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Peptide record

TPDB91308

Microbisporicin A1 (Bacteriocin) Antimicrobial Antibacterial modified_plain modified
24 amino acids
Basic Information
3D PDB MODEL
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TPDB91308
Microbisporicin A1 (Bacteriocin)
Antimicrobial Antibacterial
Anti-infective peptides
DRAMP
modified_plain
Yes
A 24-aa modified multi-activity (Antimicrobial and Antibacterial) peptide sequence curated from DRAMP, with an available 3D structural model.
C-terminal: Amidation and Cyclization Other: ①There are five thioether intramolecular bridges which link Ala3 and Ala7, Ala8 and Ala11, Ala13 and Ala20, Ala18 and Ala23, respectively. ②The residue at position 2 is (Z)-2,3-didehydrobutyrine (Dhb). ③The residue at position 4 is chloro-tryptophan (ClTrp). ④The residue at position 5 is 2,3-didehydroalanine. ⑤The residue at position 8 is 2-Aminobutyric acid (Abu). ⑥The residue at position 14 is bis-hydroxylated proline.
Sequence
VTSWSLCTPGCTSPGGGSNCSFCC
Physicochemical Analysis
C95H144N26O34S5
ARDEQHIKMY
CS
2354.64
4.98
0
0
4
-0
-2.24
0.333
28.33
Mammalian: 100 hour Yeast: >20 hour E.coli: >10 hour
5750
244.20
14
Residue Composition
number
0
A
0
R
1
N
0
D
5
C
0
E
0
Q
4
G
0
H
0
I
1
L
0
K
0
M
1
F
2
P
5
S
3
T
1
W
0
Y
1
V
Amino Acid Distribution
A: 0 R: 0 N: 1 D: 0 C: 5 E: 0 Q: 0 G: 4 H: 0 I: 0 L: 1 K: 0 M: 0 F: 1 P: 2 S: 5 T: 3 W: 1 Y: 0 V: 1
Chemical Descriptors
24
C95H144N26O34S5
2354.64
4.98
-0
-2.24
0.333
Amidation and Cyclization
Free
Evidence Records 1 records
Evidence 1 Activity

Target

Cutibacterium acnes

Source & Reference

DRAMP
Castiglione F, Lazzarini A, Carrano L, Corti E, Ciciliato I, Gastaldo L, Candiani P, Losi D, Marinelli F, Selva E, Parenti F.
Determining the structure and mode of action of microbisporicin, a potent lantibiotic active against multiresistant pathogens.
Chem Biol. 2008 Jan 15(1):22-31.

Other

Source Activity Label Source Definition
Antimicrobial Antibacterial
DRAMP antibacterial activity supported by MIC records against bacterial target organisms.
Microbispora corallina (Gram-positive bacteria)
Belongs to the lantibiotic family (Class I bacteriocin)
Function: Microbisporicins A1 displayed similar antibacterial activity by selectively blocking peptidoglycan biosynthesis, leading to cytoplasmic accumulation of the UDP-linked precursor. PTM: Microbisporicin A1 contains five ether rings: S3-C7, T8-C11, S13-C20, S18-C23, and S21-C24. Also, residues T2 and S5 are dehydrated, Trp4 is chlorinated and Pro14 is hydroxylated (3,4-dihydroxylation).
Additional Detail Fields 1 fields
Belongs to the lantibiotic family (Class I bacteriocin)