LYS5_CAEEL
ID LYS5_CAEEL Reviewed; 215 AA.
AC Q20967;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Lysozyme-like protein 5 {ECO:0000305};
DE Flags: Precursor;
GN Name=lys-5 {ECO:0000312|WormBase:F58B3.2};
GN ORFNames=F58B3.2 {ECO:0000312|WormBase:F58B3.2};
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=21931778; DOI=10.1371/journal.pone.0024619;
RA Boehnisch C., Wong D., Habig M., Isermann K., Michiels N.K., Roeder T.,
RA May R.C., Schulenburg H.;
RT "Protist-type lysozymes of the nematode Caenorhabditis elegans contribute
RT to resistance against pathogenic Bacillus thuringiensis.";
RL PLoS ONE 6:E24619-E24619(2011).
RN [3] {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).
CC -!- FUNCTION: Plays a role in resistance to Gram-positive bacteria S.aureus
CC or B.thuringiensis infection. {ECO:0000269|PubMed:21931778,
CC ECO:0000269|PubMed:24882217}.
CC -!- INDUCTION: Induced by Gram-positive bacterium S.aureus infection
CC (PubMed:24882217). Down-regulated by exposure to Gram-positive
CC bacterium B.thuringiensis spore toxins (PubMed:21931778).
CC {ECO:0000269|PubMed:21931778, ECO:0000269|PubMed:24882217}.
CC -!- DISRUPTION PHENOTYPE: Reduced survival in response to bacterium
CC B.thuringiensis infection (PubMed:21931778). Simultaneous RNAi-mediated
CC knockdown of ilys-2 results in a reduction in survival following
CC bacterium S.aureus infection. {ECO:0000269|PubMed:21931778,
CC ECO:0000269|PubMed:24882217}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 25 family.
CC {ECO:0000255|PROSITE-ProRule:PRU01252, ECO:0000305}.
CC -!- CAUTION: Lacks conserved active site residues, suggesting it has no
CC catalytic activity. {ECO:0000305}.
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DR EMBL; BX284604; CAA97800.1; -; Genomic_DNA.
DR PIR; T22895; T22895.
DR RefSeq; NP_502193.1; NM_069792.4.
DR AlphaFoldDB; Q20967; -.
DR SMR; Q20967; -.
DR STRING; 6239.F58B3.2; -.
DR PaxDb; Q20967; -.
DR PeptideAtlas; Q20967; -.
DR EnsemblMetazoa; F58B3.2.1; F58B3.2.1; WBGene00003094.
DR GeneID; 186491; -.
DR KEGG; cel:CELE_F58B3.2; -.
DR UCSC; F58B3.2; c. elegans.
DR CTD; 186491; -.
DR WormBase; F58B3.2; CE06004; WBGene00003094; lys-5.
DR eggNOG; ENOG502S5CG; Eukaryota.
DR GeneTree; ENSGT00970000195882; -.
DR HOGENOM; CLU_073372_3_0_1; -.
DR InParanoid; Q20967; -.
DR OMA; HFFITIL; -.
DR OrthoDB; 1437716at2759; -.
DR PhylomeDB; Q20967; -.
DR PRO; PR:Q20967; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00003094; Expressed in adult organism and 1 other tissue.
DR GO; GO:0003796; F:lysozyme activity; IEA:InterPro.
DR GO; GO:0016998; P:cell wall macromolecule catabolic process; IEA:InterPro.
DR GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IMP:WormBase.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR InterPro; IPR002053; Glyco_hydro_25.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF01183; Glyco_hydro_25; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS51904; GLYCOSYL_HYDROL_F25_2; 1.
PE 2: Evidence at transcript level;
KW Antimicrobial; Bacteriolytic enzyme; Glycosidase; Hydrolase; Immunity;
KW Innate immunity; Reference proteome; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..215
FT /note="Lysozyme-like protein 5"
FT /evidence="ECO:0000255"
FT /id="PRO_5004199032"
FT DOMAIN 18..215
FT /note="Ch-type lysozyme"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01252"
FT ACT_SITE 23
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01252"
FT ACT_SITE 113
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01252"
FT ACT_SITE 115
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01252"
SQ SEQUENCE 215 AA; 23529 MW; 026249629A61DD7C CRC64;
MKHFFITILL FCSVVSAARN GIDINSPVST STFTCIKNAG FSFIIPRIYH SSGSVDTVGV
QNVKNARAAG LTDVDGYIFP CLKSTCASAA NQVKASLDAV KAAGTKISTL WLDIERLNWP
ADHASNRAFI EAMVSEAKAY GQQVGIYSNY YNWQDIVGLD YHGQSSLMLW WPAYDGVKDF
SKYAPFGGWS KPTIHQWSDT TTGPCGVSVD MNYIP
