ID   LYB_BACIU               Reviewed;         117 AA.
AC   P10773;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   03-MAY-2023, entry version 49.
DE   RecName: Full=B-enzyme;
DE   AltName: Full=Lysozyme;
DE            EC=3.2.1.17;
GN   Name=lyzB;
OS   Bacillus subtilis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1423;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   STRAIN=YT-25;
RX   PubMed=3148618; DOI=10.1093/oxfordjournals.jbchem.a122558;
RA   Kamei K., Hara S., Ikenaka T., Murao S.;
RT   "Amino acid sequence of a lysozyme (B-enzyme) from Bacillus subtilis
RT   YT-25.";
RL   J. Biochem. 104:832-836(1988).
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   -!- MISCELLANEOUS: Usually lysozymes have a catalytic site with Asp and
CC       Glu, but B-enzyme has no Glu (two Asp for catalytic site).
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DR   PIR; JX0053; JX0053.
DR   AlphaFoldDB; P10773; -.
DR   GO; GO:0003796; F:lysozyme activity; IEA:UniProtKB-EC.
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:0008152; P:metabolic process; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Antimicrobial; Bacteriolytic enzyme; Direct protein sequencing;
KW   Glycosidase; Hydrolase.
FT   CHAIN           1..117
FT                   /note="B-enzyme"
FT                   /id="PRO_0000057725"
FT   ACT_SITE        89
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   117 AA;  12732 MW;  322C5FD7C5EB3762 CRC64;
     ISPLGSVTKK NQDSTAYNWT GNKTANGNWP VLGICAVHRK KDIGGSGNSP VIPFGTTLKT
     DKDIWLPDGV GYKSSFNVDD TGSGPKKTDY WIDIYYSKDT KAAINYGVVK LSYTYST
//