ID   AMP20_XENBU             Reviewed;          20 AA.
AC   B3A0L3;
DT   31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2012, sequence version 1.
DT   25-MAY-2022, entry version 7.
DE   RecName: Full=Antimicrobial peptide EP-20 {ECO:0000303|PubMed:22497806};
OS   Xenorhabdus budapestensis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=290110;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, AND SUBCELLULAR LOCATION.
RC   STRAIN=NMC-10 {ECO:0000269|PubMed:22497806};
RX   PubMed=22497806; DOI=10.1016/j.peptides.2012.03.027;
RA   Xiao Y., Meng F., Qiu D., Yang X.;
RT   "Two novel antimicrobial peptides purified from the symbiotic bacteria
RT   Xenorhabdus budapestensis NMC-10.";
RL   Peptides 35:253-260(2012).
CC   -!- FUNCTION: The synthetic peptide inhibits growth of fungus P.capsici and
CC       partially that of V.dahliae, F.graminearum and F.omysporum.
CC       {ECO:0000269|PubMed:22497806}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22497806}.
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DR   AlphaFoldDB; B3A0L3; -.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0050832; P:defense response to fungus; IDA:UniProtKB.
DR   GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:UniProtKB.
DR   GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
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; Secreted.
FT   PEPTIDE         1..20
FT                   /note="Antimicrobial peptide EP-20"
FT                   /evidence="ECO:0000269|PubMed:22497806"
FT                   /id="PRO_0000419964"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   20 AA;  1788 MW;  64A12FCA49D99E96 CRC64;
     EGPVGLADPD GPASAPLGAP