ID   F9F2K4_FUSOF            Unreviewed;       259 AA.
AC   F9F2K4;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   RecName: Full=lysozyme {ECO:0000256|ARBA:ARBA00012732};
DE            EC=3.2.1.17 {ECO:0000256|ARBA:ARBA00012732};
GN   ORFNames=FOXB_00628 {ECO:0000313|EMBL:EGU88852.1};
OS   Fusarium oxysporum (strain Fo5176) (Fusarium vascular wilt).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=660025 {ECO:0000313|EMBL:EGU88852.1};
RN   [1] {ECO:0000313|EMBL:EGU88852.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fo5176 {ECO:0000313|EMBL:EGU88852.1};
RX   PubMed=21942452; DOI=10.1094/mpmi-08-11-0212;
RA   Thatcher L.F., Gardiner D.M., Kazan K., Manners J.;
RT   "A highly conserved effector in Fusarium oxysporum is required for full
RT   virulence on Arabidopsis.";
RL   Mol. Plant Microbe Interact. 25:180-190(2012).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic
CC         acid and N-acetyl-D-glucosamine residues in a peptidoglycan and
CC         between N-acetyl-D-glucosamine residues in chitodextrins.;
CC         EC=3.2.1.17; Evidence={ECO:0000256|ARBA:ARBA00000632};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EGU88852.1}.
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DR   EMBL; AFQF01000180; EGU88852.1; -; Genomic_DNA.
DR   AlphaFoldDB; F9F2K4; -.
DR   STRING; 660025.F9F2K4; -.
DR   PaxDb; 5507-FOXG_17588P0; -.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0003796; F:lysozyme activity; IEA:UniProtKB-EC.
DR   GO; GO:0016998; P:cell wall macromolecule catabolic process; IEA:InterPro.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR   GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR   CDD; cd00737; lyz_endolysin_autolysin; 1.
DR   Gene3D; 1.10.530.40; -; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   HAMAP; MF_04110; ENDOLYSIN_T4; 1.
DR   InterPro; IPR033907; Endolysin_autolysin.
DR   InterPro; IPR034690; Endolysin_T4_type.
DR   InterPro; IPR002196; Glyco_hydro_24.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   InterPro; IPR023347; Lysozyme_dom_sf.
DR   PANTHER; PTHR38107; -; 1.
DR   PANTHER; PTHR38107:SF3; LYSOZYME RRRD-RELATED; 1.
DR   Pfam; PF00959; Phage_lysozyme; 1.
DR   SUPFAM; SSF53955; Lysozyme-like; 1.
PE   3: Inferred from homology;
KW   Antimicrobial {ECO:0000256|ARBA:ARBA00022529};
KW   Bacteriolytic enzyme {ECO:0000256|ARBA:ARBA00022638};
KW   Host cytoplasm {ECO:0000256|ARBA:ARBA00023200};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..259
FT                   /note="lysozyme"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003382774"
SQ   SEQUENCE   259 AA;  27713 MW;  2D69E8ACF0D9B041 CRC64;
     MKFALFALST LTASLAAAYP ITGNDVKCRS GPGTSYAVKK VLKKGTDVKI TCQTEGTNIS
     GNTIWDKISD GCYVSDYYVK TGSSGYIKPK CGGGCSAPSS NQATVDLIGE FEGFVPHIYK
     DAAGYPTVGY GHLCSNSKCT DVKYPIPLSK ANGKKLLADD MRKFEKCIAK MVSSKVTLNK
     NQFGALVSWS FNLGCGAAEG SQLLKRLNKG EKPNTVISQE LPKWVYAGGR KLPGLVRRRN
     AEVALAKKAT SEKALPVKC
//