LYSC2_BOVIN
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 03-AUG-2022, entry version 140.
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; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RX 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 and
RT concerted evolution.";
RL J. Mol. Evol. 37:355-366(1993).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 19-147, AND DISULFIDE BONDS.
RX PubMed=19348005; DOI=10.1111/j.1742-4658.2009.06948.x;
RA Nonaka Y., Akieda D., Aizawa T., Watanabe N., Kamiya M., Kumaki Y.,
RA Mizuguchi M., Kikukawa T., Demura M., Kawano K.;
RT "X-ray crystallography and structural stability of digestive lysozyme from
RT cow stomach.";
RL FEBS J. 276:2192-2200(2009).
CC -!- FUNCTION: Lysozymes have primarily a bacteriolytic function; those in
CC tissues and body fluids are associated with the monocyte-macrophage
CC system and enhance the activity of immunoagents.
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 -!- 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 acts
CC rapidly on both peptide-substituted and unsubstituted peptidoglycan,
CC and slowly on chitin oligosaccharides.
CC -!- MISCELLANEOUS: The ruminant gastric lysozymes, which digest symbiotic
CC bacteria coming with cud from the rumen, are much more resistant to
CC inactivation by pepsin than are other lysozymes.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 22 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00680}.
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DR EMBL; M95098; AAC37311.1; -; Unassigned_DNA.
DR PIR; C34277; LZBO.
DR RefSeq; NP_851342.1; NM_180999.1.
DR PDB; 2Z2F; X-ray; 1.50 A; A=19-147.
DR PDBsum; 2Z2F; -.
DR AlphaFoldDB; Q06283; -.
DR SMR; Q06283; -.
DR STRING; 9913.ENSBTAP00000007924; -.
DR CAZy; GH22; Glycoside Hydrolase Family 22.
DR PaxDb; Q06283; -.
DR Ensembl; ENSBTAT00000007924; ENSBTAP00000007924; ENSBTAG00000026088.
DR GeneID; 280849; -.
DR KEGG; bta:280849; -.
DR CTD; 17105; -.
DR VEuPathDB; HostDB:ENSBTAG00000026088; -.
DR eggNOG; ENOG502S1S1; Eukaryota.
DR GeneTree; ENSGT00940000153832; -.
DR HOGENOM; CLU_111620_0_1_1; -.
DR InParanoid; Q06283; -.
DR OMA; GCGVSCK; -.
DR OrthoDB; 1551203at2759; -.
DR TreeFam; TF324882; -.
DR BRENDA; 3.2.1.17; 908.
DR EvolutionaryTrace; Q06283; -.
DR Proteomes; UP000009136; Chromosome 5.
DR Bgee; ENSBTAG00000026088; Expressed in urinary bladder and 72 other tissues.
DR GO; GO:0003796; F:lysozyme activity; IBA:GO_Central.
DR GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IBA:GO_Central.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IBA:GO_Central.
DR GO; GO:0007586; P:digestion; IEA:UniProtKB-KW.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR001916; Glyco_hydro_22.
DR InterPro; IPR019799; Glyco_hydro_22_CS.
DR InterPro; IPR000974; Glyco_hydro_22_lys.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR InterPro; IPR030056; Lysozyme_C.
DR PANTHER; PTHR11407; PTHR11407; 1.
DR PANTHER; PTHR11407:SF28; PTHR11407:SF28; 1.
DR Pfam; PF00062; Lys; 1.
DR PRINTS; PR00137; LYSOZYME.
DR PRINTS; PR00135; LYZLACT.
DR SMART; SM00263; LYZ1; 1.
DR SUPFAM; SSF53955; SSF53955; 1.
DR PROSITE; PS00128; GLYCOSYL_HYDROL_F22_1; 1.
DR PROSITE; PS51348; GLYCOSYL_HYDROL_F22_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antimicrobial; Bacteriolytic enzyme; Digestion;
KW Disulfide bond; Glycosidase; Hydrolase; Reference proteome; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000250"
FT CHAIN 19..147
FT /note="Lysozyme C-2"
FT /id="PRO_0000018455"
FT DOMAIN 19..147
FT /note="C-type lysozyme"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT ACT_SITE 53
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT ACT_SITE 71
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT DISULFID 24..145
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680,
FT ECO:0000269|PubMed:19348005"
FT DISULFID 48..133
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680,
FT ECO:0000269|PubMed:19348005"
FT DISULFID 83..99
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680,
FT ECO:0000269|PubMed:19348005"
FT DISULFID 95..113
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680,
FT ECO:0000269|PubMed:19348005"
FT HELIX 23..32
FT /evidence="ECO:0007829|PDB:2Z2F"
FT HELIX 43..54
FT /evidence="ECO:0007829|PDB:2Z2F"
FT STRAND 61..64
FT /evidence="ECO:0007829|PDB:2Z2F"
FT TURN 65..68
FT /evidence="ECO:0007829|PDB:2Z2F"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:2Z2F"
FT TURN 73..76
FT /evidence="ECO:0007829|PDB:2Z2F"
FT TURN 79..81
FT /evidence="ECO:0007829|PDB:2Z2F"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:2Z2F"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:2Z2F"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:2Z2F"
FT HELIX 99..103
FT /evidence="ECO:0007829|PDB:2Z2F"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:2Z2F"
FT HELIX 108..121
FT /evidence="ECO:0007829|PDB:2Z2F"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:2Z2F"
FT HELIX 127..132
FT /evidence="ECO:0007829|PDB:2Z2F"
FT TURN 133..135
FT /evidence="ECO:0007829|PDB:2Z2F"
FT HELIX 139..142
FT /evidence="ECO:0007829|PDB:2Z2F"
SQ SEQUENCE 147 AA; 16304 MW; B0A38B9ECE1E66BE CRC64;
MKALVILGFL FLSVAVQGKV FERCELARTL KKLGLDGYKG VSLANWLCLT KWESSYNTKA
TNYNPSSEST DYGIFQINSK WWCNDGKTPN AVDGCHVSCS ELMENDIAKA VACAKHIVSE
QGITAWVAWK SHCRDHDVSS YVEGCTL
