | Lantibiotic subtilin

1 General Description

AMPDB ID: AMPDB_149

Protein Names: Lantibiotic subtilin

Protein Family: Type A lantibiotic family

Gene Name: spaS sub

Source Organism: Bacillus subtilis

Protein Length: 56 AA

Protein Existence: Evidence at protein level

2 Protein Sequence & Composition

MSKFDDFDLDVVKVSKQDSKITPQWKSESLCTPGCVTGALQTCFLQTLTCNCKISK

FASTA format

Counts of Amino Acids

'A': 1, 'R': 0, 'N': 1, 'D': 5, 'C': 5, 'Q': 4, 'E': 1, 'G': 2, 'H': 0, 'I': 2, 'L': 5, 'K': 7, 'M': 1, 'F': 3, 'P': 2, 'S': 6, 'T': 6, 'W': 1, 'Y': 0, 'V': 4

Frequencies of Amino Acids

'A': 1.79%, 'R': 0%, 'N': 1.79%, 'D': 8.93%, 'C': 8.93%, 'Q': 7.14%, 'E': 1.79%, 'G': 3.57%, 'H': 0%, 'I': 3.57%, 'L': 8.93%, 'K': 12.5%, 'M': 1.79%, 'F': 5.36%, 'P': 3.57%, 'S': 10.71%, 'T': 10.71%, 'W': 1.79%, 'Y': 0%, 'V': 7.14%

Missing Amino Acid(s)

H, R, Y

Most Occurring Amino Acid(s)

Less Occurring Amino Acid(s)

A, E, M, N, 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	6218.21 Da	Computed by ProtParam module (biopython 1.79)
2.	Aliphatic Index	71.25	Computed by ProtParam module (biopython 1.79)
3.	Instability Index (Half Life)	48.146	Computed by ProtParam module (biopython 1.79)
4.	Hydrophobicity (GRAVY)	-0.184	Computed by ProtParam module (biopython 1.79)
5.	Hydrophobic Moment	0.475	Computed by ProtParam module (biopython 1.79)
6.	Isoelectric Point	7.813	Computed by ProtParam module (biopython 1.79)
7.	Charge (at pH 7)	0.69	Computed by ProtParam module (biopython 1.79)
8.	Secondary Structure Fraction	0.268, 0.196, 0.143 [Helix, Turn, Sheet]	Computed by ProtParam module (biopython 1.79)
9.	Aromaticity	0.071	Computed by ProtParam module (biopython 1.79)
10.	Molar Extinction Coefficient (cysteine\|cystine)	5500, 5750	Computed by ProtParam module (biopython 1.79)

4.1 Target Organism(s)

Gram Positive Bacteria

4.2 Antimicrobial Activity

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

4.3 Enzymatic Activity

4.4 Inhibitory Effect

4.5 Other Biological Activity

Non-hemolytic, Non-ribosomal

Activity data manually curated from Literature and UniProt

5 Database Cross-references

5.1 Literature Database

Citation 1: Banerjee S, Hansen JN, Hansen JN. Structure and expression of a gene encoding the precursor of subtilin, a small protein antibiotic. J Biol Chem. 1988;263(19):9508-14. Published 1988 Jul 5. doi:

PMID: 2837490

Citation 2: Chung YJ, Steen MT, Hansen JN, et al. 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. 1992;174(4):1417-22. Published 1992 Feb. doi:10.1128/jb.174.4.1417-1422.1992

PMID: 1735728

Citation 3: Klein C, Kaletta C, Schnell N, et al. Analysis of genes involved in biosynthesis of the lantibiotic subtilin. Appl Environ Microbiol. 1992;58(1):132-42. Published 1992 Jan. doi:10.1128/aem.58.1.132-142.1992

PMID: 1539969

Citation 4: Chung YJ, Hansen JN, Hansen JN. Determination of the sequence of spaE and identification of a promoter in the subtilin (spa) operon in Bacillus subtilis. J Bacteriol. 1992;174(20):6699-702. Published 1992 Oct. doi:10.1128/jb.174.20.6699-6702.1992

PMID: 1400221

Citation 5: Klein C, Entian KD, Entian KD. Genes involved in self-protection against the lantibiotic subtilin produced by Bacillus subtilis ATCC 6633. Appl Environ Microbiol. 1994;60(8):2793-801. Published 1994 Aug. doi:10.1128/aem.60.8.2793-2801.1994

PMID: 8085823

Citation 6: Gross E, Kiltz HH, Nebelin E, et al. [Subtilin, VI: the structure of subtilin (author's transl)]. Hoppe Seylers Z Physiol Chem. 1973;354(7):810-2. Published 1973 Jul. doi:

PMID: 4154277

Citation 7: SchÃ¼ller F, Benz R, Sahl HG, et al. The peptide antibiotic subtilin acts by formation of voltage-dependent multi-state pores in bacterial and artificial membranes. Eur J Biochem. 1989;182(1):181-6. Published 1989 Jun 1. doi:10.1111/j.1432-1033.1989.tb14815.x

PMID: 2471644

Citation 8: Chan WC, Bycroft BW, Leyland ML, et al. A novel post-translational modification of the peptide antibiotic subtilin: isolation and characterization of a natural variant from Bacillus subtilis A.T.C.C. 6633. Biochem J. 1993;291 ( Pt 1)(Pt 1):23-7. Published 1993 Apr 1. doi:10.1042/bj2910023

PMID: 8471040

Citation 9: Chan WC, Bycroft BW, Leyland ML, et al. Sequence-specific resonance assignment and conformational analysis of subtilin by 2D NMR. FEBS Lett. 1992;300(1):56-62. Published 1992 Mar 23. doi:10.1016/0014-5793(92)80163-b

PMID: 1547888

Citation 10: Liu W, Hansen JN, Hansen JN. 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. 1993;59(2):648-51. Published 1993 Feb. doi:10.1128/aem.59.2.648-651.1993

PMID: 8434932

5.2 Protein Sequence Databases

5.3 3D Structure Databases

AlphaFoldDB: P10946

5.4 Nucleotide Sequence Databases

Sl. no.	Accession(s)	Access Link(s)
1.	J03767	GenBank \|\| EMBL
2.	M83944	GenBank \|\| EMBL
3.	M86869	GenBank \|\| EMBL
4.	M99263	GenBank \|\| EMBL
5.	U09819	GenBank \|\| EMBL

RefSeq: WP_003220055.1

5.5 Protein-Protein Interaction Databases

STRING: Not found

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: IPR006079

PANTHER: Not found

PROSITE: Not found

5.8 Genome Annotation Databases

Ensembl: Not found

5.9 Phylogenomic Databases

GeneTree: Not found

5.10 Enzyme & Pathway Databases

BRENDA: Not found

BioCyc: Not found

5.11 Protein-RNA Interaction Databases

RNAct: Not found

Download