ID A0A2K0WKX5_GIBNY Unreviewed; 259 AA.
AC A0A2K0WKX5;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=lysozyme {ECO:0000256|ARBA:ARBA00012732};
DE EC=3.2.1.17 {ECO:0000256|ARBA:ARBA00012732};
GN ORFNames=FNYG_03805 {ECO:0000313|EMBL:PNP82927.1};
OS Gibberella nygamai (Bean root rot disease fungus) (Fusarium nygamai).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium fujikuroi species complex.
OX NCBI_TaxID=42673 {ECO:0000313|EMBL:PNP82927.1, ECO:0000313|Proteomes:UP000236664};
RN [1] {ECO:0000313|EMBL:PNP82927.1, ECO:0000313|Proteomes:UP000236664}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CS10214 {ECO:0000313|EMBL:PNP82927.1,
RC ECO:0000313|Proteomes:UP000236664};
RA Gardiner D.M., Obanor F., Kazan K.;
RT "Genome of Fusarium nygamai isolate CS10214.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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:PNP82927.1}.
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DR EMBL; MTQA01000055; PNP82927.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K0WKX5; -.
DR STRING; 42673.A0A2K0WKX5; -.
DR OrthoDB; 1387528at2759; -.
DR Proteomes; UP000236664; Unassembled WGS sequence.
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 Reference proteome {ECO:0000313|Proteomes:UP000236664};
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_5014433712"
SQ SEQUENCE 259 AA; 27743 MW; DD744F668C7E7F69 CRC64;
MKFALFALST LTASLAAAYP ITGNDVKCRS GPGTSYTVKK VLKKGTDVKI TCQTEGTNIS
GNTIWDKISD GCYVSDYYVK TGSSGYIKPK CGGGCSAPSS NQATVDLIGE FEGFVPHIYK
DAAGYPTVGY GHLCSNSKCT DVKYPIPLSK ANGKKLLADD MRKFEKCIAK MVSSKVTLNK
NQFGALVSWS FNLGCGAAEG SQLLKRLNKG EKPNTVISQE LPKWVYAGGR KLPGLVRRRN
AEVALAKKAT SEKALPVKC
//
