ID   AMP1_ALLCE              Reviewed;         132 AA.
AC   Q41258;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   25-MAY-2022, entry version 73.
DE   RecName: Full=Antimicrobial protein Ace-AMP1;
DE   Flags: Precursor;
OS   Allium cepa (Onion).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Amaryllidaceae;
OC   Allioideae; Allieae; Allium.
OX   NCBI_TaxID=4679;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 37-120, AND DISULFIDE
RP   BONDS.
RC   TISSUE=Seed;
RX   PubMed=7480341; DOI=10.1104/pp.109.2.445;
RA   Cammue B.P.A., Thevissen K., Hendriks M., Eggermont K., Goderis I.J.,
RA   Proost P., van Damme J., Osborn R.W., Guerbette F., Kader J.-C.,
RA   Broekaert W.F.;
RT   "A potent antimicrobial protein from onion seeds showing sequence homology
RT   to plant lipid transfer proteins.";
RL   Plant Physiol. 109:445-455(1995).
RN   [2]
RP   STRUCTURE BY NMR.
RX   PubMed=9521681; DOI=10.1021/bi9723515;
RA   Tassin S., Broekaert W.F., Marion D., Acland D.P., Ptak M., Vovelle F.,
RA   Sodano P.;
RT   "Solution structure of Ace-AMP1, a potent antimicrobial protein extracted
RT   from onion seeds. Structural analogies with plant nonspecific lipid
RT   transfer proteins.";
RL   Biochemistry 37:3623-3637(1998).
CC   -!- FUNCTION: Antifungal and antibacterial activity against the Gram-
CC       positive bacteria B.megaterium and S.lutea.
CC   -!- SUBUNIT: Monomer.
CC   -!- SIMILARITY: Belongs to the plant LTP family. Highly divergent.
CC       {ECO:0000305}.
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DR   EMBL; AF004946; AAB60896.1; -; mRNA.
DR   AlphaFoldDB; Q41258; -.
DR   SMR; Q41258; -.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
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.
DR   Gene3D; 1.10.110.10; -; 1.
DR   InterPro; IPR036312; Bifun_inhib/LTP/seed_sf.
DR   InterPro; IPR016140; Bifunc_inhib/LTP/seed_store.
DR   SMART; SM00499; AAI; 1.
DR   SUPFAM; SSF47699; SSF47699; 1.
PE   1: Evidence at protein level;
KW   Antibiotic; Antimicrobial; Direct protein sequencing; Disulfide bond;
KW   Fungicide; Plant defense; Signal.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..132
FT                   /note="Antimicrobial protein Ace-AMP1"
FT                   /id="PRO_0000018416"
FT   DISULFID        31..76
FT                   /evidence="ECO:0000269|PubMed:7480341"
FT   DISULFID        41..54
FT                   /evidence="ECO:0000269|PubMed:7480341"
FT   DISULFID        55..100
FT                   /evidence="ECO:0000269|PubMed:7480341"
FT   DISULFID        74..116
FT                   /evidence="ECO:0000269|PubMed:7480341"
SQ   SEQUENCE   132 AA;  15142 MW;  ABFE54828DFCD1EB CRC64;
     MVRVVSLLAA STFILLIMII SSPYANSQNI CPRVNRIVTP CVAYGLGRAP IAPCCRALND
     LRFVNTRNLR RAACRCLVGV VNRNPGLRRN PRFQNIPRDC RNTFVRPFWW RPRIQCGRIN
     LTDKLIYLDA EE