Bacteriocin: mersacidin
Accession: BAC014
Classification
Class: Lantibiotic, type B
Genetics
Gene: mrsA
Producer and target organisms
Producer Organism: Bacillus sp (strain HIL-Y85/54728) [Gram-positive]
Taxonomy: Bacteria
FirmicutesBacillalesBacillaceaeBacillus
Target organismsGram-positive bacteria
Description
Mode of action:
Acts at the level of cell wall biosynthesis by interfering with bacterial peptidoglycan biosynthesis. Specifically inhibits the conversion of the lipid II intermediate into polymeric nascent glycan strands by transglycosylation. May interact with the peptidoglycan precursor rather than with the enzyme.
Post-translational modification:
Maturation of lantibiotics involves the enzymic conversion of Thr, and Ser into dehydrated AA and the formation of thioether bonds with cysteine. The carboxy-terminal beta-methyllanthionine undergoes decarboxylation. This is followed by membrane translocation and cleavage of the modified precursor.
Acts at the level of cell wall biosynthesis by interfering with bacterial peptidoglycan biosynthesis. Specifically inhibits the conversion of the lipid II intermediate into polymeric nascent glycan strands by transglycosylation. May interact with the peptidoglycan precursor rather than with the enzyme.
Post-translational modification:
Maturation of lantibiotics involves the enzymic conversion of Thr, and Ser into dehydrated AA and the formation of thioether bonds with cysteine. The carboxy-terminal beta-methyllanthionine undergoes decarboxylation. This is followed by membrane translocation and cleavage of the modified precursor.
Uniprot and PDB links
UniProt Entry: P43683
PDB Entry1QOW resolved by X-ray. 1MQX resolved by NMR. 1MQY resolved by NMR. 1MQZ resolved by NMR.
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
MEDLINE=95255620;PubMed=7737474;DOI=10.1016/0378-1097(95)00048-A
Bierbaum G., Broetz H., Koller K.-P., Sahl H.-G.
"Cloning, sequencing and production of the lantibiotic mersacidin.", FEMS Microbiol. Lett. 127:121-126(1995).
MEDLINE=95255620;PubMed=7737474;DOI=10.1016/0378-1097(95)00048-A
Bierbaum G., Broetz H., Koller K.-P., Sahl H.-G.
"Cloning, sequencing and production of the lantibiotic mersacidin.", FEMS Microbiol. Lett. 127:121-126(1995).
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
MEDLINE=20292831;PubMed=10831439;DOI=10.1128/AEM.66.6.2565-2571.2000
Altena K., Guder A., Cramer C., Bierbaum G.
"Biosynthesis of the lantibiotic mersacidin: organization of a type B lantibiotic gene cluster.", Appl. Environ. Microbiol. 66:2565-2571(2000).
MEDLINE=20292831;PubMed=10831439;DOI=10.1128/AEM.66.6.2565-2571.2000
Altena K., Guder A., Cramer C., Bierbaum G.
"Biosynthesis of the lantibiotic mersacidin: organization of a type B lantibiotic gene cluster.", Appl. Environ. Microbiol. 66:2565-2571(2000).
CHARACTERIZATION.
MEDLINE=97354189;PubMed=9210483;
Broetz H., Bierbaum G., Reynolds P.E., Sahl H.-G.
"The lantibiotic mersacidin inhibits peptidoglycan biosynthesis at the level of transglycosylation.", Eur. J. Biochem. 246:193-199(1997).
MEDLINE=97354189;PubMed=9210483;
Broetz H., Bierbaum G., Reynolds P.E., Sahl H.-G.
"The lantibiotic mersacidin inhibits peptidoglycan biosynthesis at the level of transglycosylation.", Eur. J. Biochem. 246:193-199(1997).
STRUCTURE BY NMR.
MEDLINE=97234581;PubMed=9119018;
Prasch T., Naumann T., Markert R.L.M., Sattler M., Schubert W., Schaal S., Bauch M., Kogler H., Gresinger C.
"Constitution and solution conformation of the antibiotic mersacidin determined by NMR and molecular dynamics.", Eur. J. Biochem. 244:501-512(1997).
MEDLINE=97234581;PubMed=9119018;
Prasch T., Naumann T., Markert R.L.M., Sattler M., Schubert W., Schaal S., Bauch M., Kogler H., Gresinger C.
"Constitution and solution conformation of the antibiotic mersacidin determined by NMR and molecular dynamics.", Eur. J. Biochem. 244:501-512(1997).
X-RAY CRYSTALLOGRAPHY (1.06 ANGSTROMS).
