LYSC_COLVI
ID LYSC_COLVI Reviewed; 129 AA.
AC P00700;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 25-MAY-2022, entry version 115.
DE RecName: Full=Lysozyme C;
DE EC=3.2.1.17;
DE AltName: Full=1,4-beta-N-acetylmuramidase C;
GN Name=LYZ;
OS Colinus virginianus (Northern bobwhite) (Tetrao virginianus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Odontophoridae;
OC Colinus.
OX NCBI_TaxID=9014;
RN [1]
RP PROTEIN SEQUENCE.
RC TISSUE=Egg white;
RX PubMed=4112539; DOI=10.1016/s0021-9258(19)45297-6;
RA Prager E.M., Arnheim N., Mross G.A., Wilson A.C.;
RT "Amino acid sequence studies on bobwhite quail egg white lysozyme.";
RL J. Biol. Chem. 247:2905-2916(1972).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=8880929;
RX DOI=10.1002/(sici)1097-0134(199609)26:1<55::aid-prot5>3.0.co;2-f;
RA Chacko S., Silverton E.W., Smith-Gill S.J., Davies D.R., Schick K.A.,
RA Xavier K.A., Willson R.C., Jeffrey P.D., Chang C.Y., Sieker L.C.,
RA Sheriff S.;
RT "Refined structures of bobwhite quail lysozyme uncomplexed and complexed
RT with the HyHEL-5 Fab fragment.";
RL Proteins 26:55-65(1996).
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 -!- SUBCELLULAR LOCATION: Secreted.
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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 22 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00680}.
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DR PIR; A00855; LZQJEB.
DR PDB; 1BQL; X-ray; 2.60 A; Y=1-129.
DR PDB; 1DKJ; X-ray; 2.00 A; A=1-129.
DR PDB; 1DKK; X-ray; 1.90 A; A/B=1-129.
DR PDBsum; 1BQL; -.
DR PDBsum; 1DKJ; -.
DR PDBsum; 1DKK; -.
DR AlphaFoldDB; P00700; -.
DR BMRB; P00700; -.
DR SMR; P00700; -.
DR CAZy; GH22; Glycoside Hydrolase Family 22.
DR ABCD; P00700; 1 sequenced antibody.
DR EvolutionaryTrace; P00700; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0003796; F:lysozyme activity; IEA:UniProtKB-EC.
DR GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR GO; GO:0042742; P:defense response to bacterium; 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;
KW Direct protein sequencing; Disulfide bond; Glycosidase; Hydrolase;
KW Secreted.
FT CHAIN 1..129
FT /note="Lysozyme C"
FT /id="PRO_0000208863"
FT DOMAIN 1..129
FT /note="C-type lysozyme"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT ACT_SITE 35
FT ACT_SITE 52
FT DISULFID 6..127
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680,
FT ECO:0000269|PubMed:4112539"
FT DISULFID 30..115
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680,
FT ECO:0000269|PubMed:4112539"
FT DISULFID 64..80
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680,
FT ECO:0000269|PubMed:4112539"
FT DISULFID 76..94
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680,
FT ECO:0000269|PubMed:4112539"
FT HELIX 5..14
FT /evidence="ECO:0007829|PDB:1DKK"
FT HELIX 25..36
FT /evidence="ECO:0007829|PDB:1DKK"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:1DKK"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:1DKK"
FT TURN 54..57
FT /evidence="ECO:0007829|PDB:1DKK"
FT TURN 60..63
FT /evidence="ECO:0007829|PDB:1DKK"
FT HELIX 80..84
FT /evidence="ECO:0007829|PDB:1DKK"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:1DKK"
FT HELIX 89..99
FT /evidence="ECO:0007829|PDB:1DKK"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:1DKK"
FT HELIX 104..107
FT /evidence="ECO:0007829|PDB:1DKK"
FT HELIX 109..114
FT /evidence="ECO:0007829|PDB:1DKK"
FT TURN 115..117
FT /evidence="ECO:0007829|PDB:1DKK"
FT HELIX 120..124
FT /evidence="ECO:0007829|PDB:1DKK"
SQ SEQUENCE 129 AA; 14271 MW; 1C5797001951FF38 CRC64;
KVFGRCELAA AMKRHGLDNY RGYSLGNWVC AAKFESNFNS QATNRNTDGS TDYGVLQINS
RWWCNDGKTP GSRNLCNIPC SALLSSDITA TVNCAKKIVS DGNGMNAWVA WRNRCKGTDV
QAWIRGCRL
