LYS_ASTRU
ID LYS_ASTRU Reviewed; 25 AA.
AC P37715;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 02-DEC-2020, entry version 50.
DE RecName: Full=Lysozyme;
DE EC=3.2.1.17;
DE AltName: Full=1,4-beta-N-acetylmuramidase;
DE Flags: Fragment;
OS Asterias rubens (Common European starfish) (Asterias vulgaris).
OC Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Asterozoa; Asteroidea;
OC Forcipulatacea; Forcipulatida; Asteriidae; Asterias.
OX NCBI_TaxID=7604;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=1149747; DOI=10.1111/j.1432-1033.1975.tb04108.x;
RA Jolles J., Jolles P.;
RT "The losozyme from Asterias rubens.";
RL Eur. J. Biochem. 54:19-23(1975).
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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 22 family. Type-I
CC lysozyme subfamily. {ECO:0000255|PROSITE-ProRule:PRU01257}.
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DR PIR; A11762; A11762.
DR CAZy; GH22; Glycoside Hydrolase Family 22.
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; IPR008597; Invert_lysozyme.
DR PROSITE; PS51909; LYSOZYME_I; 1.
PE 1: Evidence at protein level;
KW Antimicrobial; Bacteriolytic enzyme; Direct protein sequencing;
KW Glycosidase; Hydrolase.
FT CHAIN 1..>25
FT /note="Lysozyme"
FT /id="PRO_0000208877"
FT DOMAIN 1..>25
FT /note="I-type lysozyme"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01257"
FT NON_TER 25
SQ SEQUENCE 25 AA; 2569 MW; 6FA1D6BE87C5BE18 CRC64;
SGPVPSGCLR CICVVESGXR MPNPV