ID   LYSG5_DICDI             Reviewed;         216 AA.
AC   Q54BL8;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=Probable GH family 25 lysozyme 5;
DE            EC=3.2.1.17;
DE   AltName: Full=1,4-beta-N-acetylmuramidase 5;
DE   Flags: Precursor;
GN   ORFNames=DDB_G0293566;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
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;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 25 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU01252, ECO:0000305}.
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DR   EMBL; AAFI02000218; EAL60595.1; -; Genomic_DNA.
DR   RefSeq; XP_629011.1; XM_629009.1.
DR   AlphaFoldDB; Q54BL8; -.
DR   SMR; Q54BL8; -.
DR   PaxDb; Q54BL8; -.
DR   EnsemblProtists; EAL60595; EAL60595; DDB_G0293566.
DR   GeneID; 8629295; -.
DR   KEGG; ddi:DDB_G0293566; -.
DR   dictyBase; DDB_G0293566; lyEh3.
DR   eggNOG; ENOG502S41H; Eukaryota.
DR   HOGENOM; CLU_073372_3_0_1; -.
DR   InParanoid; Q54BL8; -.
DR   OMA; QYAQVET; -.
DR   PhylomeDB; Q54BL8; -.
DR   PRO; PR:Q54BL8; -.
DR   Proteomes; UP000002195; Chromosome 6.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR   InterPro; IPR002053; Glyco_hydro_25.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF01183; Glyco_hydro_25; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS51904; GLYCOSYL_HYDROL_F25_2; 1.
PE   3: Inferred from homology;
KW   Antimicrobial; Bacteriolytic enzyme; Glycoprotein; Glycosidase; Hydrolase;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..216
FT                   /note="Probable GH family 25 lysozyme 5"
FT                   /id="PRO_0000330651"
FT   DOMAIN          21..216
FT                   /note="Ch-type lysozyme"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01252"
FT   ACT_SITE        25
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01252"
FT   ACT_SITE        113
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01252"
FT   ACT_SITE        115
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01252"
FT   CARBOHYD        31
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   216 AA;  24565 MW;  C2815F5B580C3D9C CRC64;
     MRFIISLLFV FTLIFNLAFS HIGIDVSSGT NESGFECFKQ KKYSRAIIRC YESIGSIDTN
     CKPSIENAKK AGIETIDVYL FPCYDCGNPE NQVTTTSHYL KDYLKDLDFL WLDIEGPGQY
     WSGSYDNNKK FIQGLLDSAK TAGFKHVGIY TSESQWPGIV GSWDGGKDYP IWYANYDGAE
     NFNDFSPFNG WTKPHMKQYA GNINECGLGI DKNYWE