LYSC_PHACO
ID LYSC_PHACO Reviewed; 147 AA.
AC P00702;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 2.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Lysozyme C;
DE EC=3.2.1.17;
DE AltName: Full=1,4-beta-N-acetylmuramidase C;
DE Flags: Precursor;
GN Name=LYZ;
OS Phasianus colchicus colchicus (Black-necked pheasant).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Phasianus.
OX NCBI_TaxID=9057;
RN [1]
RP PROTEIN SEQUENCE OF 1-18 (PRECURSOR PROTEIN).
RX PubMed=3511061; DOI=10.1016/s0021-9258(17)35936-7;
RA Weisman L.S., Krummel B.M., Wilson A.C.;
RT "Evolutionary shift in the site of cleavage of prelysozyme.";
RL J. Biol. Chem. 261:2309-2313(1986).
RN [2]
RP PROTEIN SEQUENCE OF 18-147.
RX PubMed=476049; DOI=10.1021/bi00580a009;
RA Jolles J., Ibrahimi I.M., Prager E.M., Schoentgen F., Jolles P.,
RA Wilson A.C.;
RT "Amino acid sequence of pheasant lysozyme. Evolutionary change affecting
RT processing of prelysozyme.";
RL Biochemistry 18:2744-2752(1979).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RX PubMed=8356074; DOI=10.1073/pnas.90.16.7711;
RA Chitarra V., Alzari P.M., Bentley G.A., Bhat T.N., Eisele J.L.,
RA Houdusse A., Lescar J., Souchon H., Poljak R.J.;
RT "Three-dimensional structure of a heteroclitic antigen-antibody cross-
RT reaction complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:7711-7715(1993).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), AND SEQUENCE REVISION TO 121.
RX PubMed=8061608; DOI=10.1002/pro.5560030508;
RA Lescar J., Souchon H., Alzari P.M.;
RT "Crystal structures of pheasant and guinea fowl egg-white lysozymes.";
RL Protein Sci. 3:788-798(1994).
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 -!- PTM: By an evolutionary shift in the site of proteolytic cleavage of
CC prelysozyme, Gly-18 became the N-terminal residue of the mature protein
CC instead of being the C-terminal residue of the signal sequence as in
CC other birds.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR PDB; 1GHL; X-ray; 2.10 A; A/B=18-147.
DR PDB; 1JHL; X-ray; 2.40 A; A=19-147.
DR PDBsum; 1GHL; -.
DR PDBsum; 1JHL; -.
DR AlphaFoldDB; P00702; -.
DR SMR; P00702; -.
DR CAZy; GH22; Glycoside Hydrolase Family 22.
DR PRIDE; P00702; -.
DR ABCD; P00702; 1 sequenced antibody.
DR EvolutionaryTrace; P00702; -.
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; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000269|PubMed:476049"
FT CHAIN 18..147
FT /note="Lysozyme C"
FT /id="PRO_0000018499"
FT DOMAIN 19..147
FT /note="C-type lysozyme"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT ACT_SITE 53
FT ACT_SITE 70
FT DISULFID 24..145
FT DISULFID 48..133
FT DISULFID 82..98
FT DISULFID 94..112
FT HELIX 23..32
FT /evidence="ECO:0007829|PDB:1GHL"
FT HELIX 43..54
FT /evidence="ECO:0007829|PDB:1GHL"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:1JHL"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:1GHL"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:1GHL"
FT TURN 72..75
FT /evidence="ECO:0007829|PDB:1GHL"
FT TURN 78..80
FT /evidence="ECO:0007829|PDB:1GHL"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:1GHL"
FT HELIX 98..102
FT /evidence="ECO:0007829|PDB:1GHL"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:1GHL"
FT HELIX 107..117
FT /evidence="ECO:0007829|PDB:1GHL"
FT TURN 118..121
FT /evidence="ECO:0007829|PDB:1GHL"
FT HELIX 122..125
FT /evidence="ECO:0007829|PDB:1GHL"
FT HELIX 127..132
FT /evidence="ECO:0007829|PDB:1GHL"
FT TURN 133..135
FT /evidence="ECO:0007829|PDB:1GHL"
FT HELIX 138..142
FT /evidence="ECO:0007829|PDB:1GHL"
SQ SEQUENCE 147 AA; 16166 MW; 7A0EF8CCFD6B8249 CRC64;
MRSLLILVLC FLPLAAPGKV YGRCELAAAM KRMGLDNYRG YSLGNWVCAA KFESNFNTGA
TNRNTDGSTD YGILQINSRW WCNDGRTPGS KNLCHIPCSA LLSSDITASV NCAKKIVSDG
NGMNAWVAWR KHCKGTDVNV WIRGCRL
