DEFEU_ASPAM
ID DEFEU_ASPAM Reviewed; 42 AA.
AC K7N5L0;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 1.
DT 03-AUG-2022, entry version 33.
DE RecName: Full=Fungal defensin eurocin {ECO:0000303|PubMed:23093408};
OS Aspergillus amstelodami.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Aspergillus.
OX NCBI_TaxID=5054;
RN [1] {ECO:0000312|PDB:2LT8}
RP NUCLEOTIDE SEQUENCE [MRNA], STRUCTURE BY NMR, BIOPHYSICOCHEMICAL
RP PROPERTIES, DISULFIDE BOND, AND SUBCELLULAR LOCATION.
RX PubMed=23093408; DOI=10.1074/jbc.m112.382028;
RA Oeemig J.S., Lynggaard C., Knudsen D.H., Hansen F.T., Norgaard K.D.,
RA Schneider T., Vad B.S., Sandvang D.H., Nielsen L.A., Neve S.,
RA Kristensen H.H., Sahl H.G., Otzen D.E., Wimmer R.;
RT "Eurocin, a new fungal defensin: structure, lipid binding, and its mode of
RT action.";
RL J. Biol. Chem. 287:42361-42372(2012).
CC -!- FUNCTION: Antimicrobial peptide that acts against Gram-positive
CC bacteria but not against Gram-negative bacteria (PubMed:23093408). It
CC selectively inhibits peptidoglycan biosynthesis through complex
CC formation with the cell wall precursor lipid II (1:1 molar ratio) thus
CC inhibiting cell wall synthesis (PubMed:23093408). It does not disrupt
CC cell membranes (PubMed:23093408). In vivo, is effective against an
CC intraperitoneal infection with S.pneumoniae (PubMed:23093408). In
CC vitro, it shows very low hemolytic and cytolytic activities
CC (PubMed:23093408). {ECO:0000269|PubMed:23093408}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Has the lowest denaturation temperature of 56.5 degrees Celsius at pH
CC 7. Binding to DPC micelles does not affect the thermal stability in
CC alpkaline pH. Has the lowest denaturation temperature of 71.7 degrees
CC Celsius at pH 2. Binding to DPC micelles strongly increases the
CC thermal stability in acidic pH. {ECO:0000269|PubMed:23093408};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Target cell membrane
CC {ECO:0000269|PubMed:23093408}.
CC -!- MISCELLANEOUS: The Cys-4-Pro-5 bond is in cis conformation, whereas
CC Gly-29-Pro-30 and His-35-Pro-36 bonds are in trans conformations.
CC {ECO:0000269|PubMed:23093408}.
CC -!- SIMILARITY: Belongs to the invertebrate defensin family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=The antimicrobial peptide database;
CC URL="https://wangapd3.com/database/query_output.php?ID=02119";
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DR PDB; 2LT8; NMR; -; A=1-42.
DR PDBsum; 2LT8; -.
DR AlphaFoldDB; K7N5L0; -.
DR SMR; K7N5L0; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0020002; C:host cell plasma membrane; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0032994; C:protein-lipid complex; IDA:UniProtKB.
DR GO; GO:0008289; F:lipid binding; IDA:UniProtKB.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
DR GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
DR Gene3D; 3.30.30.10; -; 1.
DR InterPro; IPR001542; Defensin_invertebrate/fungal.
DR InterPro; IPR036574; Scorpion_toxin-like_sf.
DR Pfam; PF01097; Defensin_2; 1.
DR SUPFAM; SSF57095; SSF57095; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic; Antimicrobial; Defensin; Disulfide bond;
KW Immunity; Innate immunity; Lipid-binding; Membrane; Secreted;
KW Target cell membrane; Target membrane.
FT CHAIN 1..42
FT /note="Fungal defensin eurocin"
FT /id="PRO_0000449380"
FT REGION 31..35
FT /note="Interaction site with membranes lipids"
FT /evidence="ECO:0000305|PubMed:23093408"
FT BINDING 2
FT /ligand="beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-
FT L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl
FT diphosphate"
FT /ligand_id="ChEBI:CHEBI:60033"
FT /evidence="ECO:0000250|UniProtKB:Q53I06"
FT BINDING 3
FT /ligand="beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-
FT L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl
FT diphosphate"
FT /ligand_id="ChEBI:CHEBI:60033"
FT /evidence="ECO:0000250|UniProtKB:Q53I06"
FT BINDING 4
FT /ligand="beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-
FT L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl
FT diphosphate"
FT /ligand_id="ChEBI:CHEBI:60033"
FT /evidence="ECO:0000250|UniProtKB:Q53I06"
FT BINDING 14
FT /ligand="beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-
FT L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl
FT diphosphate"
FT /ligand_id="ChEBI:CHEBI:60033"
FT /evidence="ECO:0000250|UniProtKB:Q53I06"
FT BINDING 38
FT /ligand="beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-
FT L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl
FT diphosphate"
FT /ligand_id="ChEBI:CHEBI:60033"
FT /evidence="ECO:0000250|UniProtKB:Q53I06"
FT SITE 6
FT /note="Interaction site with membranes lipids"
FT /evidence="ECO:0000305|PubMed:23093408"
FT DISULFID 4..27
FT /evidence="ECO:0000269|PubMed:23093408,
FT ECO:0007744|PDB:2LT8"
FT DISULFID 11..38
FT /evidence="ECO:0000269|PubMed:23093408,
FT ECO:0007744|PDB:2LT8"
FT DISULFID 15..40
FT /evidence="ECO:0000269|PubMed:23093408,
FT ECO:0007744|PDB:2LT8"
FT TURN 2..6
FT /evidence="ECO:0007829|PDB:2LT8"
FT HELIX 8..18
FT /evidence="ECO:0007829|PDB:2LT8"
FT STRAND 24..28
FT /evidence="ECO:0007829|PDB:2LT8"
FT STRAND 31..35
FT /evidence="ECO:0007829|PDB:2LT8"
FT STRAND 37..41
FT /evidence="ECO:0007829|PDB:2LT8"
SQ SEQUENCE 42 AA; 4345 MW; 84D82995BDAFCFEC CRC64;
GFGCPGDAYQ CSEHCRALGG GRTGGYCAGP WYLGHPTCTC SF
