ID   LYSG4_DICDI             Reviewed;         213 AA.
AC   Q54BQ8;
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 4;
DE            EC=3.2.1.17;
DE   AltName: Full=1,4-beta-N-acetylmuramidase 4;
DE   Flags: Precursor;
GN   ORFNames=DDB_G0293492;
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; AAFI02000215; EAL60698.1; -; Genomic_DNA.
DR   RefSeq; XP_629111.1; XM_629109.1.
DR   AlphaFoldDB; Q54BQ8; -.
DR   SMR; Q54BQ8; -.
DR   PaxDb; Q54BQ8; -.
DR   EnsemblProtists; EAL60698; EAL60698; DDB_G0293492.
DR   GeneID; 8629251; -.
DR   KEGG; ddi:DDB_G0293492; -.
DR   dictyBase; DDB_G0293492; lyEh2.
DR   eggNOG; ENOG502S1SN; Eukaryota.
DR   HOGENOM; CLU_073372_3_0_1; -.
DR   InParanoid; Q54BQ8; -.
DR   OMA; NCANAHA; -.
DR   PhylomeDB; Q54BQ8; -.
DR   PRO; PR:Q54BQ8; -.
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; Glycosidase; Hydrolase;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..213
FT                   /note="Probable GH family 25 lysozyme 4"
FT                   /id="PRO_0000330650"
FT   DOMAIN          21..213
FT                   /note="Ch-type lysozyme"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01252"
FT   ACT_SITE        24
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01252"
FT   ACT_SITE        112
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01252"
FT   ACT_SITE        114
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01252"
SQ   SEQUENCE   213 AA;  23179 MW;  3FAADF14EB14F4BB CRC64;
     MRLFLLLITF IALFGAINAF SGVDISQGSS VGDFQCMLNQ GFEFAIIRGY METGQVDPEV
     VNSIACAREA GVEYVDTYLF PCFNCGNPQD QGPALVNYLS GYNANYGMVW LDIESSDWSG
     DQSANVAFFE GLISGLQSVG AHIGVYTSAS QWIPIMGGYT GGSEFPLWYA NWDGVQSFDD
     FSAFGGWSTP AIKQYNDGGS NCGVGYDFNW YPN