LYS1_MUSDO
ID LYS1_MUSDO Reviewed; 141 AA.
AC Q7YT16; Q7M437;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 25-MAY-2022, entry version 81.
DE RecName: Full=Lysozyme 1;
DE EC=3.2.1.17;
DE AltName: Full=1,4-beta-N-acetylmuramidase 1;
DE Flags: Precursor;
OS Musca domestica (House fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Muscoidea;
OC Muscidae; Musca.
OX NCBI_TaxID=7370;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Midgut epithelium;
RA Chimoy P., Marana S.R., Ferreira C., Terra W.R.;
RT "Cloning, sequencing and characterization of a digestive lysozyme from
RT Musca domestica midgut.";
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 20-141.
RC TISSUE=Larva;
RX PubMed=8690715; DOI=10.1093/oxfordjournals.jbchem.a124943;
RA Ito Y., Nakamura M., Hotani T., Imoto T.;
RT "Insect lysozyme from house fly (Musca domestica) larvae: possible
RT digestive function based on sequence and enzymatic properties.";
RL J. Biochem. 118:546-551(1995).
CC -!- FUNCTION: May not function as a self-defense protein, but as a
CC digestive enzyme, probably in the gut of the insect body. Inactive
CC towards Micrococcus luteus. Active toward glycol chitin.
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Active at acidic pHs. Inactive above pH 7.;
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 22 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00680}.
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DR EMBL; AY344589; AAQ20048.1; -; mRNA.
DR PIR; PC4062; PC4062.
DR RefSeq; NP_001295901.1; NM_001308972.1.
DR RefSeq; XP_005185827.1; XM_005185770.3.
DR RefSeq; XP_019891658.1; XM_020036099.1.
DR RefSeq; XP_019893140.1; XM_020037581.1.
DR RefSeq; XP_019893141.1; XM_020037582.1.
DR PDB; 2FBD; X-ray; 1.90 A; A/B=20-141.
DR PDB; 2H5Z; X-ray; 1.92 A; A/B=20-141.
DR PDBsum; 2FBD; -.
DR PDBsum; 2H5Z; -.
DR AlphaFoldDB; Q7YT16; -.
DR SMR; Q7YT16; -.
DR STRING; 7370.XP_005181668.1; -.
DR CAZy; GH22; Glycoside Hydrolase Family 22.
DR GeneID; 101892974; -.
DR GeneID; 101893151; -.
DR GeneID; 101895951; -.
DR KEGG; mde:101892974; -.
DR KEGG; mde:101893151; -.
DR KEGG; mde:101895951; -.
DR VEuPathDB; VectorBase:MDOA012752; -.
DR VEuPathDB; VectorBase:MDOA012964; -.
DR VEuPathDB; VectorBase:MDOA013199; -.
DR eggNOG; ENOG502S1S1; Eukaryota.
DR BRENDA; 3.2.1.17; 3486.
DR EvolutionaryTrace; Q7YT16; -.
DR Proteomes; UP000095301; Unplaced.
DR GO; GO:0003796; F:lysozyme activity; IEA:UniProtKB-EC.
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; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Glycosidase; Hydrolase; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:8690715"
FT CHAIN 20..141
FT /note="Lysozyme 1"
FT /id="PRO_0000018508"
FT DOMAIN 20..141
FT /note="C-type lysozyme"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT ACT_SITE 51
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT ACT_SITE 69
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT CARBOHYD 65
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 25..140
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT DISULFID 46..130
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT DISULFID 81..97
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT DISULFID 93..111
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT HELIX 24..33
FT /evidence="ECO:0007829|PDB:2FBD"
FT HELIX 38..40
FT /evidence="ECO:0007829|PDB:2FBD"
FT HELIX 41..52
FT /evidence="ECO:0007829|PDB:2FBD"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:2FBD"
FT TURN 71..74
FT /evidence="ECO:0007829|PDB:2FBD"
FT TURN 77..80
FT /evidence="ECO:0007829|PDB:2FBD"
FT HELIX 97..101
FT /evidence="ECO:0007829|PDB:2FBD"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:2FBD"
FT HELIX 106..119
FT /evidence="ECO:0007829|PDB:2FBD"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:2FBD"
FT HELIX 127..130
FT /evidence="ECO:0007829|PDB:2FBD"
FT HELIX 138..140
FT /evidence="ECO:0007829|PDB:2FBD"
SQ SEQUENCE 141 AA; 15733 MW; C640C6407AD80F0E CRC64;
MKFFIVLVAA LALAAPAMGK TFTRCSLARE MYALGVPKSE LPQWTCIAEH ESSYRTNVVG
PTNSNGSNDY GIFQINNYYW CQPSNGRFSY NECHLSCDAL LTDNISNSVT CARKIKSQQG
WTAWSTWKYC SGSLPSINDC F
