Bacteriocin: Cypemycin
Accession: BAC218
Classification
Class: Unclassified
Genetics
Gene: cypA
Producer and target organisms
Producer Organism: Streptomyces sp [Gram-positive]
Taxonomy: Bacteria
ActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces
Target organismsUnavailable data
Description
FUNCTION:
- Antibiotic peptide structurally related to lantibiotics.
- Active against M.luteus (MIC=0.2 ug/ml). Has cytotoxic activity against mouse P388 leukemia cells (IC(50)=1.3 ug/ml).
SUBCELLULAR LOCATION:
- Secreted. Secreted, extracellular space.
PTM:
- Maturation involves the enzymatic conversion of Cys-61 into 2,3-didehydroalanine followed by formation of a thioether bond with Cys-64. The C-terminal meso-lanthionine then undergoes decarboxylation.
- Dimethylated at the N-terminus. Dimethylation is required for antibiotic activity.
- The configuration of reformed Cys-61 as the D form was attributed by similarity to related structures.
SIMILARITY:
- Belongs to the linaridin family.
- Antibiotic peptide structurally related to lantibiotics.
- Active against M.luteus (MIC=0.2 ug/ml). Has cytotoxic activity against mouse P388 leukemia cells (IC(50)=1.3 ug/ml).
SUBCELLULAR LOCATION:
- Secreted. Secreted, extracellular space.
PTM:
- Maturation involves the enzymatic conversion of Cys-61 into 2,3-didehydroalanine followed by formation of a thioether bond with Cys-64. The C-terminal meso-lanthionine then undergoes decarboxylation.
- Dimethylated at the N-terminus. Dimethylation is required for antibiotic activity.
- The configuration of reformed Cys-61 as the D form was attributed by similarity to related structures.
SIMILARITY:
- Belongs to the linaridin family.
Uniprot and PDB links
UniProt Entry: E5KIB6
PDB EntryUnknown
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 45-60, FUNCTION, MASS SPECTROMETRY, AND METHYLATION AT ALA-43, STRAIN=OH-4156.
PubMed=20805503;DOI=10.1073/pnas.1008608107
Claesen J., Bibb M.
"Genome mining and genetic analysis of cypemycin biosynthesis reveal an unusual class of posttranslationally modified peptides.", Proc. Natl. Acad. Sci. U.S.A. 107:16297-16302(2010).
PubMed=20805503;DOI=10.1073/pnas.1008608107
Claesen J., Bibb M.
"Genome mining and genetic analysis of cypemycin biosynthesis reveal an unusual class of posttranslationally modified peptides.", Proc. Natl. Acad. Sci. U.S.A. 107:16297-16302(2010).
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Gene structure
| Gene id | Name | Description | Location |
| BACGene998 | putative regulatory protein orf1 | complement(57..3308) | |
| BACGene999 | cypemycin structural protein cypA | 3882..4076 | |
| BACGene1000 | hypothetical protein cypH; contains N-terminal HTTM domain and C-terminal alpha/beta hydrolase fold | 4191..5945 | |
| BACGene1001 | unknown cypL | 5935..6495 | |
| BACGene1002 | HFCD family decarboxylase cypD | 6492..7064 | |
| BACGene1003 | SAM-dependent methyltransferase cypM | 7057..7794 | |
| BACGene1004 | ABC transporter ATP binding subunit cypT | 7791..8423 | |
| BACGene1005 | putative transmembrane pore cypP; contains 12 transmembrane helices | 8420..9970 | |
| BACGene1006 | DUF255 family protein cypI | 10053..12074 |
Protein sequence
| ........10 ........20 ........30 | | | ATPATPTVAQ FVIQGSTICL VC |
Wheel representation
Protein sequence annotations
| Feature | Position(s) | Length | Description |
| PEPTIDE | 1↔22 | 22 | Cypemycin. Feature identifier = PRO_0000408758.
|
| Modified residue | 1 | N,N-dimethylalanine. | |
| Modified residue | 2 | (E)-2,3-didehydrobutyrine. | |
| Modified residue | 5 | (E)-2,3-didehydrobutyrine. | |
| Modified residue | 7 | (E)-2,3-didehydrobutyrine. | |
| Modified residue | 13 | L-allo-isoleucine. | |
| Modified residue | 17 | (E)-2,3-didehydrobutyrine. | |
| Modified residue | 18 | L-allo-isoleucine. | |
| Cross-link | 19↔22 | 4 | S-(2-aminovinyl)-D-cysteine (Cys-Cys). |
Composition
| Amino acid | Count | Percent |
|---|---|---|
| A | 3 | 13.64 % |
| C | 2 | 9.09 % |
| D | 0 | 0.00 % |
| E | 0 | 0.00 % |
| F | 1 | 4.55 % |
| G | 1 | 4.55 % |
| H | 0 | 0.00 % |
| I | 2 | 9.09 % |
| K | 0 | 0.00 % |
| L | 1 | 4.55 % |
| M | 0 | 0.00 % |
| N | 0 | 0.00 % |
| P | 2 | 9.09 % |
| Q | 2 | 9.09 % |
| R | 0 | 0.00 % |
| S | 1 | 4.55 % |
| T | 4 | 18.18 % |
| V | 3 | 13.64 % |
| W | 0 | 0.00 % |
| Y | 0 | 0.00 % |
Hydrophobicity
Composition
| Formula | C0
H0
N0
O0
S0 |
| Absent amino acids | DEHKMNRWY |
| Common amino acids | T |
| Mass (Da) | 2 |
| Net charge | 0 |
| Isoelectric point | 5.84 |
| Basic residues | 0 |
| Acidic residues | 0 |
| Hydrophobic residues | 10 |
| Polar residues | 8 |
| Aliphatic residues | 6 |
| Tiny residues | 5 |
| Boman Index | 14.03 |
| Hydropathy Index | 1.109 |
| Aliphatic Index | 106.36 |
| Instability Index | 23.63 (stable) |
| Half Life |
Mammalian : 4.4 hour Yeast : >20 hour E. coli : >10 hour |
| Extinction Coefficient | 125 M-1 cm-1 |
| Absorbance 280nm | 5.95 |