ID   LYSC1_BOVIN             Reviewed;         147 AA.
AC   Q06285;
DT   27-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1999, sequence version 2.
DT   16-JUN-2009, entry version 62.
DE   RecName: Full=Lysozyme C-1;
DE            EC=3.2.1.17;
DE   AltName: Full=1,4-beta-N-acetylmuramidase C;
DE   Flags: Precursor;
GN   Name=LYZ1;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=94141937; PubMed=8308905; DOI=10.1007/BF00178866;
RA   Irwin D.M., White R.T., Wilson A.C.;
RT   "Characterization of the cow stomach lysozyme genes: repetitive DNA
RT   and concerted evolution.";
RL   J. Mol. Evol. 37:355-366(1993).
CC   -!- FUNCTION: Lysozymes have primarily a bacteriolytic function; those
CC       in tissues and body fluids are associated with the monocyte-
CC       macrophage system and enhance the activity of immunoagents.
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of (1->4)-beta-linkages between N-
CC       acetylmuramic acid and N-acetyl-D-glucosamine residues in a
CC       peptidoglycan and between N-acetyl-D-glucosamine residues in
CC       chitodextrins.
CC   -!- SUBUNIT: Monomer.
CC   -!- TISSUE SPECIFICITY: Stomach-specific.
CC   -!- MISCELLANEOUS: Lysozyme C is capable of both hydrolysis and
CC       transglycosylation; it shows also a slight esterase activity. It
CC       acts rapidly on both peptide-substituted and unsubstituted
CC       peptidoglycan, and slowly on chitin oligosaccharides.
CC   -!- MISCELLANEOUS: The ruminant gastric lysozymes, which digest
CC       symbiotic bacteria coming with cud from the rumen, are much more
CC       resistant to inactivation by pepsin than are other lysozymes.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 22 family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; M95097; AAC37310.1; -; Unassigned_DNA.
DR   IPI; IPI00700821; -.
DR   PIR; A34277; A34277.
DR   UniGene; Bt.89770; -.
DR   HSSP; P00695; 1LZ6.
DR   Ensembl; ENSBTAG00000003270; Bos taurus.
DR   HOVERGEN; Q06285; -.
DR   OMA; Q06285; ILTECEI.
DR   BRENDA; 3.2.1.17; 251.
DR   GO; GO:0003796; F:lysozyme activity; IEA: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:0007586; P:digestion; IEA:UniProtKB-KW.
DR   InterPro; IPR001916; Glyco_hydro_22.
DR   InterPro; IPR019799; Glyco_hydro_22_CS.
DR   InterPro; IPR000974; Glyco_hydro_22_lys.
DR   Pfam; PF00062; Lys; 1.
DR   PRINTS; PR00137; LYSOZYME.
DR   PRINTS; PR00135; LYZLACT.
DR   SMART; SM00263; LYZ1; 1.
DR   PROSITE; PS00128; LACTALBUMIN_LYSOZYME_1; 1.
DR   PROSITE; PS51348; LACTALBUMIN_LYSOZYME_2; 1.
PE   2: Evidence at transcript level;
KW   Antimicrobial; Bacteriolytic enzyme; Digestion; Disulfide bond;
KW   Glycosidase; Hydrolase; Signal.
FT   SIGNAL        1     18       By similarity.
FT   CHAIN        19    147       Lysozyme C-1.
FT                                /FTId=PRO_0000018454.
FT   ACT_SITE     53     53       By similarity.
FT   ACT_SITE     71     71       By similarity.
FT   DISULFID     24    145       By similarity.
FT   DISULFID     48    133       By similarity.
FT   DISULFID     83     99       By similarity.
FT   DISULFID     95    113       By similarity.
SQ   SEQUENCE   147 AA;  16279 MW;  CBB1AB8402B2A2A9 CRC64;
     MKALIILGFL FLSVAVQGKV FERCELARTL KKLGLDGYKG VSLANWLCLT KWESSYNTKA
     TNYNPGSEST DYGIFQINSK WWCNDGKTPN AVDGCHVSCS ELMENDIAKA VACAKQIVSE
     QGITAWVAWK SHCRDHDVSS YVEGCTL
//