ID LYS_MERLU Reviewed; 122 AA. AC P86383; DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot. DT 24-NOV-2009, sequence version 1. DT 03-MAY-2023, entry version 44. DE RecName: Full=Lysozyme {ECO:0000303|PubMed:24200802}; DE EC=3.2.1.17 {ECO:0000269|PubMed:24200802}; DE AltName: Full=1,4-beta-N-acetylmuramidase {ECO:0000250|UniProtKB:P83673}; DE AltName: Full=Invertebrate-type lysozyme {ECO:0000305}; OS Meretrix lusoria (Hard clam) (Common Orient clam). OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia; OC Autobranchia; Heteroconchia; Euheterodonta; Imparidentia; Neoheterodontei; OC Venerida; Veneroidea; Veneridae; Meretrix. OX NCBI_TaxID=74491; RN [1] RP PROTEIN SEQUENCE (ISOZYMES A AND B), IDENTIFICATION BY MASS SPECTROMETRY, RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=24200802; DOI=10.1271/bbb.130534; RA Kuwano Y., Yoneda K., Kawaguchi Y., Araki N., Araki T.; RT "The complete amino acid sequence and enzymatic properties of an i-type RT lysozyme isolated from the common orient clam (Meretrix lusoria)."; RL Biosci. Biotechnol. Biochem. 77:2269-2277(2013). RN [2] {ECO:0007744|PDB:3AYQ} RP X-RAY CRYSTALLOGRAPHY (1.77 ANGSTROMS) IN COMPLEX WITH INHIBITOR, AND RP DISULFIDE BONDS. RA Yoneda K., Kuwano Y., Usui T., Ogata M., Suzuki A., Araki T.; RT "Crystal structure of inhibitor bound lysozyme from Meretrix lusoria."; RL Submitted (MAY-2011) to the PDB data bank. RN [3] {ECO:0007744|PDB:3AB6} RP X-RAY CRYSTALLOGRAPHY (1.78 ANGSTROMS) IN COMPLEX WITH SUBSTRATE (ISOZYME RP B), AND DISULFIDE BONDS. RX PubMed=24192349; DOI=10.1107/s1744309113028170; RA Kuwano Y., Yoneda K., Kawaguchi Y., Araki T.; RT "The tertiary structure of an i-type lysozyme isolated from the common RT orient clam (Meretrix lusoria)."; RL Acta Crystallogr. F 69:1202-1206(2013). RN [4] {ECO:0007744|PDB:4PJ2} RP X-RAY CRYSTALLOGRAPHY (1.24 ANGSTROMS) IN COMPLEX WITH INHIBITOR. RX PubMed=25664745; DOI=10.1107/s1399004714025863; RA Leysen S., Van Herreweghe J.M., Yoneda K., Ogata M., Usui T., Araki T., RA Michiels C.W., Strelkov S.V.; RT "The structure of the proteinaceous inhibitor PliI from Aeromonas RT hydrophila in complex with its target lysozyme."; RL Acta Crystallogr. D 71:344-351(2015). CC -!- FUNCTION: Has bacteriolytic activity against Gram-positive bacteria CC M.luteus. Also has chitinase activity. {ECO:0000269|PubMed:24200802}. 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:24200802}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC pH dependence: CC Optimum pH is 6.5 at 37 degrees Celsius for bacteriolytic activity. CC Optimum pH is 3 at 40 degrees Celsius for chitinase activity. CC {ECO:0000269|PubMed:24200802}; CC -!- SUBUNIT: Monomer. {ECO:0000303|PubMed:24200802}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P83673}. CC -!- MASS SPECTROMETRY: Mass=13376; Method=MALDI; CC Evidence={ECO:0000269|PubMed:24200802}; CC -!- MISCELLANEOUS: Unlike Ruditapes philippinarum lysozyme, catalytic CC activity is not affected by variation in salt concentrations. CC {ECO:0000269|PubMed:24200802}. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 22 family. Type-I CC lysozyme subfamily. {ECO:0000255|PROSITE-ProRule:PRU01257}. 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; 3AB6; X-ray; 1.78 A; A=1-122. DR PDB; 3AYQ; X-ray; 1.77 A; A=1-122. DR PDB; 4PJ2; X-ray; 1.24 A; C/D=1-122. DR PDBsum; 3AB6; -. DR PDBsum; 3AYQ; -. DR PDBsum; 4PJ2; -. DR AlphaFoldDB; P86383; -. DR SMR; P86383; -. DR CAZy; GH22; Glycoside Hydrolase Family 22. DR BRENDA; 3.2.1.17; 3231. