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Protein

Lysozyme

Gene
N/A
Organism
Meretrix lusoria (Hard clam) (Common Orient clam)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Has bacteriolytic activity against Gram-positive bacteria M.luteus. Also has chitinase activity.1 Publication

Miscellaneous

Unlike Ruditapes philippinarum lysozyme, catalytic activity is not affected by variation in salt concentrations.1 Publication

Catalytic activityi

Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins.1 Publication

pH dependencei

Optimum pH is 6.5 at 37 degrees Celsius for bacteriolytic activity. Optimum pH is 3 at 40 degrees Celsius for chitinase activity.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei18Proton donorBy similarity1
Active sitei29NucleophileBy similarity1
Binding sitei72SubstrateCombined sources1 Publication1 Publication1
Binding sitei93SubstrateCombined sources1 Publication1 Publication1
Binding sitei102SubstrateCombined sources1 Publication1 Publication1

GO - Molecular functioni

  • chitinase activity Source: UniProtKB
  • lysozyme activity Source: UniProtKB

GO - Biological processi

  • catabolism by organism of cell wall peptidoglycan in other organism Source: UniProtKB
  • cytolysis Source: UniProtKB-KW
  • defense response to bacterium Source: UniProtKB

Keywordsi

Molecular functionAntibiotic, Antimicrobial, Bacteriolytic enzyme, Glycosidase, Hydrolase

Protein family/group databases

CAZyiGH22. Glycoside Hydrolase Family 22.

Names & Taxonomyi

Protein namesi
Recommended name:
Lysozyme1 Publication (EC:3.2.1.171 Publication)
Alternative name(s):
1,4-beta-N-acetylmuramidaseBy similarity
Invertebrate-type lysozymeCurated
OrganismiMeretrix lusoria (Hard clam) (Common Orient clam)
Taxonomic identifieri74491 [NCBI]
Taxonomic lineageiEukaryotaMetazoaLophotrochozoaMolluscaBivalviaHeteroconchiaEuheterodontaVeneroidaVeneroideaVeneridaeMeretrix

Subcellular locationi

  • Secreted By similarity

GO - Cellular componenti

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003895301 – 122LysozymeAdd BLAST122

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi10 ↔ 86Combined sources2 Publications
Disulfide bondi13 ↔ 118Combined sources2 Publications
Disulfide bondi15 ↔ 21Combined sources2 Publications
Disulfide bondi26 ↔ 35Combined sources2 Publications
Disulfide bondi48 ↔ 68Combined sources2 Publications
Disulfide bondi58 ↔ 64Combined sources2 Publications
Disulfide bondi82 ↔ 100Combined sources2 Publications

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Monomer.1 Publication

Structurei

Secondary structure

1122
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 6Combined sources3
Helixi8 – 19Combined sources12
Beta strandi20 – 22Combined sources3
Beta strandi29 – 32Combined sources4
Turni36 – 39Combined sources4
Helixi42 – 47Combined sources6
Beta strandi52 – 54Combined sources3
Helixi55 – 59Combined sources5
Helixi62 – 76Combined sources15
Helixi78 – 80Combined sources3
Helixi86 – 95Combined sources10
Helixi99 – 101Combined sources3
Helixi103 – 105Combined sources3
Helixi106 – 112Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3AB6X-ray1.78A1-122[»]
3AYQX-ray1.77A1-122[»]
4PJ2X-ray1.24C/D1-122[»]
ProteinModelPortaliP86383.
SMRiP86383.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni41 – 47Substrate bindingCombined sources1 Publication1 Publication7
Regioni93 – 95Substrate bindingBy similarity3

Sequence similaritiesi

Belongs to the lysozyme type I family.Sequence analysis

Family and domain databases

InterProiView protein in InterPro
IPR008597. Destabilase.
IPR023346. Lysozyme-like_dom.
PANTHERiPTHR11195. PTHR11195. 1 hit.
PfamiView protein in Pfam
PF05497. Destabilase. 1 hit.
SUPFAMiSSF53955. SSF53955. 1 hit.

Sequencei

Sequence statusi: Complete.

P86383-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
FAGGIVSQRC LSCICKMESG CRNVGCKMDM GSLSCGYFQI KEAYWIDCGR
60 70 80 90 100
PGSSWKSCAA SSYCASLCVQ NYMKRYAKWA GCPLRCEGFA REHNGGPRGC
110 120
KKGSTIGYWN RLQKISGCHG VQ
Length:122
Mass (Da):13,377
Last modified:November 24, 2009 - v1
Checksum:i92366099E8AD7881
GO

Mass spectrometryi

Molecular mass is 13376 Da from positions 1 - 122. Determined by MALDI. 1 Publication

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti5I → T in isozyme B. 1 Publication1

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.

Entry informationi

Entry nameiLYS_MERLU
AccessioniPrimary (citable) accession number: P86383
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 24, 2009
Last sequence update: November 24, 2009
Last modified: June 7, 2017
This is version 22 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families