LYS_BOMMO
ID LYS_BOMMO Reviewed; 137 AA.
AC P48816; Q9TWL7;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 25-MAY-2022, entry version 128.
DE RecName: Full=Lysozyme;
DE EC=3.2.1.17;
DE AltName: Full=1,4-beta-N-acetylmuramidase;
DE Flags: Precursor;
OS Bombyx mori (Silk moth).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC Bombycidae; Bombycinae; Bombyx.
OX NCBI_TaxID=7091;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Fat body;
RX PubMed=7665079; DOI=10.1016/0378-1119(95)00199-g;
RA Lee W.J., Brey P.T.;
RT "Isolation and characterization of the lysozyme-encoding gene from the
RT silkworm Bombyx mori.";
RL Gene 161:199-203(1995).
RN [2]
RP PROTEIN SEQUENCE OF 19-38, AND FUNCTION.
RC STRAIN=NB18; TISSUE=Larval hemolymph;
RX PubMed=7876591; DOI=10.1006/jipa.1995.1003;
RA Abraham E.G., Nagaraju J., Salunke D., Gupta H.M., Datta R.K.;
RT "Purification and partial characterization of an induced antibacterial
RT protein in the silkworm, Bombyx mori.";
RL J. Invertebr. Pathol. 65:17-24(1995).
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. Active against E.coli
CC and M.luteus. {ECO:0000255|PROSITE-ProRule:PRU00680,
CC ECO:0000269|PubMed:7876591}.
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 -!- DEVELOPMENTAL STAGE: Expressed within 6 hours after induction, reaches
CC maximum levels after 48 hours and declines after 72 hours after
CC induction.
CC -!- INDUCTION: By bacterial infection.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 22 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00680}.
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DR EMBL; L37416; AAB40947.1; -; mRNA.
DR PIR; JC4233; JC4233.
DR RefSeq; NP_001037448.1; NM_001043983.1.
DR PDB; 1GD6; X-ray; 2.50 A; A=19-137.
DR PDB; 2RSC; NMR; -; A=19-137.
DR PDBsum; 1GD6; -.
DR PDBsum; 2RSC; -.
DR AlphaFoldDB; P48816; -.
DR BMRB; P48816; -.
DR SMR; P48816; -.
DR STRING; 7091.BGIBMGA010439-TA; -.
DR CAZy; GH22; Glycoside Hydrolase Family 22.
DR EnsemblMetazoa; BGIBMGA010439-RA; BGIBMGA010439-TA; BGIBMGA010439.
DR GeneID; 693015; -.
DR KEGG; bmor:693015; -.
DR CTD; 693015; -.
DR eggNOG; ENOG502S4CB; Eukaryota.
DR HOGENOM; CLU_111620_2_0_1; -.
DR InParanoid; P48816; -.
DR OMA; INSETYI; -.
DR OrthoDB; 1551203at2759; -.
DR EvolutionaryTrace; P48816; -.
DR Proteomes; UP000005204; Unassembled WGS sequence.
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 PANTHER; PTHR11407; PTHR11407; 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; Antibiotic; Antimicrobial; Bacteriolytic enzyme;
KW Direct protein sequencing; Disulfide bond; Glycosidase; Hydrolase;
KW Reference proteome; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000269|PubMed:7876591"
FT CHAIN 19..137
FT /note="Lysozyme"
FT /id="PRO_0000018505"
FT DOMAIN 19..137
FT /note="C-type lysozyme"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT ACT_SITE 50
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT ACT_SITE 67
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT DISULFID 24..137
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT DISULFID 45..127
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT DISULFID 79..93
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT DISULFID 89..107
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT HELIX 23..32
FT /evidence="ECO:0007829|PDB:1GD6"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:1GD6"
FT HELIX 40..50
FT /evidence="ECO:0007829|PDB:1GD6"
FT TURN 51..53
FT /evidence="ECO:0007829|PDB:1GD6"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:1GD6"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:1GD6"
FT TURN 69..72
FT /evidence="ECO:0007829|PDB:1GD6"
FT TURN 75..78
FT /evidence="ECO:0007829|PDB:1GD6"
FT STRAND 80..84
FT /evidence="ECO:0007829|PDB:1GD6"
FT TURN 87..90
FT /evidence="ECO:0007829|PDB:1GD6"
FT HELIX 93..96
FT /evidence="ECO:0007829|PDB:1GD6"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:1GD6"
FT HELIX 102..115
FT /evidence="ECO:0007829|PDB:1GD6"
FT HELIX 116..119
FT /evidence="ECO:0007829|PDB:1GD6"
FT HELIX 121..124
FT /evidence="ECO:0007829|PDB:1GD6"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:1GD6"
SQ SEQUENCE 137 AA; 15668 MW; FFE5710506C61A1D CRC64;
MQKLIIFALV VLCVGSEAKT FTRCGLVHEL RKHGFEENLM RNWVCLVEHE SSRDTSKTNT
NRNGSKDYGL FQINDRYWCS KGASPGKDCN VKCSDLLTDD ITKAAKCAKK IYKRHRFDAW
YGWKNHCQGS LPDISSC
