ID   LYSC_AMYCA              Reviewed;         130 AA.
AC   P85345;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   25-MAY-2022, entry version 45.
DE   RecName: Full=Lysozyme C;
DE            EC=3.2.1.17;
DE   AltName: Full=1,4-beta-N-acetylmuramidase C;
DE   AltName: Full=Asiatic softshell turtle lysozyme C;
DE            Short=ASTL;
GN   Name=LYZ {ECO:0000250|UniProtKB:P00702};
OS   Amyda cartilaginea (Asiatic softshell turtle).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Testudinata; Testudines; Cryptodira; Trionychia;
OC   Trionychidae; Amyda.
OX   NCBI_TaxID=161655;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL
RP   PROPERTIES.
RC   TISSUE=Egg white;
RX   PubMed=16549391; DOI=10.1016/j.cbpc.2006.02.004;
RA   Thammasirirak S., Ponkham P., Preecharram S., Khanchanuan R.,
RA   Phonyothee P., Daduang S., Srisomsap C., Araki T., Svasti J.;
RT   "Purification, characterization and comparison of reptile lysozymes.";
RL   Comp. Biochem. Physiol. 143:209-217(2006).
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. Has strong
CC       bacteriolytic activity against M.luteus and V.cholerae, weak
CC       bacteriolytic activity against P.aeruginosa and no activity against
CC       A.hydrophila. {ECO:0000255|PROSITE-ProRule:PRU00680,
CC       ECO:0000269|PubMed:16549391}.
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; Evidence={ECO:0000269|PubMed:16549391};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 6.0. {ECO:0000269|PubMed:16549391};
CC       Temperature dependence:
CC         Optimum temperature is 40 degrees Celsius. Retains the bulk of its
CC         activity after incubation for 1 hour at 90 degrees Celsius.
CC         {ECO:0000269|PubMed:16549391};
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P00702}.
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. {ECO:0000305}.
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   AlphaFoldDB; P85345; -.
DR   SMR; P85345; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0003796; F:lysozyme activity; IDA:UniProtKB.
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   Antimicrobial; Bacteriolytic enzyme; Direct protein sequencing;
KW   Disulfide bond; Glycosidase; Hydrolase; Secreted.
FT   CHAIN           1..130
FT                   /note="Lysozyme C"
FT                   /id="PRO_0000315890"
FT   DOMAIN          1..130
FT                   /note="C-type lysozyme"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT   ACT_SITE        35
FT                   /evidence="ECO:0000250|UniProtKB:P00702,
FT                   ECO:0000255|PROSITE-ProRule:PRU00680"
FT   ACT_SITE        53
FT                   /evidence="ECO:0000250|UniProtKB:P00702,
FT                   ECO:0000255|PROSITE-ProRule:PRU00680"
FT   DISULFID        6..128
FT                   /evidence="ECO:0000250|UniProtKB:P00702,
FT                   ECO:0000255|PROSITE-ProRule:PRU00680"
FT   DISULFID        30..116
FT                   /evidence="ECO:0000250|UniProtKB:P00702,
FT                   ECO:0000255|PROSITE-ProRule:PRU00680"
FT   DISULFID        65..81
FT                   /evidence="ECO:0000250|UniProtKB:P00702,
FT                   ECO:0000255|PROSITE-ProRule:PRU00680"
FT   DISULFID        77..95
FT                   /evidence="ECO:0000250|UniProtKB:P00702,
FT                   ECO:0000255|PROSITE-ProRule:PRU00680"
SQ   SEQUENCE   130 AA;  14543 MW;  F6760A314D34FF91 CRC64;
     KIYEQCEAAR EMKRLGLDGY DGYSLGDWVC TAKHESNFNT GATNYNRGDQ STDYGIFQIN
     SRWWCNDGKT PNAKNACGIE CSELLKADIT AAVICAKRVV RDPNGMGAWV AWTKYCKGKD
     VSQWIKGCKL