MEDLINE=20280185;PubMed=10818347;DOI=10.1107/S0907444900003711
Schneider T.R., Karcher J., Pohl E., Lubini P., Sheldrick G.M.
"Ab initio structure determination of the lantibiotic mersacidin.", Acta Crystallogr. D 56:705-713(2000).
MEDLINE=20280185;PubMed=10818347;DOI=10.1107/S0907444900003711
Schneider T.R., Karcher J., Pohl E., Lubini P., Sheldrick G.M.
"Ab initio structure determination of the lantibiotic mersacidin.", Acta Crystallogr. D 56:705-713(2000).
PROTEIN STRUCTURE.
PubMed=12562773;
Hsu, S.-T., Breukink, E., Bierbaum, G., Sahl, H.-G., de Kruijff, B., Kaptein, R., van Nuland, N.A., Bonvin, A.M.
"NMR study of mersacidin and lipid II interaction in dodecylphosphocholine micelles. Conformational changes are a key to antimicrobial activity", J.Biol.Chem. (2003) 278: 13110-13117.
PubMed=12562773;
Hsu, S.-T., Breukink, E., Bierbaum, G., Sahl, H.-G., de Kruijff, B., Kaptein, R., van Nuland, N.A., Bonvin, A.M.
"NMR study of mersacidin and lipid II interaction in dodecylphosphocholine micelles. Conformational changes are a key to antimicrobial activity", J.Biol.Chem. (2003) 278: 13110-13117.
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Gene structure
| Gene id | Name | Description | Location |
| BACGene8 | mrsK2 | MrsK2 protein putative histidine-kinase | complement(1..1440) |
| BACGene9 | mrsR2 | MrsR2 protein putative response-regulator | complement(1437..2159) |
| BACGene10 | mrsF | MrsF protein putative ABC-transporter | 2402..3313 |
| BACGene11 | mrsG | MrsG protein putative ABC-transporter integral membrane protein | 3310..4068 |
| BACGene12 | mrsE | MrsE protein putative ABC-transporter integral membrane protein | 4085..4819 |
| BACGene13 | mrsA | MrsA protein mersacidin pre-peptide | 5104..5310 |
| BACGene14 | mrsR1 | MrsR1 protein putative response-regulator | 5406..6047 |
| BACGene15 | mrsD | MrsD protein putative mersacidin modifying enzyme | complement(6096..6680) |
| BACGene16 | mrsM | MrsM protein putative mersacidin modifying enzyme | 6892..10080 |
| BACGene17 | mrsT | MrsT protein putative ABC-transporter | 10132..12324 |
Protein sequence
| ........10 ........20 ........30 | | | CTFTLPGGGG VCTLTSECIC |
Wheel representation
3D Structure
Protein sequence annotations
| Feature | Position(s) | Length | Description |
| PEPTIDE | 1↔20 | 20 | Lantibiotic mersacidin. Feature identifier = PRO_0000017151. |
| Modified residue | 16 | 2,3-didehydroalanine (Ser). | |
| Cross-link | 1↔2 | 2 | Beta-methyllanthionine (Cys-Thr). |
| Cross-link | 4↔12 | 9 | Beta-methyllanthionine (Thr-Cys). |
| Cross-link | 13↔18 | 6 | Beta-methyllanthionine (Thr-Cys). |
| Cross-link | 15↔20 | 6 | S-(2-aminovinyl)-3-methyl-D-cysteine(Thr-Cys). |
| TURN | 3↔4 | 2 | |
| TURN | 7↔8 | 2 | |
| TURN | 12↔13 | 2 | |
| TURN | 16↔17 | 2 |
Composition
Hydrophobicity
Composition
| Formula | C81
H132
N20
O28
S4 |
| Absent amino acids | ADHKMNQRWY |
| Common amino acids | CGT |
| Mass (Da) | 1980.63 |
| Net charge | -1 |
| Isoelectric point | 3.85 |
| Basic residues | 0 |
| Acidic residues | 1 |
| Hydrophobic residues | 5 |
| Polar residues | 13 |
| Aliphatic residues | 4 |
| Tiny residues | 5 |
| Boman Index | 10.17 |
| Hydropathy Index | 0.94 |
| Aliphatic Index | 73 |
| Instability Index | 108.01 (unstable) |
| Half Life |
Mammalian : 1.2 hour Yeast : >20 hour E. coli : >10 hour |
| Extinction Coefficient | 250 M-1 cm-1 |
| Absorbance 280nm | 13.16 |
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