ID   AMP1_LIPSI              Reviewed;          18 AA.
AC   P86895;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   03-MAY-2011, sequence version 1.
DT   25-MAY-2022, entry version 8.
DE   RecName: Full=Putative antimicrobial peptide 1;
DE            Short=Ls-AMP1 {ECO:0000303|PubMed:21210197};
DE   Flags: Fragment;
OS   Lippia sidoides (Pepper-rosmarin).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Verbenaceae; Lantaneae; Lippia.
OX   NCBI_TaxID=320357;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, AND FUNCTION.
RC   TISSUE=Flower {ECO:0000269|PubMed:21210197};
RX   PubMed=21210197; DOI=10.1007/s10930-010-9299-4;
RA   Moreira J.S., Almeida R.G., Tavares L.S., Santos M.O., Viccini L.F.,
RA   Vasconcelos I.M., Oliveira J.A.T., Raposo N.R.B., Dias S.C., Franco O.L.;
RT   "Identification of botryticidal proteins with similarity to NBS LRR
RT   proteins in rosemary pepper Lippia sidoides cham flowers.";
RL   Protein J. 30:32-38(2011).
CC   -!- FUNCTION: May possess antifungal activity against B.cinerea.
CC       {ECO:0000305}.
CC   -!- CAUTION: Antifungal activity was tested using a fraction containing a
CC       number of different peptides. It is not clear which peptide actually
CC       has antifungal activity. {ECO:0000305}.
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DR   AlphaFoldDB; P86895; -.
DR   GO; GO:0050832; P:defense response to fungus; IEA:UniProtKB-KW.
DR   GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Antimicrobial; Direct protein sequencing; Fungicide; Plant defense.
FT   PEPTIDE         1..>18
FT                   /note="Putative antimicrobial peptide 1"
FT                   /id="PRO_0000407550"
FT   NON_TER         18
FT                   /evidence="ECO:0000303|PubMed:21210197"
SQ   SEQUENCE   18 AA;  2095 MW;  58BE870BE2221338 CRC64;
     EALYNSEDLY EETSDSDD