ID   LYSC2_BOVIN             Reviewed;         147 AA.
AC   Q06283;
DT   27-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1999, sequence version 2.
DT   16-JUN-2009, entry version 65.
DE   RecName: Full=Lysozyme C-2;
DE            EC=3.2.1.17;
DE   AltName: Full=1,4-beta-N-acetylmuramidase C;
DE   Flags: Precursor;
GN   Name=LYZ2;
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.
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DR   EMBL; M95098; AAC37311.1; -; Unassigned_DNA.
DR   IPI; IPI00718701; -.
DR   PIR; C34277; LZBO.
DR   RefSeq; NP_851342.1; -.
DR   UniGene; Bt.29367; -.
DR   PDB; 2Z2F; X-ray; 1.50 A; A=19-147.
DR   PDBsum; 2Z2F; -.
DR   CAZy; GH22; Glycoside Hydrolase Family 22.
DR   Ensembl; ENSBTAG00000026088; Bos taurus.
DR   GeneID; 280849; -.
DR   KEGG; bta:280849; -.
DR   HOVERGEN; Q06283; -.
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   1: Evidence at protein level;
KW   3D-structure; Antimicrobial; Bacteriolytic enzyme; Digestion;
KW   Disulfide bond; Glycosidase; Hydrolase; Signal.
FT   SIGNAL        1     18       By similarity.
FT   CHAIN        19    147       Lysozyme C-2.
FT                                /FTId=PRO_0000018455.
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.
FT   HELIX        23     32
FT   HELIX        43     54
FT   STRAND       61     64
FT   TURN         65     68
FT   STRAND       69     72
FT   TURN         73     76
FT   TURN         79     81
FT   STRAND       82     84
FT   STRAND       88     90
FT   STRAND       96     98
FT   HELIX        99    103
FT   STRAND      104    106
FT   HELIX       108    121
FT   HELIX       123    125
FT   HELIX       127    132
FT   TURN        133    135
FT   HELIX       139    142
SQ   SEQUENCE   147 AA;  16304 MW;  B0A38B9ECE1E66BE CRC64;
     MKALVILGFL FLSVAVQGKV FERCELARTL KKLGLDGYKG VSLANWLCLT KWESSYNTKA
     TNYNPSSEST DYGIFQINSK WWCNDGKTPN AVDGCHVSCS ELMENDIAKA VACAKHIVSE
     QGITAWVAWK SHCRDHDVSS YVEGCTL
//