LYSC_PELSI
ID LYSC_PELSI Reviewed; 131 AA.
AC Q7LZQ1;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 3.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=Lysozyme C;
DE EC=3.2.1.17;
DE AltName: Full=1,4-beta-N-acetylmuramidase C;
DE AltName: Full=Softshell turtle lysozyme C;
DE Short=SSTL;
GN Name=LYZ;
OS Pelodiscus sinensis (Chinese softshell turtle) (Trionyx sinensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Trionychia;
OC Trionychidae; Pelodiscus.
OX NCBI_TaxID=13735;
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).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RC TISSUE=Egg white;
RX PubMed=19029145; DOI=10.1093/jb/mvn156;
RA Siritapetawee J., Thammasirirak S., Robinson R.C., Yuvaniyama J.;
RT "The 1.9 A X-ray structure of egg-white lysozyme from Taiwanese soft-
RT shelled turtle (Trionyx Sinensis Wiegmann) exhibits structural differences
RT from the standard chicken-type lysozyme.";
RL J. Biochem. 145:193-198(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. 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. Activity rapidly decreases
CC within 30 minutes of incubation at 90 degrees Celsius.
CC {ECO:0000269|PubMed:16549391};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
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; JC5493; JC5493.
DR PDB; 2GV0; X-ray; 1.90 A; A=1-131.
DR PDBsum; 2GV0; -.
DR AlphaFoldDB; Q7LZQ1; -.
DR SMR; Q7LZQ1; -.
DR STRING; 13735.ENSPSIP00000018209; -.
DR CAZy; GH22; Glycoside Hydrolase Family 22.
DR eggNOG; ENOG502RZU4; Eukaryota.
DR HOGENOM; CLU_111620_0_1_1; -.
DR BRENDA; 3.2.1.17; 6494.
DR EvolutionaryTrace; Q7LZQ1; -.
DR Proteomes; UP000007267; Unassembled WGS sequence.
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 Reference proteome; Secreted.
FT CHAIN 1..131
FT /note="Lysozyme C"
FT /id="PRO_0000208876"
FT DOMAIN 2..131
FT /note="C-type lysozyme"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT ACT_SITE 36
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT ACT_SITE 54
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT DISULFID 7..129
FT DISULFID 31..117
FT DISULFID 66..82
FT DISULFID 78..96
FT HELIX 6..15
FT /evidence="ECO:0007829|PDB:2GV0"
FT HELIX 21..23
FT /evidence="ECO:0007829|PDB:2GV0"
FT HELIX 26..37
FT /evidence="ECO:0007829|PDB:2GV0"
FT STRAND 44..47
FT /evidence="ECO:0007829|PDB:2GV0"
FT TURN 48..51
FT /evidence="ECO:0007829|PDB:2GV0"
FT STRAND 52..55
FT /evidence="ECO:0007829|PDB:2GV0"
FT TURN 56..59
FT /evidence="ECO:0007829|PDB:2GV0"
FT TURN 62..65
FT /evidence="ECO:0007829|PDB:2GV0"
FT HELIX 82..86
FT /evidence="ECO:0007829|PDB:2GV0"
FT HELIX 91..102
FT /evidence="ECO:0007829|PDB:2GV0"
FT HELIX 106..109
FT /evidence="ECO:0007829|PDB:2GV0"
FT HELIX 111..116
FT /evidence="ECO:0007829|PDB:2GV0"
FT TURN 117..119
FT /evidence="ECO:0007829|PDB:2GV0"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:2GV0"
FT TURN 126..128
FT /evidence="ECO:0007829|PDB:2GV0"
SQ SEQUENCE 131 AA; 14732 MW; D59A7791775E6AA1 CRC64;
GKIYEQCELA REFKRHGMDG YHGYSLGDWV CTAKHESNFN TAATNYNRGD QSTDYGILQI
NSRWWCNDGK TPKAKNACGI ECSELLKADI TAAVNCAKRI VRDPNGMGAW VAWTKYCKGK
DVSQWIKGCK L
