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Protein

Lysozyme

Gene

lysoz

Organism
Ostrea edulis (Native oyster) (European flat oyster)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Has bacteriolytic activity (By similarity). May play a role in digestion and in the host defense mechanisms against invading microbes (PubMed:16996284).1 PublicationBy similarity

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.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei33Proton donorBy similarity1
Active sitei45NucleophileBy similarity1
Binding sitei88SubstrateBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionAntibiotic, Antimicrobial, Bacteriolytic enzyme, Glycosidase, Hydrolase

Protein family/group databases

CAZyiGH22. Glycoside Hydrolase Family 22.

Names & Taxonomyi

Protein namesi
Recommended name:
Lysozyme (EC:3.2.1.17By similarity)
Alternative name(s):
1,4-beta-N-acetylmuramidase
Invertebrate-type lysozymeCurated
Gene namesi
Name:lysoz
OrganismiOstrea edulis (Native oyster) (European flat oyster)
Taxonomic identifieri37623 [NCBI]
Taxonomic lineageiEukaryotaMetazoaLophotrochozoaMolluscaBivalviaPteriomorphiaOstreoidaOstreoideaOstreidaeOstrea

Subcellular locationi

  • Secreted By similarity

GO - Cellular componenti

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 20Sequence analysisAdd BLAST20
ChainiPRO_000028051221 – 137LysozymeAdd BLAST117

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi25 ↔ 102By similarity
Disulfide bondi28 ↔ 133By similarity
Disulfide bondi30 ↔ 37By similarity
Disulfide bondi42 ↔ 51By similarity
Disulfide bondi64 ↔ 84By similarity
Disulfide bondi74 ↔ 80By similarity
Disulfide bondi98 ↔ 116By similarity

Keywords - PTMi

Disulfide bond

Structurei

3D structure databases

ProteinModelPortaliQ6L6Q5.
SMRiQ6L6Q5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni57 – 63Substrate bindingBy similarity7
Regioni109 – 111Substrate bindingBy similarity3

Sequence similaritiesi

Belongs to the lysozyme type I family.Curated

Keywords - Domaini

Signal

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.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q6L6Q5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSAVLVLALV LLSLTCVTDA ISDACLTCIC KQESYGCTQI GCRMDGRSLS
60 70 80 90 100
CGYFQIKKSY WIDCGRLGSS WEACADDYNC AVRCVRAYMK KYIGKSGCTA
110 120 130
NCKNYARLHN GGPKGCTKPS TLTYWNAVKN QGCSINS
Length:137
Mass (Da):14,918
Last modified:July 5, 2004 - v1
Checksum:i5E267529DE695722
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB179776 mRNA. Translation: BAD19060.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB179776 mRNA. Translation: BAD19060.1.

3D structure databases

ProteinModelPortaliQ6L6Q5.
SMRiQ6L6Q5.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH22. Glycoside Hydrolase Family 22.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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.
ProtoNetiSearch...

Entry informationi

Entry nameiLYS_OSTED
AccessioniPrimary (citable) accession number: Q6L6Q5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: July 5, 2004
Last modified: June 7, 2017
This is version 39 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

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.