ILYS2_CAEEL
ID ILYS2_CAEEL Reviewed; 139 AA.
AC O76358;
DT 07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Invertebrate-type lysozyme 2 {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-2 {ECO:0000312|WormBase:C45G7.2};
GN ORFNames=C45G7.2 {ECO:0000312|WormBase:C45G7.2};
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 FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24882217; DOI=10.1016/j.immuni.2014.05.002;
RA Visvikis O., Ihuegbu N., Labed S.A., Luhachack L.G., Alves A.M.,
RA Wollenberg A.C., Stuart L.M., Stormo G.D., Irazoqui J.E.;
RT "Innate host defense requires TFEB-mediated transcription of cytoprotective
RT and antimicrobial genes.";
RL Immunity 40:896-909(2014).
RN [3] {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 (By
CC similarity). May play a role in resistance to Gram-positive bacterium
CC S.aureus infection (PubMed:24882217). {ECO:0000250|UniProtKB:O76357,
CC ECO:0000269|PubMed:24882217}.
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 muscle cell pm3, nerve ring
CC 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 (PubMed:27525822). Induced by Gram-positive bacterium
CC S.aureus infection (PubMed:24882217). {ECO:0000269|PubMed:24882217,
CC ECO:0000269|PubMed:27525822}.
CC -!- DISRUPTION PHENOTYPE: Simultaneous RNAi-mediated knockdown of lys-5
CC results in a reduction in survival following S.aureus infection.
CC {ECO:0000269|PubMed:24882217}.
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; CCD65530.1; -; Genomic_DNA.
DR PIR; T33138; T33138.
DR RefSeq; NP_500207.1; NM_067806.1.
DR AlphaFoldDB; O76358; -.
DR SMR; O76358; -.
DR STRING; 6239.C45G7.2; -.
DR CAZy; GH22; Glycoside Hydrolase Family 22.
DR MEROPS; S81.001; -.
DR PaxDb; O76358; -.
DR PeptideAtlas; O76358; -.
DR EnsemblMetazoa; C45G7.2.1; C45G7.2.1; WBGene00016669.
DR GeneID; 183475; -.
DR KEGG; cel:CELE_C45G7.2; -.
DR UCSC; C45G7.2; c. elegans.
DR CTD; 183475; -.
DR WormBase; C45G7.2; CE17549; WBGene00016669; ilys-2.
DR eggNOG; ENOG502SAEY; Eukaryota.
DR GeneTree; ENSGT00940000166559; -.
DR HOGENOM; CLU_130604_1_0_1; -.
DR InParanoid; O76358; -.
DR OMA; VKYGQDC; -.
DR OrthoDB; 1343143at2759; -.
DR PhylomeDB; O76358; -.
DR PRO; PR:O76358; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00016669; Expressed in adult organism and 1 other tissue.
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; IGI:WormBase.
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..139
FT /note="Invertebrate-type lysozyme 2"
FT /evidence="ECO:0000255"
FT /id="PRO_5004159765"
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 23..138
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 139 AA; 15074 MW; 77BB60112EE1C384 CRC64;
MFVKAILLLS IAVAYASADC LHCICMRESG CKPIGCHMDV GSLSCGYYQI KIPYYEDCGQ
PGKKHGESTE VAWKRCADDL KCATNCVENY YNRYKHECAG TGQGACEVMA RNHNGGPRGC
HASGTLGYWK GVHSCCGCS