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0004568; F:chitinase activity; IDA:UniProtKB. DR GO; GO:0003796; F:lysozyme activity; IDA:UniProtKB. DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW. DR GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW. DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW. DR CDD; cd16890; lyz_i; 1. DR Gene3D; 1.10.530.10; -; 1. DR InterPro; IPR008597; Invert_lysozyme. DR InterPro; IPR023346; Lysozyme-like_dom_sf. DR PANTHER; PTHR11195; DESTABILASE-RELATED; 1. DR PANTHER; PTHR11195:SF13; INVERTEBRATE-TYPE LYSOZYME 2-RELATED; 1. DR Pfam; PF05497; Destabilase; 1. DR SUPFAM; SSF53955; Lysozyme-like; 1. DR PROSITE; PS51909; LYSOZYME_I; 1. PE 1: Evidence at protein level; KW 3D-structure; Antibiotic; Antimicrobial; Bacteriolytic enzyme; KW Direct protein sequencing; Disulfide bond; Glycosidase; Hydrolase; KW Secreted. FT CHAIN 1..122 FT /note="Lysozyme" FT /id="PRO_0000389530" FT DOMAIN 3..118 FT /note="I-type lysozyme" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01257" FT ACT_SITE 18 FT /note="Proton donor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01257" FT ACT_SITE 29 FT /note="Nucleophile" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01257" FT BINDING 41..47 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:24192349, ECO:0000305|Ref.2, FT ECO:0007744|PDB:3AB6, ECO:0007744|PDB:3AYQ" FT BINDING 72 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:24192349, ECO:0000305|Ref.2, FT ECO:0007744|PDB:3AB6, ECO:0007744|PDB:3AYQ" FT BINDING 93..95 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:Q8IU26" FT BINDING 93 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:24192349, ECO:0000305|Ref.2, FT ECO:0007744|PDB:3AB6, ECO:0007744|PDB:3AYQ" FT BINDING 102 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:24192349, ECO:0000305|Ref.2, FT ECO:0007744|PDB:3AB6, ECO:0007744|PDB:3AYQ" FT DISULFID 10..86 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01257, FT ECO:0000269|PubMed:24192349, ECO:0000269|Ref.2, FT ECO:0007744|PDB:3AB6, ECO:0007744|PDB:3AYQ" FT DISULFID 13..118 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01257, FT ECO:0000269|PubMed:24192349, ECO:0000269|Ref.2, FT ECO:0007744|PDB:3AB6, ECO:0007744|PDB:3AYQ" FT DISULFID 15..21 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01257, FT ECO:0000269|PubMed:24192349, ECO:0000269|Ref.2, FT ECO:0007744|PDB:3AB6, ECO:0007744|PDB:3AYQ" FT DISULFID 26..35 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01257, FT ECO:0000269|PubMed:24192349, ECO:0000269|Ref.2, FT ECO:0007744|PDB:3AB6, ECO:0007744|PDB:3AYQ" FT DISULFID 48..68 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01257, FT ECO:0000269|PubMed:24192349, ECO:0000269|Ref.2, FT ECO:0007744|PDB:3AB6, ECO:0007744|PDB:3AYQ" FT DISULFID 58..64 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01257, FT ECO:0000269|PubMed:24192349, ECO:0000269|Ref.2, FT ECO:0007744|PDB:3AB6, ECO:0007744|PDB:3AYQ" FT DISULFID 82..100 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01257, FT ECO:0000269|PubMed:24192349, ECO:0000269|Ref.2, FT ECO:0007744|PDB:3AB6, ECO:0007744|PDB:3AYQ" FT VARIANT 5 FT /note="I -> T (in isozyme B)" FT /evidence="ECO:0000269|PubMed:24200802" FT STRAND 4..6 FT /evidence="ECO:0007829|PDB:4PJ2" FT HELIX 8..19 FT /evidence="ECO:0007829|PDB:4PJ2" FT STRAND 20..22 FT /evidence="ECO:0007829|PDB:4PJ2" FT STRAND 29..32 FT /evidence="ECO:0007829|PDB:4PJ2" FT TURN 36..39 FT /evidence="ECO:0007829|PDB:4PJ2" FT HELIX 42..47 FT /evidence="ECO:0007829|PDB:4PJ2" FT STRAND 52..54 FT /evidence="ECO:0007829|PDB:4PJ2" FT HELIX 55..59 FT /evidence="ECO:0007829|PDB:4PJ2" FT HELIX 62..76 FT /evidence="ECO:0007829|PDB:4PJ2" FT HELIX 78..80 FT /evidence="ECO:0007829|PDB:4PJ2" FT HELIX 86..95 FT /evidence="ECO:0007829|PDB:4PJ2" FT HELIX 99..101 FT /evidence="ECO:0007829|PDB:4PJ2" FT HELIX 103..105 FT /evidence="ECO:0007829|PDB:4PJ2" FT HELIX 106..112 FT /evidence="ECO:0007829|PDB:4PJ2" SQ SEQUENCE 122 AA; 13377 MW; 92366099E8AD7881 CRC64; FAGGIVSQRC LSCICKMESG CRNVGCKMDM GSLSCGYFQI KEAYWIDCGR PGSSWKSCAA SSYCASLCVQ NYMKRYAKWA GCPLRCEGFA REHNGGPRGC KKGSTIGYWN RLQKISGCHG VQ //