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MYP_048719
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Basic Information
Rombocin A
Antimicrobial
Standard
25 amino acids
C101H179N27O34S6
Standard
Sequence
ITSISLCTAGCITGVIMTCMSNGCK
Physicochemical Analysis
2508.05 Da
7.88
0.72
0.46
0.0288
1.11
0.39
0.37
42.70
93.60
0.0000
0.00
250.00
The radar chart summarizes major physicochemical dimensions for quick comparison, while exact numerical values remain listed on the left.
Residue Composition
Amino Acid Composition
Chemical Descriptors
972.44
-13.44
39.0
41.0
83.0
168.0
0.0
25.0
Structural Visualization
3D PDB MODEL
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2D CHEMICAL STRUCTURE
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Experimental Records
RECORD: Rec_0061493 VERIFIED: YES
Provenance & Taxonomy
Romboutsia sedimentorum [Bacterium]
Bacteriocin
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
genome mining with antiSMASH and BAGEL4. Biosynthetic gene cluster: romA: the precursor peptide; romBTC: biosynthetic genes; romRK: regulatory genes; romFEG: immunity genes, romP: maturation protease. Chemical modification: 3 amino acids dehydrated (XXW): T2, S5, and T18; four thiether rings (XXT): 3 and 8, 8 and 11, 13 and 19, and 21 and 24. Sequence analysis: APD analysis reveals that this peptide is similar (54.84%) to nisin U This peptide differs from nisin A by five amino acids, viz, P9A, K2I, A15V, L16I, and G18T, all located in rings B and C
Bio-Activity Profile
Antimicrobial
Bacillus cereus CH-85
25 μg/mL
MIC
PaperRombocin, a Short Stable Natural Nisin Variant, Displays Selective Antimicrobial Activity against Listeria monocytogenes and Employs a Dual Mode of Action to Kill Target Bacterial Strains.
RECORD: Rec_0066027 VERIFIED: YES
Provenance & Taxonomy
Romboutsia sedimentorum [Bacterium]
Bacteriocin
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
genome mining with antiSMASH and BAGEL4. Biosynthetic gene cluster: romA: the precursor peptide; romBTC: biosynthetic genes; romRK: regulatory genes; romFEG: immunity genes, romP: maturation protease. Chemical modification: 3 amino acids dehydrated (XXW): T2, S5, and T18; four thiether rings (XXT): 3 and 8, 8 and 11, 13 and 19, and 21 and 24. Sequence analysis: APD analysis reveals that this peptide is similar (54.84%) to nisin U This peptide differs from nisin A by five amino acids, viz, P9A, K2I, A15V, L16I, and G18T, all located in rings B and C
Bio-Activity Profile
Antimicrobial
Listeria monocytogenes LMG10470 or TT82E or LK132
12.5-25 μg/mL
MIC
PaperRombocin, a Short Stable Natural Nisin Variant, Displays Selective Antimicrobial Activity against Listeria monocytogenes and Employs a Dual Mode of Action to Kill Target Bacterial Strains.
RECORD: Rec_0130740 VERIFIED: YES
Provenance & Taxonomy
Romboutsia sedimentorum [Bacterium]
Bacteriocin
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
genome mining with antiSMASH and BAGEL4. Biosynthetic gene cluster: romA: the precursor peptide; romBTC: biosynthetic genes; romRK: regulatory genes; romFEG: immunity genes, romP: maturation protease. Chemical modification: 3 amino acids dehydrated (XXW): T2, S5, and T18; four thiether rings (XXT): 3 and 8, 8 and 11, 13 and 19, and 21 and 24. Sequence analysis: APD analysis reveals that this peptide is similar (54.84%) to nisin U This peptide differs from nisin A by five amino acids, viz, P9A, K2I, A15V, L16I, and G18T, all located in rings B and C
Bio-Activity Profile
Antimicrobial
Listeria monocytogenes. MIC measured: L. lactis MG1363
0.78 μg/mL
MIC
PaperRombocin, a Short Stable Natural Nisin Variant, Displays Selective Antimicrobial Activity against Listeria monocytogenes and Employs a Dual Mode of Action to Kill Target Bacterial Strains.
RECORD: Rec_0242477 VERIFIED: YES
Provenance & Taxonomy
Romboutsia sedimentorum [Bacterium]
Bacteriocin
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
genome mining with antiSMASH and BAGEL4. Biosynthetic gene cluster: romA: the precursor peptide; romBTC: biosynthetic genes; romRK: regulatory genes; romFEG: immunity genes, romP: maturation protease. Chemical modification: 3 amino acids dehydrated (XXW): T2, S5, and T18; four thiether rings (XXT): 3 and 8, 8 and 11, 13 and 19, and 21 and 24. Sequence analysis: APD analysis reveals that this peptide is similar (54.84%) to nisin U This peptide differs from nisin A by five amino acids, viz, P9A, K2I, A15V, L16I, and G18T, all located in rings B and C
Bio-Activity Profile
Antimicrobial
Staphylococcus aureus LMG10147 or LMG15975 MRSA
100 μg/mL
MIC
PaperRombocin, a Short Stable Natural Nisin Variant, Displays Selective Antimicrobial Activity against Listeria monocytogenes and Employs a Dual Mode of Action to Kill Target Bacterial Strains.
RECORD: Rec_0344377 VERIFIED: YES
Provenance & Taxonomy
Romboutsia sedimentorum [Bacterium]
Bacteriocin
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
genome mining with antiSMASH and BAGEL4. Biosynthetic gene cluster: romA: the precursor peptide; romBTC: biosynthetic genes; romRK: regulatory genes; romFEG: immunity genes, romP: maturation protease. Chemical modification: 3 amino acids dehydrated (XXW): T2, S5, and T18; four thiether rings (XXT): 3 and 8, 8 and 11, 13 and 19, and 21 and 24. Sequence analysis: APD analysis reveals that this peptide is similar (54.84%) to nisin U This peptide differs from nisin A by five amino acids, viz, P9A, K2I, A15V, L16I, and G18T, all located in rings B and C
Bio-Activity Profile
Antimicrobial
E. faecium LMG11423 or LMG16003 or LMG16216
50-100 μg/mL
MIC
PaperRombocin, a Short Stable Natural Nisin Variant, Displays Selective Antimicrobial Activity against Listeria monocytogenes and Employs a Dual Mode of Action to Kill Target Bacterial Strains.