Bacteriocin: mersacidin

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Bacteriocin: mersacidin

Accession: BAC014

Classification
Genetics
Gene: mrsA
Producer and target organisms

Producer Organism: Bacillus sp (strain HIL-Y85/54728) [Gram-positive]

Taxonomy: BacteriaFirmicutesBacillalesBacillaceaeBacillus

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.
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).
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).
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).
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).
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).
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.
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Gene structure
genome of mersacidin

Gene idNameDescriptionLocation
BACGene8mrsK2MrsK2 protein putative histidine-kinasecomplement(1..1440)
BACGene9mrsR2MrsR2 protein putative response-regulatorcomplement(1437..2159)
BACGene10mrsFMrsF protein putative ABC-transporter2402..3313
BACGene11mrsGMrsG protein putative ABC-transporter integral membrane protein3310..4068
BACGene12mrsEMrsE protein putative ABC-transporter integral membrane protein4085..4819
BACGene13mrsAMrsA protein mersacidin pre-peptide5104..5310
BACGene14mrsR1MrsR1 protein putative response-regulator5406..6047
BACGene15mrsDMrsD protein putative mersacidin modifying enzymecomplement(6096..6680)
BACGene16mrsMMrsM protein putative mersacidin modifying enzyme6892..10080
BACGene17mrsTMrsT protein putative ABC-transporter10132..12324
mrsK2mrsR2mrsFmrsGmrsEmrsAmrsR1mrsDmrsMmrsT
Protein sequence
 ........10 ........20 ........30 
          |          |          | 
 CTFTLPGGGG VCTLTSECIC

Wheel representation
wheel representation of mersacidin
3D Structure
Protein sequence annotations
Features of mersacidin

S
FeaturePosition(s)LengthDescription
PEPTIDE1↔2020
Lantibiotic mersacidin.
Feature identifier = PRO_0000017151.
Modified residue162,3-didehydroalanine (Ser).
Cross-link1↔22Beta-methyllanthionine (Cys-Thr).
Cross-link4↔129Beta-methyllanthionine (Thr-Cys).
Cross-link13↔186Beta-methyllanthionine (Thr-Cys).
Cross-link15↔206S-(2-aminovinyl)-3-methyl-D-cysteine(Thr-Cys).
TURN3↔42
TURN7↔82
TURN12↔132
TURN16↔172
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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