LYSM1_STRGL
ID LYSM1_STRGL Reviewed; 294 AA.
AC P25310;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 25-MAY-2022, entry version 105.
DE RecName: Full=Lysozyme M1;
DE EC=3.2.1.17;
DE AltName: Full=1,4-beta-N-acetylmuramidase M1;
DE Flags: Precursor;
GN Name=acm;
OS Streptomyces globisporus.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=1908;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 78-117, AND
RP DISULFIDE BOND.
RC STRAIN=ATCC 21553 / DSM 40991 / FERM P-596;
RX PubMed=2341041; DOI=10.1016/0378-1119(90)90062-v;
RA Lichenstein H.S., Hastings A.E., Langley K.E., Mendiaz E.A., Rohde M.F.,
RA Elmore R., Zukowski M.M.;
RT "Cloning and nucleotide sequence of the N-acetylmuramidase M1-encoding gene
RT from Streptomyces globisporus.";
RL Gene 88:81-86(1990).
CC -!- FUNCTION: This enzyme has both lysozyme (acetylmuramidase) and
CC diacetylmuramidase activities.
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.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 25 family.
CC {ECO:0000255|PROSITE-ProRule:PRU01252, ECO:0000305}.
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DR EMBL; M30645; AAA26687.1; -; Genomic_DNA.
DR PIR; JQ0529; MUSMM1.
DR PDB; 1JFX; X-ray; 1.65 A; A=78-294.
DR PDBsum; 1JFX; -.
DR AlphaFoldDB; P25310; -.
DR SMR; P25310; -.
DR CAZy; GH25; Glycoside Hydrolase Family 25.
DR EvolutionaryTrace; P25310; -.
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 InterPro; IPR002053; Glyco_hydro_25.
DR InterPro; IPR008270; Glyco_hydro_25_AS.
DR InterPro; IPR018077; Glyco_hydro_fam25_subgr.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF01183; Glyco_hydro_25; 1.
DR SMART; SM00641; Glyco_25; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS00953; GLYCOSYL_HYDROL_F25_1; 1.
DR PROSITE; PS51904; GLYCOSYL_HYDROL_F25_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antimicrobial; Bacteriolytic enzyme;
KW Direct protein sequencing; Disulfide bond; Glycosidase; Hydrolase;
KW Secreted; Signal.
FT SIGNAL 1..?
FT /evidence="ECO:0000255"
FT PROPEP ?..77
FT /evidence="ECO:0000269|PubMed:2341041"
FT /id="PRO_0000018517"
FT CHAIN 78..294
FT /note="Lysozyme M1"
FT /id="PRO_0000018518"
FT DOMAIN 81..294
FT /note="Ch-type lysozyme"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01252"
FT ACT_SITE 86
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01252"
FT ACT_SITE 175
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01252"
FT ACT_SITE 177
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01252,
FT ECO:0000255|PROSITE-ProRule:PRU10065"
FT DISULFID 185..224
FT /evidence="ECO:0000269|PubMed:2341041"
FT STRAND 81..87
FT /evidence="ECO:0007829|PDB:1JFX"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:1JFX"
FT HELIX 96..101
FT /evidence="ECO:0007829|PDB:1JFX"
FT STRAND 106..113
FT /evidence="ECO:0007829|PDB:1JFX"
FT TURN 114..116
FT /evidence="ECO:0007829|PDB:1JFX"
FT HELIX 122..131
FT /evidence="ECO:0007829|PDB:1JFX"
FT STRAND 135..141
FT /evidence="ECO:0007829|PDB:1JFX"
FT TURN 144..146
FT /evidence="ECO:0007829|PDB:1JFX"
FT HELIX 149..158
FT /evidence="ECO:0007829|PDB:1JFX"
FT STRAND 166..169
FT /evidence="ECO:0007829|PDB:1JFX"
FT STRAND 173..175
FT /evidence="ECO:0007829|PDB:1JFX"
FT STRAND 180..182
FT /evidence="ECO:0007829|PDB:1JFX"
FT TURN 184..187
FT /evidence="ECO:0007829|PDB:1JFX"
FT HELIX 190..208
FT /evidence="ECO:0007829|PDB:1JFX"
FT STRAND 213..216
FT /evidence="ECO:0007829|PDB:1JFX"
FT HELIX 218..225
FT /evidence="ECO:0007829|PDB:1JFX"
FT TURN 230..234
FT /evidence="ECO:0007829|PDB:1JFX"
FT STRAND 237..240
FT /evidence="ECO:0007829|PDB:1JFX"
FT STRAND 253..255
FT /evidence="ECO:0007829|PDB:1JFX"
FT STRAND 257..267
FT /evidence="ECO:0007829|PDB:1JFX"
FT STRAND 270..281
FT /evidence="ECO:0007829|PDB:1JFX"
FT HELIX 283..291
FT /evidence="ECO:0007829|PDB:1JFX"
SQ SEQUENCE 294 AA; 31169 MW; D96EFE914FA04997 CRC64;
MPAYSSLARR GRRPAVVLLG GLVSASLALT LAPTAAAAPL APPPGKDVGP GEAYMGVGTR
IEQGLGAGPD ERTIGPADTS GVQGIDVSHW QGSINWSSVK SAGMSFAYIK ATEGTNYKDD
RFSANYTNAY NAGIIRGAYH FARPNASSGT AQADYFASNG GGWSRDNRTL PGVLDIEHNP
SGAMCYGLST TQMRTWINDF HARYKARTTR DVVIYTTASW WNTCTGSWNG MAAKSPFWVA
HWGVSAPTVP SGFPTWTFWQ YSATGRVGGV SGDVDRNKFN GSAARLLALA NNTA
