{PDOC51909}
{PS51909; LYSOZYME_I}
{BEGIN}
*************************************************
* Invertebrate (I)-type lysozyme domain profile *
*************************************************

Lysozyme (EC  3.2.1.17) is an ubiquitous enzyme and is widely distributed in a
range of  phylogenetically  diverse  organisms  from  bacteriophage to humans.
Lysozyme is mainly involved in the innate immune system and protection of host
against microbial  infection. The mechanism of lysozyme in killing bacteria is
by hydrolyzing  the beta-1,4-glycosidic linkages between N-acetyl muramic acid
(NAM) and  N-acetyl  glucosamine (NAG) of peptidoglycan (PG), which is a layer
in the  bacterial  cell  wall.  Based  on differences in amino acid sequences,
catalytic characteristic,  and original sources, lysozymes are classified into
chicken (C)-type   (see   <PDOC00119>),   goose   (G)-type,   virus  (V)-type,
lambda (L)-type,  chalaropsis  (Ch)-type (see <PDOC00737>), plant (P)-type and
invertebrate (I)-type.    I-type    lysozymes    have   been   identified   in
phylogenetically diverse  organisms,  including  mollusca, nematoda, annelida,
arthropoda and  echinodermata.  I-type  lysozymes  play  an  important role in
immunity and  digestion in invertebrates and are usually regarded as the first
barrier against  pathogens.  The  I-type lysozyme has multiple activities. For
its muramidase  activity,  it  is identified as lysozyme; for its isopeptidase
activity, it  is  named destabilase; chitinase and non-enzymatic antibacterial
activities are  also  manifested  [1,2,3,4,5].  They  belong  to  the glycosyl
hydrolase 22 (GH22) family [E1].

The I-type lysozyme domain is characterized by six alpha-helices and one beta-
sheet (see <PDB:2DQA>). It contains 14 cysteines that all form disulfide bonds
(C1-C12, C2-C14, C3-C4, C5-C6, C7-C10, C8-C9, C11-C13). The catalytic residues
are a  glutamate  in  the  alpha1-helix  and  an aspartate in the beta1-strand
[6,7].

The profile we developed covers the entire I-type lysozyme domain.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: October 2019 / First entry.

[ 1] Bachali S., Bailly X., Jolles J., Jolles P., Deutsch J.S.
     "The lysozyme of the starfish Asterias rubens. A paradygmatic type i
     lysozyme."
     Eur. J. Biochem. 271:237-242(2004).
     PubMed=14717691; DOI=10.1046/j.1432-1033.2003.03915.x
[ 2] Schulenburg H., Boehnisch C.
     "Diversification and adaptive sequence evolution of Caenorhabditis
     lysozymes (Nematoda: Rhabditidae)."
     BMC Evol. Biol. 8:114-114(2008).
     PubMed=18423043; DOI=10.1186/1471-2148-8-114
     PubMed=29807121; DOI=10.1016/j.fsi.2018.05.037
[ 3] Zhang H.-W., Sun C., Sun S.-S., Zhao X.-F., Wang J.-X.
     "Functional analysis of two invertebrate-type lysozymes from red swamp
     crayfish, Procambarus clarkii."
     Fish. Shellfish. Immunol. 29:1066-1072(2010).
     PubMed=20816803; DOI=10.1016/j.fsi.2010.08.023
[ 4] Ren Q., Qi Y.-L., Hui K.-M., Zhang Z., Zhang C.-Y., Wang W.
     "Four invertebrate-type lysozyme genes from triangle-shell pearl
     mussel (Hyriopsis cumingii)."
     Fish. Shellfish. Immunol. 33:909-915(2012).
     PubMed=22884462; DOI=10.1016/j.fsi.2012.07.019
[ 5] Chen F., Wei Z., Zhao X., Shao Y., Zhang W.
     "Molecular characteristics, expression, and antimicrobial activities
     of i-type lysozyme from the razor clam Sinonovacula constricta."
     Fish. Shellfish. Immunol. 79:321-326(2018).
[ 6] Goto T., Abe Y., Kakuta Y., Takeshita K., Imoto T., Ueda T.
     "Crystal structure of Tapes japonica Lysozyme with substrate analogue:
     structural  basis of the catalytic mechanism and manifestation of its
     chitinase activity accompanied by quaternary structural change."
     J. Biol. Chem. 282:27459-27467(2007).
     PubMed=17631496; DOI=10.1074/jbc.M704555200
[ 7] Kuwano Y., Yoneda K., Kawaguchi Y., Araki T.
     "The tertiary structure of an i-type lysozyme isolated from the common
     orient clam (Meretrix lusoria)."
     Acta Crystallogr. Sect. F. Struct. Biol. Cryst. Commun. 69:1202-1206(2013).
     PubMed=24192349; DOI=10.1107/S1744309113028170
[E1] http://www.cazy.org/GH22.html

--------------------------------------------------------------------------------
PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and
distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives
(CC BY-NC-ND 4.0) License, see https://prosite.expasy.org/prosite_license.html
--------------------------------------------------------------------------------

{END}