LYSC_PENME
ID LYSC_PENME Reviewed; 158 AA.
AC C1IIX1;
DT 12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 37.
DE RecName: Full=Lysozyme C {ECO:0000255|PROSITE-ProRule:PRU00680, ECO:0000303|PubMed:18798009, ECO:0000312|EMBL:ACD76101.1};
DE EC=3.2.1.17 {ECO:0000255|PROSITE-ProRule:PRU00680, ECO:0000312|EMBL:ACD76101.1};
DE AltName: Full=1,4-beta-N-acetylmuramidase C {ECO:0000255|PROSITE-ProRule:PRU00680};
DE Flags: Precursor;
OS Penaeus merguiensis (Banana prawn) (Fenneropenaeus merguiensis).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC Malacostraca; Eumalacostraca; Eucarida; Decapoda; Dendrobranchiata;
OC Penaeoidea; Penaeidae; Penaeus.
OX NCBI_TaxID=71412 {ECO:0000312|EMBL:ACD76101.1};
RN [1] {ECO:0000312|EMBL:ACD76101.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, INDUCTION, AND
RP PHYLOGENETIC ANALYSIS.
RX PubMed=18798009; DOI=10.1007/s11033-008-9355-8;
RA Mai W.J., Hu C.Q.;
RT "Molecular cloning, characterization, expression and antibacterial analysis
RT of a lysozyme homologue from Fenneropenaeus merguiensis.";
RL Mol. Biol. Rep. 36:1587-1595(2009).
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 (By similarity). Has
CC bacteriolytic activity against Gram-positive bacterium M.luteus, and
CC Gram-negative shrimp pathogenic bacteria V.alginolyticus,
CC V.parahaemolyticus and V.vulnificus. May play a role in host defense
CC (PubMed:18798009). {ECO:0000255|PROSITE-ProRule:PRU00680,
CC ECO:0000269|PubMed:18798009}.
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:0000255|PROSITE-ProRule:PRU00680};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P08905}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P85045}.
CC -!- TISSUE SPECIFICITY: Strongly expressed in gill and gonad, and
CC marginally detectable in hemolymph and lymphoid organ. Not expressed in
CC kidney, hepatopancreas or tail muscle. {ECO:0000269|PubMed:18798009}.
CC -!- INDUCTION: (Microbial infection) Expression is up-regulated in response
CC to heat-killed V.alginolyticus injection in kidney, hepatopancreas and
CC muscle, with the strongest up-regulation in hemolymph, gill, gonad and
CC lymphoid organ. After M.luteus challenge there is an increase in
CC expression level at 2 (11.3-fold) and 6 hours (18.3-fold)
CC postinjection, with the maximum level at 8 hours (25.4-fold), and then
CC lowering down to the original level at 16 hours postinjection. After
CC V.alginolyticus challenge there is significant increase in expression
CC level at 4, 6 and 8 hours postinjection, with the maximum level at 16
CC hours (15.7-fold), and then down-regulated at 24 hours postinjection.
CC {ECO:0000269|PubMed:18798009}.
CC -!- MISCELLANEOUS: Lysozyme C is capable of both hydrolysis and
CC transglycosylation; it shows also a slight esterase activity. It acts
CC rapidly on both peptide-substituted and unsubstituted peptidoglycan,
CC and slowly on chitin oligosaccharides. {ECO:0000250|UniProtKB:P85345}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 22 family. {ECO:0000255,
CC ECO:0000255|PROSITE-ProRule:PRU00680, ECO:0000255|RuleBase:RU004440,
CC ECO:0000305}.
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DR EMBL; EU591712; ACD76101.1; -; mRNA.
DR AlphaFoldDB; C1IIX1; -.
DR SMR; C1IIX1; -.
DR CAZy; GH22; Glycoside Hydrolase Family 22.
DR PRIDE; C1IIX1; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0003796; F:lysozyme activity; ISS:UniProtKB.
DR GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:UniProtKB.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
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; IPR023346; Lysozyme-like_dom_sf.
DR PANTHER; PTHR11407; PTHR11407; 1.
DR Pfam; PF00062; Lys; 1.
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 2: Evidence at transcript level;
KW Antimicrobial; Bacteriolytic enzyme; Disulfide bond; Glycosidase;
KW Hydrolase; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..158
FT /note="Lysozyme C"
FT /evidence="ECO:0000255"
FT /id="PRO_5002909118"
FT DOMAIN 19..150
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 68
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT DISULFID 24..147
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT DISULFID 46..135
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT DISULFID 80..93
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
FT DISULFID 89..107
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00680"
SQ SEQUENCE 158 AA; 17999 MW; E599F6DC59182128 CRC64;
MRVLPLALLV GLLAVSDAKV LGKCEFARLL ETRYNLSRND IKNWVCIAEF ESSFNTAATN
RNRNRSTDYG IFQINNKYWC GSDYGKNVCG IPCSDLMSDD ITAALRCAET VRRATERYRG
RGKGYTAWVA YNSKCKKRDL DQYMAECWSR GSNSIFPF
