ILYS6_CAEEL
ID ILYS6_CAEEL Reviewed; 138 AA.
AC O02119;
DT 07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 3.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Invertebrate-type lysozyme 6 {ECO:0000305};
DE EC=3.2.1.17 {ECO:0000250|UniProtKB:O76357};
DE AltName: Full=1,4-beta-N-acetylmuramidase {ECO:0000305};
DE Flags: Precursor;
GN Name=ilys-6 {ECO:0000312|WormBase:W03D2.7};
GN ORFNames=W03D2.7 {ECO:0000312|WormBase:W03D2.7};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=27525822; DOI=10.1371/journal.ppat.1005826;
RA Gravato-Nobre M.J., Vaz F., Filipe S., Chalmers R., Hodgkin J.;
RT "The invertebrate lysozyme effector ILYS-3 is systemically activated in
RT response to danger signals and confers antimicrobial protection in C.
RT elegans.";
RL PLoS Pathog. 12:E1005826-E1005826(2016).
CC -!- FUNCTION: Has bacteriolytic activity against Gram-positive bacteria.
CC {ECO:0000250|UniProtKB:O76357}.
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:0000250|UniProtKB:O76357};
CC -!- TISSUE SPECIFICITY: Expressed in pharyngeal gland cells and duct
CC projections, coelomocytes and intestine. {ECO:0000269|PubMed:27525822}.
CC -!- INDUCTION: Induced by Gram-positive bacterium M.nematophilum CBX102
CC infection but not by Gram-negative bacterium P.aeruginosa PAO1
CC infection. {ECO:0000269|PubMed:27525822}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 22 family. Type-I
CC lysozyme subfamily. {ECO:0000255|PROSITE-ProRule:PRU01257}.
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DR EMBL; BX284604; CCD66766.1; -; Genomic_DNA.
DR RefSeq; NP_500470.2; NM_068069.2.
DR AlphaFoldDB; O02119; -.
DR SMR; O02119; -.
DR STRING; 6239.W03D2.7; -.
DR CAZy; GH22; Glycoside Hydrolase Family 22.
DR MEROPS; S81.001; -.
DR PaxDb; O02119; -.
DR PeptideAtlas; O02119; -.
DR EnsemblMetazoa; W03D2.7.1; W03D2.7.1; WBGene00020982.
DR GeneID; 177164; -.
DR KEGG; cel:CELE_W03D2.7; -.
DR UCSC; W03D2.7; c. elegans.
DR CTD; 177164; -.
DR WormBase; W03D2.7; CE44604; WBGene00020982; ilys-6.
DR eggNOG; ENOG502SAEY; Eukaryota.
DR GeneTree; ENSGT00940000166559; -.
DR HOGENOM; CLU_130604_1_0_1; -.
DR InParanoid; O02119; -.
DR OMA; CINCICY; -.
DR OrthoDB; 1343143at2759; -.
DR PhylomeDB; O02119; -.
DR PRO; PR:O02119; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00020982; Expressed in embryo.
DR GO; GO:0003796; F:lysozyme activity; IBA:GO_Central.
DR GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IBA:GO_Central.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR CDD; cd16890; lyz_i; 1.
DR InterPro; IPR008597; Invert_lysozyme.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR PANTHER; PTHR11195; PTHR11195; 1.
DR Pfam; PF05497; Destabilase; 1.
DR SUPFAM; SSF53955; SSF53955; 1.
DR PROSITE; PS51909; LYSOZYME_I; 1.
PE 2: Evidence at transcript level;
KW Antibiotic; Antimicrobial; Bacteriolytic enzyme; Disulfide bond;
KW Glycosidase; Hydrolase; Reference proteome; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..138
FT /note="Invertebrate-type lysozyme 6"
FT /evidence="ECO:0000255"
FT /id="PRO_5004156808"
FT DOMAIN 19..138
FT /note="I-type lysozyme"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01257"
FT ACT_SITE 28
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01257"
FT ACT_SITE 39
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01257"
FT BINDING 51..57
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8IU26"
FT BINDING 90
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8IU26"
FT BINDING 113..115
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8IU26"
FT DISULFID 20..106
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01257"
FT DISULFID 25..31
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01257"
FT DISULFID 36..45
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01257"
FT DISULFID 58..86
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01257"
FT DISULFID 76..82
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01257"
FT DISULFID 98..120
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01257"
SQ SEQUENCE 138 AA; 14938 MW; 8691FCC01E8B2CE8 CRC64;
MFVKLCGILA FAVTYASSDC LQCICKKESE CKPVGCNDDV GSLSCGYYQI KLSYYKDCGQ
PGKRAGESVE AAWRRCSDEL DCASTCVQSY YNRYKKQCAG TGQGACEIMA RNHNGGPRGC
KKSATLGYWN GIKGLGCS
