DEFS2_PSEDA
ID DEFS2_PSEDA Reviewed; 94 AA.
AC A0A084G2W8;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 22-APR-2020, sequence version 2.
DT 03-AUG-2022, entry version 29.
DE RecName: Full=Fungal defensin scedosporisin-2 {ECO:0000303|PubMed:29174563};
DE Short=fDEF {ECO:0000303|PubMed:29174563};
DE Flags: Precursor;
GN ORFNames=SAPIO_CDS6842;
OS Pseudallescheria apiosperma (Scedosporium apiospermum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Microascales; Microascaceae; Scedosporium.
OX NCBI_TaxID=563466;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IHEM 14462;
RX PubMed=25278533; DOI=10.1128/genomea.00988-14;
RA Vandeputte P., Ghamrawi S., Rechenmann M., Iltis A., Giraud S., Fleury M.,
RA Thornton C., Delhaes L., Meyer W., Papon N., Bouchara J.-P.;
RT "Draft genome sequence of the pathogenic fungus Scedosporium apiospermum.";
RL Genome Announc. 2:E00988-E00988(2014).
RN [2]
RP FUNCTION, SYNTHESIS OF 53-88, 3D-STRUCTURE MODELING, AND MUTAGENESIS OF
RP 81-PRO--VAL-86.
RX PubMed=29174563; DOI=10.1016/j.peptides.2017.11.009;
RA Wu J., Liu S., Wang H.;
RT "Invasive fungi-derived defensins kill drug-resistant bacterial
RT pathogens.";
RL Peptides 99:82-91(2018).
CC -!- FUNCTION: Antibacterial peptide potently active against Gram-positive
CC bacteria (PubMed:29174563). May act by selectively inhibiting
CC peptidoglycan biosynthesis through complex formation with the cell wall
CC precursor lipid II (1:1 molar ratio) thus inhibiting cell wall
CC synthesis (By similarity). Shows remarkably activity against resistant
CC isolates such as methicillin-resistant Staphylococcus aureus (MRSA) and
CC vancomycin-resistant Enterococci (VRE) at the concentration of
CC micromolar level (PubMed:29174563). Does not act by destroying the
CC membrane integrity, which is consistent with its nonamphiphilic
CC architecture (PubMed:29174563). Acts more rapidly than vancomycin
CC (PubMed:29174563). Shows low hemolysis and cytotoxicity and high serum
CC stability (PubMed:29174563). In vivo, is as efficient as vancomycin to
CC protect mouse peritonitis models from MRSA infections
CC (PubMed:29174563). {ECO:0000250|UniProtKB:Q53I06,
CC ECO:0000269|PubMed:29174563}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Target cell membrane
CC {ECO:0000250|UniProtKB:Q53I06}.
CC -!- DOMAIN: Has the structural arrangement of an alpha-helix connected to a
CC beta-sheet by disulfide bonds (CSalpha/beta).
CC {ECO:0000305|PubMed:29174563}.
CC -!- SIMILARITY: Belongs to the invertebrate defensin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=KEZ41680.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; JOWA01000108; KEZ41680.1; ALT_FRAME; Genomic_DNA.
DR RefSeq; XP_016641479.1; XM_016788842.1.
DR AlphaFoldDB; A0A084G2W8; -.
DR SMR; A0A084G2W8; -.
DR EnsemblFungi; KEZ41680; KEZ41680; SAPIO_CDS6842.
DR GeneID; 27725914; -.
DR KEGG; sapo:SAPIO_CDS6842; -.
DR HOGENOM; CLU_1950059_0_0_1; -.
DR OrthoDB; 1612622at2759; -.
DR Proteomes; UP000028545; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
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.
DR PROSITE; PS51378; INVERT_DEFENSINS; 1.
PE 1: Evidence at protein level;
KW Antibiotic; Antimicrobial; Cleavage on pair of basic residues; Defensin;
KW Disulfide bond; Immunity; Innate immunity; Lipid-binding; Membrane;
KW Reference proteome; Secreted; Signal; Target cell membrane;
KW Target membrane.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT PROPEP 26..56
FT /evidence="ECO:0000305|PubMed:29174563"
FT /id="PRO_0000449427"
FT CHAIN 53..94
FT /note="Fungal defensin scedosporisin-2"
FT /id="PRO_0000449428"
FT REGION 57..60
FT /note="Interaction site with membrane interface"
FT /evidence="ECO:0000305|PubMed:29174563"
FT REGION 83..90
FT /note="Interaction site with membrane interface"
FT /evidence="ECO:0000305|PubMed:29174563"
FT BINDING 54
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 55
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 56
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 66
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 91
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 DISULFID 56..78
FT /evidence="ECO:0000250|UniProtKB:I1T3C7,
FT ECO:0000255|PROSITE-ProRule:PRU00710"
FT DISULFID 63..91
FT /evidence="ECO:0000250|UniProtKB:I1T3C7,
FT ECO:0000255|PROSITE-ProRule:PRU00710"
FT DISULFID 67..93
FT /evidence="ECO:0000250|UniProtKB:I1T3C7,
FT ECO:0000255|PROSITE-ProRule:PRU00710"
FT MUTAGEN 81..86
FT /note="Missing: Complete loss of antibacterial activity."
FT /evidence="ECO:0000269|PubMed:29174563"
SQ SEQUENCE 94 AA; 10048 MW; FD8724AF2FB200DE CRC64;
MKFSNISIAA LFTILASTAM AAPAADSPDS IVAREPAPVE ETYEAPSGLE KRGFGCPGSE
KKCHNHCKSV KGYKGGYCDG PYIPFVGRPR CKCY
