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PR00323

Identifier
GALLIDERMIN  [View Relations]  [View Alignment]  
Accession
PR00323
No. of Motifs
2
Creation Date
01-JUL-1994  (UPDATE 19-JUN-1999)
Title
Gallidermin signature
Database References

INTERPRO; IPR001049
Literature References
1. BIERBAUM, G. AND SAHL, H.-G. 
Lantibiotics - unusually modified bacteriocin-like peptides from Gram-
positive bacteria.
INT.J.MED.MICROBIOL.VIROL.PARASITOL.INFECT.DIS. 278 1-22 (1993).
 
2. BUCHMAN, G.W., BANERJEE, S. AND HANSEN, J.N.
Structure, expression and evolution of a gene encoding the precursor
of nisin, a small protein antibiotic.
J.BIOL.CHEM. 263(31) 16260-16266 (1988).
 
3. LIAN, L.-Y., CHAN, W.C., MORLEY, S.D., ROBERTS, G.C.K., 
BYCROFT, B.W. AND JACKSON, D.
NMR studies of the solution structure of nisin A and related peptides.
IN NISIN AND THE NOVEL LANTIBIOTICS, EDS. G.JUNG AND H.-G.SAHL, LEIDEN/
ESCOM SCIENCE PUBLISHERS (NETHERLANDS) PP.43-58 (1991).
 
4. KUIPERS, O.P., ROLLEMA, H.S., YAP, W.M.J.G., BOOT, H.J., 
SIEZEN, R.J. AND DEVOS, W.M.
Engineering dehydrated amino acid residues in the antimicrobial 
peptide nisin.
J.BIOL.CHEM. 267(34) 24340-24346 (1992).
 
5. FREUND, S., JUNG, G., GUTBROD, O., FOLKERS, G., GIBBONS, W.A.,
ALLGAIER, H. AND WERNER, R.
The solution structure of the lantibiotic gallidermin.
BIOPOLYMERS 31(6) 803-811 (1991).

Documentation
Lantibiotics are heavily-modified bacteriocin-like peptides from Gram-
positive bacteria [1]. They contain alpha,beta-unsaturated amino acids
(dehydroalanine and dehydrobutyrine) and lanthionine or 3-methyllanthionine
rings (collectively known as thioether rings). There are 2 types of
lantibiotic: type A (which include nisin, subtilin, epidermin, gallidermin
and Pep5) are strongly cationic and bactericidal - nisin, subtilin and Pep5
inhibit the growth of Gram-positive bacteria, probably by voltage-dependent
pore formation in the cytoplasmic membrane, resulting in cellular efflux of
electrolytes, amino acids and ATP; type B lantibiotics possess at most one
positive charge and are not bactericidal. Nisin, subtilin, epidermin and
gallidermin are likely to have evolved from a common ancestor [2].
 
The sequences of lantibiotics do not adopt regular secondary structures 
(i.e., alpha-helices and beta-strands) because of their constituent
thioether rings (4 are found in gallidermin). Nevertheless, the rings
may be important in providing rigid local structures, which could be
essential for pore formation in membranes [3,4]. Solution NMR indicates
gallidermin to have a similar structure to nisin in the region of its
first 2 lanthionine rings [5].
 
GALLIDERMIN is a 2-element fingerprint that provides a signature for the 
gallidermin/epidermin type of lantibiotics. The fingerprint was derived
from an initial alignment of 2 sequences: the motifs span the full
alignment length. A single iteration on OWL23.1 was required to reach
convergence, no further sequences being identified beyond the starting set.
 
An update on SPTR37_9f identified a true set of 4 sequences.
Summary Information
4 codes involving  2 elements
Composite Feature Index
244
12
True Positives
LANE_STAEP    LANG_STAGA    LANM_STRMU    O68586        
Sequence Titles
LANE_STAEP  LANTIBIOTIC EPIDERMIN PRECURSOR - STAPHYLOCOCCUS EPIDERMIDIS. 
LANG_STAGA LANTIBIOTIC GALLIDERMIN PRECURSOR - STAPHYLOCOCCUS GALLINARUM.
LANM_STRMU LANTIBIOTIC MUTACIN B-NY266 - STREPTOCOCCUS MUTANS.
O68586 MUTACIN 1140 PREPROPEPTIDE - STREPTOCOCCUS MUTANS.
Scan History
OWL23_1    1  100  NSINGLE    
OWL26_0 1 100 NSINGLE
SPTR37_9f 2 100 NSINGLE
Initial Motifs
Motif 1  width=10
Element Seqn Id St Int Rpt
ASKFLCTPGC LANG_STAGA 2 2 -
ASKFICTPGC LANE_STAEP 32 32 -

Motif 2 width=10
Element Seqn Id St Int Rpt
AKTGSFNSYC LANG_STAGA 12 0 -
AKTGSFNSYC LANE_STAEP 42 0 -
Final Motifs
Motif 1  width=10
Element Seqn Id St Int Rpt
ASKFLCTPGC LANG_STAGA 2 2 -
KSWSFCTPGC LANM_STRMU 2 2 -
ASKFICTPGC LANE_STAEP 32 32 -
KSWSLCTPGC O68586 43 43 -

Motif 2 width=10
Element Seqn Id St Int Rpt
AKTGSFNSYC LANG_STAGA 12 0 -
AKTGSFNSYC LANM_STRMU 12 0 -
AKTGSFNSYC LANE_STAEP 42 0 -
ARTGSFNSYC O68586 53 0 -